OBSCN_HUMAN
ID OBSCN_HUMAN Reviewed; 7968 AA.
AC Q5VST9; Q2A664; Q5T7G8; Q5T7G9; Q5VSU2; Q86YC7; Q8NHN0; Q8NHN1; Q8NHN2;
AC Q8NHN3; Q8NHN4; Q8NHN5; Q8NHN6; Q8NHN7; Q8NHN8; Q8NHN9; Q96AA2; Q9HCD3;
AC Q9HCL6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Obscurin;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:A2AAJ9};
DE AltName: Full=Obscurin-RhoGEF;
DE AltName: Full=Obscurin-myosin light chain kinase;
DE Short=Obscurin-MLCK;
GN Name=OBSCN; Synonyms=KIAA1556, KIAA1639;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), VARIANTS THR-51;
RP ARG-502; ASP-1508 THR-3300; ARG-4381; ARG-4450 AND HIS-4534, FUNCTION, AND
RP INTERACTION WITH TTN AND CALMODULIN.
RC TISSUE=Heart;
RX PubMed=11448995; DOI=10.1083/jcb.200102110;
RA Young P.W., Ehler E., Gautel M.;
RT "Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor
RT protein involved in sarcomere assembly.";
RL J. Cell Biol. 154:123-136(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2734-4428 (ISOFORM 5), AND NUCLEOTIDE
RP SEQUENCE [MRNA] OF 6009-7968 (ISOFORM 1).
RC TISSUE=Cardiac myocyte;
RX PubMed=16625316; DOI=10.1007/s10974-005-9025-6;
RA Fukuzawa A., Idowu S., Gautel M.;
RT "Complete human gene structure of obscurin: implications for isoform
RT generation by differential splicing.";
RL J. Muscle Res. Cell Motil. 26:427-434(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5386-7968 (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2726-7968 (ISOFORM 4), AND VARIANT VAL-7172.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP INTERACTION WITH TTN.
RX PubMed=11717165; DOI=10.1161/hh2301.100981;
RA Bang M.-L., Centner T., Fornoff F., Geach A.J., Gotthardt M., McNabb M.,
RA Witt C.C., Labeit D., Gregorio C.C., Granzier H., Labeit S.;
RT "The complete gene sequence of titin, expression of an unusual ~700 kDa
RT titin isoform and its interaction with obscurin identify a novel Z-line to
RT I-band linking system.";
RL Circ. Res. 89:1065-1072(2001).
RN [6]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11814696; DOI=10.1016/s0378-1119(01)00795-8;
RA Russell M.W., Raeker M.O., Korytkowski K.A., Sonneman K.J.;
RT "Identification, tissue expression and chromosomal localization of human
RT obscurin-MLCK, a member of the titin and Dbl families of myosin light chain
RT kinases.";
RL Gene 282:237-246(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ANK1.
RX PubMed=12527750; DOI=10.1083/jcb.200208109;
RA Bagnato P., Barone V., Giacomello E., Rossi D., Sorrentino V.;
RT "Binding of an ankyrin-1 isoform to obscurin suggests a molecular link
RT between the sarcoplasmic reticulum and myofibrils in striated muscles.";
RL J. Cell Biol. 160:245-253(2003).
RN [8]
RP CHROMOSOMAL TRANSLOCATION WITH PTHB1.
RX PubMed=12618763; DOI=10.1038/sj.onc.1206332;
RA Vernon E.G., Malik K., Reynolds P., Powlesland R., Dallosso A.R.,
RA Jackson S., Henthorn K., Green E.D., Brown K.W.;
RT "The parathyroid hormone-responsive B1 gene is interrupted by a
RT t(1;7)(q42;p15) breakpoint associated with Wilms' tumour.";
RL Oncogene 22:1371-1380(2003).
RN [9]
RP FUNCTION.
RX PubMed=16205939; DOI=10.1007/s00418-005-0069-x;
RA Borisov A.B., Sutter S.B., Kontrogianni-Konstantopoulos A., Bloch R.J.,
RA Westfall M.V., Russell M.W.;
RT "Essential role of obscurin in cardiac myofibrillogenesis and hypertrophic
RT response: evidence from small interfering RNA-mediated gene silencing.";
RL Histochem. Cell Biol. 125:227-238(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6831 AND SER-7244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHATIDYLINOSITOL-PHOSPHATE-BINDING, AND MUTAGENESIS OF ARG-5975 AND
RP ARG-5980.
RX PubMed=28826662; DOI=10.1016/j.yjmcc.2017.08.004;
RA Ackermann M.A., King B., Lieberman N.A.P., Bobbili P.J., Rudloff M.,
RA Berndsen C.E., Wright N.T., Hecker P.A., Kontrogianni-Konstantopoulos A.;
RT "Novel obscurins mediate cardiomyocyte adhesion and size via the
RT PI3K/AKT/mTOR signaling pathway.";
RL J. Mol. Cell. Cardiol. 111:27-39(2017).
RN [12]
RP STRUCTURE BY NMR OF 2826-3806.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Ig domains of human obscurin.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [13]
RP STRUCTURE BY NMR OF 5601-5668.
RA Pfuhl M., Gautel M.;
RT "Solution structure of the SH3 domain of obscurin.";
RL Submitted (APR-2005) to the PDB data bank.
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-1136; HIS-1792; MET-1930; LYS-2090;
RP PHE-2314; GLN-3983; HIS-4558; GLN-4810 AND THR-5071.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-502; SER-804; ARG-1027; SER-1086;
RP THR-1090; THR-1091; PRO-1101; ARG-1121; VAL-1133; VAL-1136; GLN-1156;
RP HIS-1248; VAL-1532; MET-1566; THR-1601; VAL-3389; GLU-3426; GLY-3834;
RP SER-4823; GLN-5598 AND GLN-6473.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [16]
RP VARIANT ARG-4492.
RX PubMed=25173926; DOI=10.1161/circgenetics.113.000486;
RA Girolami F., Iascone M., Tomberli B., Bardi S., Benelli M., Marseglia G.,
RA Pescucci C., Pezzoli L., Sana M.E., Basso C., Marziliano N., Merlini P.A.,
RA Fornaro A., Cecchi F., Torricelli F., Olivotto I.;
RT "Novel alpha-actinin 2 variant associated with familial hypertrophic
RT cardiomyopathy and juvenile atrial arrhythmias: a massively parallel
RT sequencing study.";
RL Circ. Cardiovasc. Genet. 7:741-750(2014).
CC -!- FUNCTION: Structural component of striated muscles which plays a role
CC in myofibrillogenesis. Probably involved in the assembly of myosin into
CC sarcomeric A bands in striated muscle (PubMed:11448995,
CC PubMed:16205939). Has serine/threonine protein kinase activity and
CC phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase
CC subunit ATP1B1 (By similarity). Binds (via the PH domain) strongly to
CC phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser
CC extent to phosphatidylinositol 3-phosphate (PtdIns(3)P),
CC phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-
CC phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3) (PubMed:28826662). {ECO:0000250|UniProtKB:A2AAJ9,
CC ECO:0000269|PubMed:11448995, ECO:0000269|PubMed:16205939,
CC ECO:0000269|PubMed:28826662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:A2AAJ9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A2AAJ9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A2AAJ9};
CC -!- SUBUNIT: Interacts (via protein kinase domain 2) with CDH2 and (via
CC protein kinase domain 1) with ATP1B1 (By similarity). Isoform 3
CC interacts with TTN/titin and calmodulin (PubMed:11448995,
CC PubMed:11717165). Isoform 3 interacts with ANK1 isoform Mu17/ank1.5
CC (PubMed:12527750). {ECO:0000250|UniProtKB:A2AAJ9,
CC ECO:0000269|PubMed:11448995, ECO:0000269|PubMed:11717165,
CC ECO:0000269|PubMed:12527750}.
CC -!- INTERACTION:
CC Q5VST9; Q8WZ42: TTN; NbExp=15; IntAct=EBI-941850, EBI-681210;
CC Q5VST9-3; P16157: ANK1; NbExp=3; IntAct=EBI-941921, EBI-941686;
CC Q5VST9-3; P16157-17: ANK1; NbExp=8; IntAct=EBI-941921, EBI-941819;
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, myofibril, sarcomere, M
CC line {ECO:0000269|PubMed:12527750}. Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000269|PubMed:12527750}. Note=In differentiating skeletal
CC muscle cells, isoform 3 primarily localizes to the sarcomeric M-line
CC and less frequently to the Z-disk (PubMed:12527750). Isoform 3
CC colocalizes with ANK1 isoform Mu17/ank1.5 at the M-line in
CC differentiated skeletal muscle cells (PubMed:12527750).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250|UniProtKB:A2AAJ9}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:A2AAJ9}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:A2AAJ9}. Nucleus {ECO:0000250|UniProtKB:A2AAJ9}.
CC Note=Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to
CC intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M
CC line and Z line in cardiac muscles. {ECO:0000250|UniProtKB:A2AAJ9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=B, obscurin-MLCK giant kinase;
CC IsoId=Q5VST9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VST9-2; Sequence=VSP_018436;
CC Name=3; Synonyms=unc-89-like;
CC IsoId=Q5VST9-3; Sequence=VSP_018437, VSP_018438;
CC Name=4;
CC IsoId=Q5VST9-5; Sequence=VSP_020086, VSP_020087;
CC Name=5;
CC IsoId=Q5VST9-6; Sequence=VSP_026970;
CC -!- PTM: Autophosphorylated by protein kinase domains 1 and 2.
CC {ECO:0000250|UniProtKB:A2AAJ9}.
CC -!- DISEASE: Note=A chromosomal aberration involving OBSCN has been found
CC in Wilms tumor. Translocation t(1;7)(q42;p15) with PTHB1.
CC {ECO:0000269|PubMed:12618763}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks the kinase domain. Initially
CC described as obscurin. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Initially the name obscurin was used to describe isoform 3
CC which lacks the kinase domains. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC85746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC85749.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC85750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 4]:
CC Sequence=BAB13382.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ002535; CAC44768.1; -; mRNA.
DR EMBL; AJ314896; CAC85745.1; -; Genomic_DNA.
DR EMBL; AJ314898; CAC85746.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ314900; CAC85747.1; -; Genomic_DNA.
DR EMBL; AJ314901; CAC85749.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ314903; CAC85750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ314904; CAC85751.1; -; Genomic_DNA.
DR EMBL; AJ314905; CAC85752.1; -; Genomic_DNA.
DR EMBL; AJ314906; CAC85753.1; -; Genomic_DNA.
DR EMBL; AJ314907; CAC85754.1; -; Genomic_DNA.
DR EMBL; AJ314908; CAC85755.1; -; Genomic_DNA.
DR EMBL; AL353593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL670729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AM231061; CAJ76912.1; -; mRNA.
DR EMBL; AB046776; BAB13382.1; ALT_FRAME; mRNA.
DR EMBL; AB046859; BAB13465.2; -; mRNA.
DR CCDS; CCDS1570.2; -. [Q5VST9-3]
DR CCDS; CCDS58065.1; -. [Q5VST9-1]
DR RefSeq; NP_001092093.2; NM_001098623.2. [Q5VST9-1]
DR RefSeq; NP_443075.3; NM_052843.3. [Q5VST9-3]
DR PDB; 1V1C; NMR; -; A=5601-5668.
DR PDB; 2CR6; NMR; -; A=2999-3100.
DR PDB; 2DKU; NMR; -; A=2915-3004.
DR PDB; 2DM7; NMR; -; A=3551-3631.
DR PDB; 2E7B; NMR; -; A=3184-3273.
DR PDB; 2EDF; NMR; -; A=2826-2915.
DR PDB; 2EDH; NMR; -; A=3614-3713.
DR PDB; 2EDL; NMR; -; A=3801-3887.
DR PDB; 2EDQ; NMR; -; A=3713-3806.
DR PDB; 2EDR; NMR; -; A=3361-3449.
DR PDB; 2EDT; NMR; -; A=3449-3537.
DR PDB; 2EDW; NMR; -; A=3537-3630.
DR PDB; 2ENY; NMR; -; A=2735-2825.
DR PDB; 2EO1; NMR; -; A=1623-1712.
DR PDB; 2GQH; NMR; -; A=3450-3543.
DR PDB; 2MWC; NMR; -; A=4337-4429.
DR PDB; 2N56; NMR; -; A=4430-4524.
DR PDB; 2YZ8; X-ray; 2.00 A; A=3184-3273.
DR PDB; 4C4K; X-ray; 1.95 A; O=9-103.
DR PDB; 4RSV; X-ray; 2.41 A; A=4337-4429.
DR PDB; 4UOW; X-ray; 3.30 A; 0/2/4/6/8/A/C/E/G/I/K/M/O/Q/S/U/W/Y=110-203.
DR PDB; 5TZM; X-ray; 1.18 A; A=4431-4521.
DR PDB; 6MG9; NMR; -; A=4247-4338.
DR PDBsum; 1V1C; -.
DR PDBsum; 2CR6; -.
DR PDBsum; 2DKU; -.
DR PDBsum; 2DM7; -.
DR PDBsum; 2E7B; -.
DR PDBsum; 2EDF; -.
DR PDBsum; 2EDH; -.
DR PDBsum; 2EDL; -.
DR PDBsum; 2EDQ; -.
DR PDBsum; 2EDR; -.
DR PDBsum; 2EDT; -.
DR PDBsum; 2EDW; -.
DR PDBsum; 2ENY; -.
DR PDBsum; 2EO1; -.
DR PDBsum; 2GQH; -.
DR PDBsum; 2MWC; -.
DR PDBsum; 2N56; -.
DR PDBsum; 2YZ8; -.
DR PDBsum; 4C4K; -.
DR PDBsum; 4RSV; -.
DR PDBsum; 4UOW; -.
DR PDBsum; 5TZM; -.
DR PDBsum; 6MG9; -.
DR SMR; Q5VST9; -.
DR BioGRID; 123847; 50.
DR DIP; DIP-35727N; -.
DR IntAct; Q5VST9; 41.
DR MINT; Q5VST9; -.
DR GlyGen; Q5VST9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VST9; -.
DR MetOSite; Q5VST9; -.
DR PhosphoSitePlus; Q5VST9; -.
DR BioMuta; OBSCN; -.
DR DMDM; 215274225; -.
DR EPD; Q5VST9; -.
DR jPOST; Q5VST9; -.
DR MassIVE; Q5VST9; -.
DR MaxQB; Q5VST9; -.
DR PeptideAtlas; Q5VST9; -.
DR PRIDE; Q5VST9; -.
DR ProteomicsDB; 65280; -. [Q5VST9-1]
DR ProteomicsDB; 65281; -. [Q5VST9-2]
DR ProteomicsDB; 65282; -. [Q5VST9-3]
DR ProteomicsDB; 65283; -. [Q5VST9-5]
DR ProteomicsDB; 65284; -. [Q5VST9-6]
DR Antibodypedia; 11615; 42 antibodies from 15 providers.
DR DNASU; 84033; -.
DR Ensembl; ENST00000284548.16; ENSP00000284548.11; ENSG00000154358.23. [Q5VST9-3]
DR Ensembl; ENST00000422127.5; ENSP00000409493.1; ENSG00000154358.23. [Q5VST9-1]
DR Ensembl; ENST00000636476.2; ENSP00000489816.2; ENSG00000154358.23. [Q5VST9-2]
DR Ensembl; ENST00000662438.1; ENSP00000499633.1; ENSG00000154358.23. [Q5VST9-6]
DR GeneID; 84033; -.
DR KEGG; hsa:84033; -.
DR UCSC; uc001hsn.4; human. [Q5VST9-1]
DR CTD; 84033; -.
DR DisGeNET; 84033; -.
DR GeneCards; OBSCN; -.
DR HGNC; HGNC:15719; OBSCN.
DR HPA; ENSG00000154358; Tissue enriched (skeletal).
DR MIM; 608616; gene.
DR neXtProt; NX_Q5VST9; -.
DR OpenTargets; ENSG00000154358; -.
DR PharmGKB; PA31888; -.
DR VEuPathDB; HostDB:ENSG00000154358; -.
DR GeneTree; ENSGT00940000154756; -.
DR HOGENOM; CLU_000031_0_0_1; -.
DR InParanoid; Q5VST9; -.
DR PhylomeDB; Q5VST9; -.
DR PathwayCommons; Q5VST9; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; Q5VST9; -.
DR SIGNOR; Q5VST9; -.
DR BioGRID-ORCS; 84033; 13 hits in 1109 CRISPR screens.
DR ChiTaRS; OBSCN; human.
DR EvolutionaryTrace; Q5VST9; -.
DR GeneWiki; OBSCN; -.
DR GeneWiki; Obscurin; -.
DR GenomeRNAi; 84033; -.
DR Pharos; Q5VST9; Tbio.
DR PRO; PR:Q5VST9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VST9; protein.
DR Bgee; ENSG00000154358; Expressed in hindlimb stylopod muscle and 118 other tissues.
DR ExpressionAtlas; Q5VST9; baseline and differential.
DR Genevisible; Q5VST9; HS.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031430; C:M band; ISS:BHF-UCL.
DR GO; GO:0030016; C:myofibril; NAS:BHF-UCL.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008307; F:structural constituent of muscle; NAS:BHF-UCL.
DR GO; GO:0031432; F:titin binding; IPI:BHF-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0036309; P:protein localization to M-band; ISS:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0045214; P:sarcomere organization; TAS:BHF-UCL.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd12025; SH3_Obscurin_like; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.10; -; 61.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR020682; Obscurin.
DR InterPro; IPR035526; Obscurin_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR47633:SF2; PTHR47633:SF2; 6.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 51.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 56.
DR SMART; SM00408; IGc2; 49.
DR SMART; SM00406; IGv; 14.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48726; SSF48726; 57.
DR SUPFAM; SSF49265; SSF49265; 3.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 47.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Chromosomal rearrangement; Cytoplasm; Developmental protein;
KW Differentiation; Disulfide bond; Immunoglobulin domain; Kinase;
KW Lipid-binding; Magnesium; Membrane; Metal-binding; Muscle protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..7968
FT /note="Obscurin"
FT /id="PRO_0000235298"
FT DOMAIN 10..100
FT /note="Ig-like 1"
FT DOMAIN 110..202
FT /note="Ig-like 2"
FT DOMAIN 236..322
FT /note="Ig-like 3"
FT DOMAIN 331..414
FT /note="Ig-like 4"
FT DOMAIN 420..508
FT /note="Ig-like 5"
FT DOMAIN 515..612
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 619..698
FT /note="Ig-like 6"
FT DOMAIN 701..790
FT /note="Ig-like 7"
FT DOMAIN 798..884
FT /note="Ig-like 8"
FT DOMAIN 886..977
FT /note="Ig-like 9"
FT DOMAIN 978..1066
FT /note="Ig-like 10"
FT DOMAIN 1070..1161
FT /note="Ig-like 11"
FT DOMAIN 1162..1252
FT /note="Ig-like 12"
FT DOMAIN 1254..1345
FT /note="Ig-like 13"
FT DOMAIN 1346..1432
FT /note="Ig-like 14"
FT DOMAIN 1438..1524
FT /note="Ig-like 15"
FT DOMAIN 1530..1621
FT /note="Ig-like 16"
FT DOMAIN 1622..1719
FT /note="Ig-like 17"
FT DOMAIN 1731..1808
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1809..1894
FT /note="Ig-like 18"
FT DOMAIN 1896..1982
FT /note="Ig-like 19"
FT DOMAIN 1987..2071
FT /note="Ig-like 20"
FT DOMAIN 2077..2162
FT /note="Ig-like 21"
FT DOMAIN 2165..2249
FT /note="Ig-like 22"
FT DOMAIN 2289..2380
FT /note="Ig-like 23"
FT DOMAIN 2468..2559
FT /note="Ig-like 24"
FT DOMAIN 2564..2643
FT /note="Ig-like 25"
FT DOMAIN 2646..2730
FT /note="Ig-like 26"
FT DOMAIN 2736..2823
FT /note="Ig-like 27"
FT DOMAIN 2826..2908
FT /note="Ig-like 28"
FT DOMAIN 2920..2999
FT /note="Ig-like 29"
FT DOMAIN 3003..3092
FT /note="Ig-like 30"
FT DOMAIN 3095..3183
FT /note="Ig-like 31"
FT DOMAIN 3184..3268
FT /note="Ig-like 32"
FT DOMAIN 3273..3356
FT /note="Ig-like 33"
FT DOMAIN 3359..3444
FT /note="Ig-like 34"
FT DOMAIN 3449..3532
FT /note="Ig-like 35"
FT DOMAIN 3537..3620
FT /note="Ig-like 36"
FT DOMAIN 3625..3708
FT /note="Ig-like 37"
FT DOMAIN 3713..3796
FT /note="Ig-like 38"
FT DOMAIN 3801..3884
FT /note="Ig-like 39"
FT DOMAIN 3890..3973
FT /note="Ig-like 40"
FT DOMAIN 3978..4062
FT /note="Ig-like 41"
FT DOMAIN 4068..4160
FT /note="Ig-like 42"
FT DOMAIN 4171..4239
FT /note="Ig-like 43"
FT DOMAIN 4248..4337
FT /note="Ig-like 44"
FT DOMAIN 4340..4427
FT /note="Ig-like 45"
FT DOMAIN 4430..4518
FT /note="Ig-like 46"
FT DOMAIN 4525..4619
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4624..4714
FT /note="Ig-like 47"
FT DOMAIN 4872..4901
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 4898..4989
FT /note="Ig-like 48"
FT DOMAIN 5126..5215
FT /note="Ig-like 49"
FT DOMAIN 5260..5349
FT /note="Ig-like 50"
FT DOMAIN 5371..5467
FT /note="Ig-like 51"
FT DOMAIN 5600..5667
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 5693..5877
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 5895..6004
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 6014..6097
FT /note="Ig-like 52"
FT DOMAIN 6108..6200
FT /note="Ig-like 53"
FT DOMAIN 6357..6445
FT /note="Ig-like 54"
FT DOMAIN 6468..6721
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 7463..7552
FT /note="Ig-like 55"
FT DOMAIN 7557..7649
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 7672..7924
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 228..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4749..4785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4820..4860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5238..5257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5554..5596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6237..6296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6777..6863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6952..7176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7217..7272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4749..4774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5574..5590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6785..6801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7050..7064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7077..7091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7115..7142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7155..7173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 6587
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 7791
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 5975
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000269|PubMed:28826662"
FT BINDING 5980
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57658"
FT /evidence="ECO:0000269|PubMed:28826662"
FT BINDING 6474..6482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 6497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 7678..7686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 7701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 2889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 4015
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 4750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 4754
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 4757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 4788
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 4805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 5563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 5569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 5571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 5573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AAJ9"
FT MOD_RES 6831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 7244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT DISULFID 31..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 259..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 354..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 819..870
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 912..962
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1004..1054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1096..1146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1188..1238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1280..1330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1372..1422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1464..1514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1556..1606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1648..1698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1723..1791
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1830..1880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2187..2237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2311..2361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2490..2540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2668..2718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2848..2898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2937..2987
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3117..3167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3206..3256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3295..3344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3383..3432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3471..3520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3559..3608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3647..3696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3735..3784
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3823..3872
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3911..3961
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4000..4050
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4089..4141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4453..4508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4919..4971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5147..5199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 6035..6087
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 6129..6182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 7484..7536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 3886
FT /note="R -> RALPARFTQDLKTKEASEGATATLQCELSKVAPVEWKKGPETLRDGG
FT RYSLKQDGTRCELQIHDLSVADAGEYSCMCGQERTSATLTVRALPARFTEGLRNEEAME
FT GATATLQCELSKAAPVEWRKGLEALRDGDKYSLRQDGAVCELQIHGLAMADNGVYSCVC
FT GQERTSATLTVRALPARFIEDMRNQKATEGATVTLQCKLRKAAPVEWRKGPNTLKDGDR
FT YSLKQDGTSCELQIRGLVIADAGEYSCICEQERTSATLTVRALPARFIEDVRNHEATEG
FT ATAVLQCELSKAAPVEWRKGSETLRDGDRYSLRQDGTRCELQIRGLAVEDTGEYLCVCG
FT QERTSATLTVRALPARFIDNMTNQEAREGATATLHCELSKVAPVEWRKGPETLRDGDRH
FT SLRQDGTRCELQIRGLSVADAGEYSCVCGQERTSATLTIREATEGATAMLQCELSKVAP
FT VEWRKGPETLRDGDRYNLRQDGTRCELQIHGLSVADTGEYSCVCGQEKTSATLTVK
FT (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_026970"
FT VAR_SEQ 3888..3913
FT /note="PQPVFREPLQSLQAEEGSTATLQCEL -> LPARIHSRSEDQGGLRRGHSYT
FT AV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_020086"
FT VAR_SEQ 3914..7968
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_020087"
FT VAR_SEQ 5753
FT /note="S -> SS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10997877"
FT /id="VSP_018436"
FT VAR_SEQ 6221..6620
FT /note="DTTLERADQEVTSVLKRLLGPKAPGPSTGDLTGPGPCPRGAPALQETGSQPP
FT VTGTSEAPAVPPRVPQPLLHEGPEQEPEAIARAQEWTVPIRMEGAAWPGAGTGELLWDV
FT HSHVVRETTQRTYTYQAIDTHTARPPSMQVTIEDVQAQTGGTAQFEAIIEGDPQPSVTW
FT YKDSVQLVDSTRLSQQQEGTTYSLVLRHVASKDAGVYTCLAQNTGGQVLCKAELLVLGG
FT DNEPDSEKQSHRRKLHSFYEVKEEIGRGVFGFVKRVQHKGNKILCAAKFIPLRSRTRAQ
FT AYRERDILAALSHPLVTGLLDQFETRKTLILILELCSSEELLDRLYRKGVVTEAEVKVY
FT IQQLVEGLHYLHSHGVLHLDIKPSNILMVHPAREDIKICDFGFAQNITPAELQ -> VT
FT EQETKVPKKTVIIEETITTVVKSPRGQRRSPSKSPSRSPSRCSASPLRPGLLAPDLLYL
FT PGAGQPRRPEAEPGQKPVVPTLYVTEAEAHSPALPGLSGPQPKWVEVEETIEVRVKKMG
FT PQGVSPTTEVPRSSSGHLFTLPGATPGGDPNSNNSNNKLLAQEAWAQGTAMVGVREPLV
FT FRVDARGSVDWAASGMGSLEEEGTMEEAGEEEGEDGDAFVTEESQDTHSLGDRDPKILT
FT HNGRMLTLADLEDYVPGEGETFHCGGPGPGAPDDPPCEVSVIQREIGEPTVGQPVLLSV
FT GHALGPRGPLGLFRPEPRGASPPGPQVRSLEGTSFLLREAPARPVGSAPWTQSFCTRIR
FT RSADSGQSSFTTELSTQTVNFGTVGETVTLHICPDRDGDEAAQP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11448995"
FT /id="VSP_018437"
FT VAR_SEQ 6621..7968
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11448995"
FT /id="VSP_018438"
FT VARIANT 51
FT /note="A -> T (in dbSNP:rs1771487)"
FT /evidence="ECO:0000269|PubMed:11448995"
FT /id="VAR_026409"
FT VARIANT 502
FT /note="Q -> R (in dbSNP:rs1771487)"
FT /evidence="ECO:0000269|PubMed:11448995,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_034618"
FT VARIANT 804
FT /note="G -> S (in dbSNP:rs55950009)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042276"
FT VARIANT 908
FT /note="A -> T (in dbSNP:rs1757153)"
FT /id="VAR_047743"
FT VARIANT 1027
FT /note="K -> R (in dbSNP:rs55760713)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042277"
FT VARIANT 1086
FT /note="A -> S (in dbSNP:rs117147433)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042278"
FT VARIANT 1090
FT /note="A -> T (in dbSNP:rs752906025)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042279"
FT VARIANT 1091
FT /note="S -> T (in dbSNP:rs965007403)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042280"
FT VARIANT 1101
FT /note="A -> P (in dbSNP:rs780907202)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042281"
FT VARIANT 1121
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042282"
FT VARIANT 1133
FT /note="L -> V (in dbSNP:rs777214598)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042283"
FT VARIANT 1136
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs950055015)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_035530"
FT VARIANT 1156
FT /note="H -> Q"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042284"
FT VARIANT 1248
FT /note="Q -> H (in dbSNP:rs199523598)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042285"
FT VARIANT 1508
FT /note="V -> D (in dbSNP:rs7532342)"
FT /id="VAR_034619"
FT VARIANT 1532
FT /note="A -> V (in dbSNP:rs453140)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042286"
FT VARIANT 1566
FT /note="T -> M (in dbSNP:rs56217040)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042287"
FT VARIANT 1601
FT /note="A -> T (in dbSNP:rs55706639)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042288"
FT VARIANT 1792
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs750681123)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035531"
FT VARIANT 1930
FT /note="V -> M (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs545316651)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035532"
FT VARIANT 2090
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035533"
FT VARIANT 2106
FT /note="D -> E (in dbSNP:rs1188721)"
FT /id="VAR_047744"
FT VARIANT 2116
FT /note="F -> L (in dbSNP:rs1188722)"
FT /id="VAR_047745"
FT VARIANT 2314
FT /note="S -> F (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035534"
FT VARIANT 2529
FT /note="R -> Q (in dbSNP:rs3795783)"
FT /id="VAR_047746"
FT VARIANT 2720
FT /note="V -> M (in dbSNP:rs1188697)"
FT /id="VAR_047747"
FT VARIANT 2812
FT /note="R -> W (in dbSNP:rs3795785)"
FT /id="VAR_047748"
FT VARIANT 3300
FT /note="A -> T (in dbSNP:rs437129)"
FT /evidence="ECO:0000269|PubMed:11448995"
FT /id="VAR_034620"
FT VARIANT 3372
FT /note="E -> D (in dbSNP:rs3795789)"
FT /id="VAR_047749"
FT VARIANT 3373
FT /note="S -> C (in dbSNP:rs3795790)"
FT /id="VAR_047750"
FT VARIANT 3389
FT /note="A -> V (in dbSNP:rs770177081)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042289"
FT VARIANT 3426
FT /note="D -> E"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042290"
FT VARIANT 3834
FT /note="R -> G"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042291"
FT VARIANT 3983
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs539154039)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035535"
FT VARIANT 4039
FT /note="G -> R (in dbSNP:rs435776)"
FT /id="VAR_047751"
FT VARIANT 4381
FT /note="H -> R (in dbSNP:rs1150912)"
FT /evidence="ECO:0000269|PubMed:11448995"
FT /id="VAR_034621"
FT VARIANT 4450
FT /note="C -> R (in dbSNP:rs1188732)"
FT /evidence="ECO:0000269|PubMed:11448995"
FT /id="VAR_034622"
FT VARIANT 4492
FT /note="L -> R (in dbSNP:rs369570923)"
FT /evidence="ECO:0000269|PubMed:25173926"
FT /id="VAR_074295"
FT VARIANT 4516
FT /note="R -> W (in dbSNP:rs11810627)"
FT /id="VAR_059429"
FT VARIANT 4534
FT /note="R -> H (in dbSNP:rs4653942)"
FT /evidence="ECO:0000269|PubMed:11448995"
FT /id="VAR_026410"
FT VARIANT 4558
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs199865640)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035536"
FT VARIANT 4642
FT /note="S -> C (in dbSNP:rs1188729)"
FT /id="VAR_056102"
FT VARIANT 4662
FT /note="R -> C (in dbSNP:rs3795800)"
FT /id="VAR_056103"
FT VARIANT 4666
FT /note="G -> S (in dbSNP:rs3795801)"
FT /id="VAR_056104"
FT VARIANT 4810
FT /note="R -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs570805670)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035537"
FT VARIANT 4823
FT /note="A -> S"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042292"
FT VARIANT 4962
FT /note="D -> G (in dbSNP:rs373610)"
FT /id="VAR_056105"
FT VARIANT 5071
FT /note="A -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035538"
FT VARIANT 5269
FT /note="L -> V (in dbSNP:rs369909)"
FT /id="VAR_056106"
FT VARIANT 5575
FT /note="R -> H (in dbSNP:rs3795809)"
FT /id="VAR_056107"
FT VARIANT 5598
FT /note="R -> Q (in dbSNP:rs867550675)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042293"
FT VARIANT 5891
FT /note="Q -> E (in dbSNP:rs1188710)"
FT /id="VAR_056108"
FT VARIANT 6473
FT /note="E -> Q"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042294"
FT VARIANT 7172
FT /note="A -> V (in dbSNP:rs500049)"
FT /evidence="ECO:0000269|PubMed:10997877"
FT /id="VAR_056109"
FT MUTAGEN 5975
FT /note="R->A: Reduced binding to phosphatidylinositol 4,5-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:28826662"
FT MUTAGEN 5980
FT /note="R->A: Reduced binding to phosphatidylinositol 3,4-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:28826662"
FT CONFLICT 888
FT /note="V -> A (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="L -> P (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="R -> C (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 899..900
FT /note="KL -> EV (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="A -> V (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="A -> D (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="T -> M (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 937..938
FT /note="CM -> HV (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="T -> V (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 944
FT /note="T -> M (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="A -> V (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="A -> S (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="G -> R (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="L -> V (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="H -> R (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="S -> N (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="T -> A (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1348
FT /note="A -> V (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1355
FT /note="L -> P (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1357
FT /note="H -> R (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1359
FT /note="K -> E (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1360
FT /note="V -> L (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1367
FT /note="I -> S (in Ref. 1; CAC85746/CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394
FT /note="S -> L (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397..1398
FT /note="RM -> HV (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397
FT /note="R -> C (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="V -> A (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="V -> T (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1413
FT /note="C -> G (in Ref. 1; CAC85746/CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1417
FT /note="T -> A (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1428
FT /note="R -> Q (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1432
FT /note="S -> H (in Ref. 1; CAC85746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1445
FT /note="E -> D (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1455
FT /note="Q -> E (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1458
FT /note="A -> T (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1461
FT /note="T -> M (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="H -> R (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1526
FT /note="H -> Q (in Ref. 1; CAC85749)"
FT /evidence="ECO:0000305"
FT CONFLICT 1580..1582
FT /note="VRM -> MRV (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1607
FT /note="K -> E (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1610
FT /note="D -> G (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1633
FT /note="H -> C (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1653..1655
FT /note="AQT -> GQM (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1673..1674
FT /note="RV -> HM (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1677..1679
FT /note="VGC -> SGY (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1692
FT /note="E -> D (in Ref. 1; CAC44768/CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1704
FT /note="Q -> R (in Ref. 1; CAC44768/CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1710
FT /note="Q -> H (in Ref. 1; CAC44768/CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1848
FT /note="L -> P (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 2014
FT /note="P -> A (in Ref. 1; CAC85750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3126
FT /note="V -> M (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 4155
FT /note="T -> TG (in Ref. 3; CAC85752)"
FT /evidence="ECO:0000305"
FT CONFLICT 4489
FT /note="H -> Q (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 4959
FT /note="T -> A (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 5243
FT /note="S -> ST (in Ref. 1; CAC85753)"
FT /evidence="ECO:0000305"
FT CONFLICT 5391
FT /note="S -> F (in Ref. 4; BAB13465)"
FT /evidence="ECO:0000305"
FT CONFLICT 5499..5500
FT /note="LE -> FQ (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 6115
FT /note="R -> L (in Ref. 1; CAC44768)"
FT /evidence="ECO:0000305"
FT CONFLICT 6570
FT /note="Q -> E (in Ref. 3; CAJ76912)"
FT /evidence="ECO:0000305"
FT CONFLICT 6710..6711
FT /note="PS -> SG (in Ref. 3; CAJ76912)"
FT /evidence="ECO:0000305"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4C4K"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:4C4K"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 125..137
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:4UOW"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 191..202
FT /evidence="ECO:0007829|PDB:4UOW"
FT STRAND 1634..1639
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1644..1646
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1653..1655
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1658..1661
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1670..1677
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1680..1685
FT /evidence="ECO:0007829|PDB:2EO1"
FT TURN 1690..1692
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1696..1700
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 1707..1712
FT /evidence="ECO:0007829|PDB:2EO1"
FT STRAND 2745..2750
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2753..2758
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2771..2776
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2784..2788
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2791..2796
FT /evidence="ECO:0007829|PDB:2ENY"
FT TURN 2801..2803
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2807..2811
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2814..2818
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2820..2823
FT /evidence="ECO:0007829|PDB:2ENY"
FT STRAND 2829..2831
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2836..2838
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2844..2846
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2849..2854
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2859..2863
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2869..2877
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2880..2887
FT /evidence="ECO:0007829|PDB:2EDF"
FT TURN 2890..2892
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2894..2899
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2904..2911
FT /evidence="ECO:0007829|PDB:2EDF"
FT STRAND 2925..2928
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 2931..2938
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 2947..2952
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 2957..2966
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 2969..2976
FT /evidence="ECO:0007829|PDB:2DKU"
FT TURN 2979..2981
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 2983..2988
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 2996..3001
FT /evidence="ECO:0007829|PDB:2DKU"
FT STRAND 3006..3009
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3013..3017
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3027..3030
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3037..3042
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3048..3050
FT /evidence="ECO:0007829|PDB:2CR6"
FT TURN 3057..3059
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3063..3065
FT /evidence="ECO:0007829|PDB:2CR6"
FT TURN 3070..3072
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3074..3080
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3087..3092
FT /evidence="ECO:0007829|PDB:2CR6"
FT STRAND 3187..3189
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3194..3197
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3202..3210
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3216..3219
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3227..3235
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3238..3243
FT /evidence="ECO:0007829|PDB:2YZ8"
FT HELIX 3248..3250
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3252..3258
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3261..3270
FT /evidence="ECO:0007829|PDB:2YZ8"
FT STRAND 3371..3374
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3386..3388
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3392..3397
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3402..3405
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3407..3410
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3412..3421
FT /evidence="ECO:0007829|PDB:2EDR"
FT TURN 3424..3426
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3430..3433
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3438..3441
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3443..3446
FT /evidence="ECO:0007829|PDB:2EDR"
FT STRAND 3452..3454
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3459..3462
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3467..3475
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3480..3483
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3490..3509
FT /evidence="ECO:0007829|PDB:2EDT"
FT TURN 3512..3514
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3516..3522
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3525..3534
FT /evidence="ECO:0007829|PDB:2EDT"
FT STRAND 3548..3550
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3555..3564
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3568..3575
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3578..3581
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3583..3587
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3590..3597
FT /evidence="ECO:0007829|PDB:2DM7"
FT TURN 3600..3602
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3604..3610
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3613..3618
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3620..3622
FT /evidence="ECO:0007829|PDB:2DM7"
FT STRAND 3628..3630
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3643..3651
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3656..3663
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3667..3675
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3678..3683
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3692..3698
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3701..3709
FT /evidence="ECO:0007829|PDB:2EDH"
FT STRAND 3716..3718
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3723..3726
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3731..3739
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3744..3751
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3754..3757
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3759..3763
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3766..3773
FT /evidence="ECO:0007829|PDB:2EDQ"
FT TURN 3776..3778
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3780..3788
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3790..3798
FT /evidence="ECO:0007829|PDB:2EDQ"
FT STRAND 3811..3814
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3820..3824
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3826..3828
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3831..3837
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3842..3848
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3852..3861
FT /evidence="ECO:0007829|PDB:2EDL"
FT HELIX 3864..3866
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3870..3874
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3877..3880
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 3883..3886
FT /evidence="ECO:0007829|PDB:2EDL"
FT STRAND 4257..4262
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4267..4272
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4282..4285
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4294..4301
FT /evidence="ECO:0007829|PDB:6MG9"
FT TURN 4302..4304
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4305..4310
FT /evidence="ECO:0007829|PDB:6MG9"
FT TURN 4315..4317
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4319..4324
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4329..4337
FT /evidence="ECO:0007829|PDB:6MG9"
FT STRAND 4342..4344
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4349..4351
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4353..4365
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4369..4375
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4386..4391
FT /evidence="ECO:0007829|PDB:4RSV"
FT HELIX 4392..4394
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4396..4403
FT /evidence="ECO:0007829|PDB:4RSV"
FT HELIX 4406..4408
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4410..4416
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4419..4427
FT /evidence="ECO:0007829|PDB:4RSV"
FT STRAND 4434..4436
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4441..4444
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4449..4457
FT /evidence="ECO:0007829|PDB:5TZM"
FT HELIX 4461..4463
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4464..4468
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4478..4485
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4488..4495
FT /evidence="ECO:0007829|PDB:5TZM"
FT HELIX 4498..4500
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4502..4508
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 4511..4520
FT /evidence="ECO:0007829|PDB:5TZM"
FT STRAND 5604..5609
FT /evidence="ECO:0007829|PDB:1V1C"
FT STRAND 5628..5636
FT /evidence="ECO:0007829|PDB:1V1C"
FT STRAND 5639..5644
FT /evidence="ECO:0007829|PDB:1V1C"
FT STRAND 5654..5657
FT /evidence="ECO:0007829|PDB:1V1C"
FT HELIX 5659..5661
FT /evidence="ECO:0007829|PDB:1V1C"
FT STRAND 5662..5665
FT /evidence="ECO:0007829|PDB:1V1C"
SQ SEQUENCE 7968 AA; 868484 MW; 46550B34565CAC76 CRC64;
MDQPQFSGAP RFLTRPKAFV VSVGKDATLS CQIVGNPTPQ VSWEKDQQPV AAGARFRLAQ
DGDLYRLTIL DLALGDSGQY VCRARNAIGE AFAAVGLQVD AEAACAEQAP HFLLRPTSIR
VREGSEATFR CRVGGSPRPA VSWSKDGRRL GEPDGPRVRV EELGEASALR IRAARPRDGG
TYEVRAENPL GAASAAAALV VDSDAADTAS RPGTSTAALL AHLQRRREAM RAEGAPASPP
STGTRTCTVT EGKHARLSCY VTGEPKPETV WKKDGQLVTE GRRHVVYEDA QENFVLKILF
CKQSDRGLYT CTASNLVGQT YSSVLVVVRE PAVPFKKRLQ DLEVREKESA TFLCEVPQPS
TEAAWFKEET RLWASAKYGI EEEGTERRLT VRNVSADDDA VYICETPEGS RTVAELAVQG
NLLRKLPRKT AVRVGDTAMF CVELAVPVGP VHWLRNQEEV VAGGRVAISA EGTRHTLTIS
QCCLEDVGQV AFMAGDCQTS TQFCVSAPRK PPLQPPVDPV VKARMESSVI LSWSPPPHGE
RPVTIDGYLV EKKKLGTYTW IRCHEAEWVA TPELTVADVA EEGNFQFRVS ALNSFGQSPY
LEFPGTVHLA PKLAVRTPLK AVQAVEGGEV TFSVDLTVAS AGEWFLDGQA LKASSVYEIH
CDRTRHTLTI REVPASLHGA QLKFVANGIE SSIRMEVRAA PGLTANKPPA AAAREVLARL
HEEAQLLAEL SDQAAAVTWL KDGRTLSPGP KYEVQASAGR RVLLVRDVAR DDAGLYECVS
RGGRIAYQLS VQGLARFLHK DMAGSCVDAV AGGPAQFECE TSEAHVHVHW YKDGMELGHS
GERFLQEDVG TRHRLVAATV TRQDEGTYSC RVGEDSVDFR LRVSEPKVVF AKEQLARRKL
QAEAGASATL SCEVAQAQTE VTWYKDGKKL SSSSKVCMEA TGCTRRLVVQ QAGQADAGEY
SCEAGGQRLS FHLDVKEPKV VFAKDQVAHS EVQAEAGASA TLSCEVAQAQ TEVMWYKDGK
KLSSSLKVHV EAKGCRRRLV VQQAGKTDAG DYSCEARGQR VSFRLHITEP KMMFAKEQSV
HNEVQAEAGA SAMLSCEVAQ AQTEVTWYKD GKKLSSSSKV GMEVKGCTRR LVLPQAGKAD
AGEYSCEAGG QRVSFHLHIT EPKGVFAKEQ SVHNEVQAEA GTTAMLSCEV AQPQTEVTWY
KDGKKLSSSS KVRMEVKGCT RRLVVQQVGK ADAGEYSCEA GGQRVSFQLH ITEPKAVFAK
EQLVHNEVRT EAGASATLSC EVAQAQTEVT WYKDGKKLSS SSKVRIEAAG CMRQLVVQQA
GQADAGEYTC EAGGQRLSFH LDVSEPKAVF AKEQLAHRKV QAEAGAIATL SCEVAQAQTE
VTWYKDGKKL SSSSKVRMEA VGCTRRLVVQ QACQADTGEY SCEAGGQRLS FSLDVAEPKV
VFAKEQPVHR EVQAQAGAST TLSCEVAQAQ TEVMWYKDGK KLSFSSKVRM EAVGCTRRLV
VQQAGQAVAG EYSCEAGSQR LSFHLHVAEP KAVFAKEQPA SREVQAEAGT SATLSCEVAQ
AQTEVTWYKD GKKLSSSSKV RMEAVGCTRR LVVQEAGQAD AGEYSCKAGD QRLSFHLHVA
EPKVVFAKEQ PAHREVQAEA GASATLSCEV AQAQTEVTWY KDGKKLSSSS KVRVEAVGCT
RRLVVQQAGQ AEAGEYSCEA GGQQLSFRLQ VAELEPQISE RPCRREPLVV KEHEDIILTA
TLATPSAATV TWLKDGVEIR RSKRHETASQ GDTHTLTVHG AQVLDSAIYS CRVGAEGQDF
PVQVEEVAAK FCRLLEPVCG ELGGTVTLAC ELSPACAEVV WRCGNTQLRV GKRFQMVAEG
PVRSLTVLGL RAEDAGEYVC ESRDDHTSAQ LTVSVPRVVK FMSGLSTVVA EEGGEATFQC
VVSPSDVAVV WFRDGALLQP SEKFAISQSG ASHSLTISDL VLEDAGQITV EAEGASSSAA
LRVREAPVLF KKKLEPQTVE ERSSVTLEVE LTRPWPELRW TRNATALAPG KNVEIHAEGA
RHRLVLHNVG FADRGFFGCE TPDDKTQAKL TVEMRQVRLV RGLQAVEARE QGTATMEVQL
SHADVDGSWT RDGLRFQQGP TCHLAVRGPM HTLTLSGLRP EDSGLMVFKA EGVHTSARLV
VTELPVSFSR PLQDVVTTEK EKVTLECELS RPNVDVRWLK DGVELRAGKT MAIAAQGACR
SLTIYRCEFA DQGVYVCDAH DAQSSASVKV QGRTYTLIYR RVLAEDAGEI QFVAENAESR
AQLRVKELPV TLVRPLRDKI AMEKHRGVLE CQVSRASAQV RWFKGSQELQ PGPKYELVSD
GLYRKLIISD VHAEDEDTYT CDAGDVKTSA QFFVEEQSIT IVRGLQDVTV MEPAPAWFEC
ETSIPSVRPP KWLLGKTVLQ AGGNVGLEQE GTVHRLMLRR TCSTMTGPVH FTVGKSRSSA
RLVVSDIPVV LTRPLEPKTG RELQSVVLSC DFRPAPKAVQ WYKDDTPLSP SEKFKMSLEG
QMAELRILRL MPADAGVYRC QAGSAHSSTE VTVEAREVTV TGPLQDAEAT EEGWASFSCE
LSHEDEEVEW SLNGMPLYND SFHEISHKGR RHTLVLKSIQ RADAGIVRAS SLKVSTSARL
EVRVKPVVFL KALDDLSAEE RGTLALQCEV SDPEAHVVWR KDGVQLGPSD KYDFLHTAGT
RGLVVHDVSP EDAGLYTCHV GSEETRARVR VHDLHVGITK RLKTMEVLEG ESCSFECVLS
HESASDPAMW TVGGKTVGSS SRFQATRQGR KYILVVREAA PSDAGEVVFS VRGLTSKASL
IVRERPAAII KPLEDQWVAP GEDVELRCEL SRAGTPVHWL KDRKAIRKSQ KYDVVCEGTM
AMLVIRGASL KDAGEYTCEV EASKSTASLH VEEKANCFTE ELTNLQVEEK GTAVFTCKTE
HPAATVTWRK GLLELRASGK HQPSQEGLTL RLTISALEKA DSDTYTCDIG QAQSRAQLLV
QGRRVHIIED LEDVDVQEGS SATFRCRISP ANYEPVHWFL DKTPLHANEL NEIDAQPGGY
HVLTLRQLAL KDSGTIYFEA GDQRASAALR VTEKPSVFSR ELTDATITEG EDLTLVCETS
TCDIPVCWTK DGKTLRGSAR CQLSHEGHRA QLLITGATLQ DSGRYKCEAG GACSSSIVRV
HARPVRFQEA LKDLEVLEGG AATLRCVLSS VAAPVKWCYG NNVLRPGDKY SLRQEGAMLE
LVVRNLRPQD SGRYSCSFGD QTTSATLTVT ALPAQFIGKL RNKEATEGAT ATLRCELSKA
APVEWRKGSE TLRDGDRYCL RQDGAMCELQ IRGLAMVDAA EYSCVCGEER TSASLTIRPM
PAHFIGRLRH QESIEGATAT LRCELSKAAP VEWRKGRESL RDGDRHSLRQ DGAVCELQIC
GLAVADAGEY SCVCGEERTS ATLTVKALPA KFTEGLRNEE AVEGATAMLW CELSKVAPVE
WRKGPENLRD GDRYILRQEG TRCELQICGL AMADAGEYLC VCGQERTSAT LTIRALPARF
IEDVKNQEAR EGATAVLQCE LNSAAPVEWR KGSETLRDGD RYSLRQDGTK CELQIRGLAM
ADTGEYSCVC GQERTSAMLT VRALPIKFTE GLRNEEATEG ATAVLRCELS KMAPVEWWKG
HETLRDGDRH SLRQDGARCE LQIRGLVAED AGEYLCMCGK ERTSAMLTVR AMPSKFIEGL
RNEEATEGDT ATLWCELSKA APVEWRKGHE TLRDGDRHSL RQDGSRCELQ IRGLAVVDAG
EYSCVCGQER TSATLTVRAL PARFIEDVKN QEAREGATAV LQCELSKAAP VEWRKGSETL
RGGDRYSLRQ DGTRCELQIH GLSVADTGEY SCVCGQERTS ATLTVRAPQP VFREPLQSLQ
AEEGSTATLQ CELSEPTATV VWSKGGLQLQ ANGRREPRLQ GCTAELVLQD LQREDTGEYT
CTCGSQATSA TLTVTAAPVR FLRELQHQEV DEGGTAHLCC ELSRAGASVE WRKGSLQLFP
CAKYQMVQDG AAAELLVRGV EQEDAGDYTC DTGHTQSMAS LSVRVPRPKF KTRLQSLEQE
TGDIARLCCQ LSDAESGAVV QWLKEGVELH AGPKYEMRSQ GATRELLIHQ LEAKDTGEYA
CVTGGQKTAA SLRVTEPEVT IVRGLVDAEV TADEDVEFSC EVSRAGATGV QWCLQGLPLQ
SNEVTEVAVR DGRIHTLRLK GVTPEDAGTV SFHLGNHASS AQLTVRAPEV TILEPLQDVQ
LSEGQDASFQ CRLSRASGQE ARWALGGVPL QANEMNDITV EQGTLHLLTL HKVTLEDAGT
VSFHVGTCSS EAQLKVTAKN TVVRGLENVE ALEGGEALFE CQLSQPEVAA HTWLLDDEPV
HTSENAEVVF FENGLRHLLL LKNLRPQDSC RVTFLAGDMV TSAFLTVRGW RLEILEPLKN
AAVRAGAQAC FTCTLSEAVP VGEASWYING AAVQPDDSDW TVTADGSHHA LLLRSAQPHH
AGEVTFACRD AVASARLTVL GLPDPPEDAE VVARSSHTVT LSWAAPMSDG GGGLCGYRVE
VKEGATGQWR LCHELVPGPE CVVDGLAPGE TYRFRVAAVG PVGAGEPVHL PQTVRLAEPP
KPVPPQPSAP ESRQVAAGED VSLELEVVAE AGEVIWHKGM ERIQPGGRFE VVSQGRQQML
VIKGFTAEDQ GEYHCGLAQG SICPAAATFQ VALSPASVDE APQPSLPPEA AQEGDLHLLW
EALARKRRMS REPTLDSISE LPEEDGRSQR LPQEAEEVAP DLSEGYSTAD ELARTGDADL
SHTSSDDESR AGTPSLVTYL KKAGRPGTSP LASKVGAPAA PSVKPQQQQE PLAAVRPPLG
DLSTKDLGDP SMDKAAVKIQ AAFKGYKVRK EMKQQEGPMF SHTFGDTEAQ VGDALRLECV
VASKADVRAR WLKDGVELTD GRHHHIDQLG DGTCSLLITG LDRADAGCYT CQVSNKFGQV
THSACVVVSG SESEAESSSG GELDDAFRRA ARRLHRLFRT KSPAEVSDEE LFLSADEGPA
EPEEPADWQT YREDEHFICI RFEALTEARQ AVTRFQEMFA TLGIGVEIKL VEQGPRRVEM
CISKETPAPV VPPEPLPSLL TSDAAPVFLT ELQNQEVQDG YPVSFDCVVT GQPMPSVRWF
KDGKLLEEDD HYMINEDQQG GHQLIITAVV PADMGVYRCL AENSMGVSST KAELRVDLTS
TDYDTAADAT ESSSYFSAQG YLSSREQEGT ESTTDEGQLP QVVEELRDLQ VAPGTRLAKF
QLKVKGYPAP RLYWFKDGQP LTASAHIRMT DKKILHTLEI ISVTREDSGQ YAAYISNAMG
AAYSSARLLV RGPDEPEEKP ASDVHEQLVP PRMLERFTPK KVKKGSSITF SVKVEGRPVP
TVHWLREEAE RGVLWIGPDT PGYTVASSAQ QHSLVLLDVG RQHQGTYTCI ASNAAGQALC
SASLHVSGLP KVEEQEKVKE ALISTFLQGT TQAISAQGLE TASFADLGGQ RKEEPLAAKE
ALGHLSLAEV GTEEFLQKLT SQITEMVSAK ITQAKLQVPG GDSDEDSKTP SASPRHGRSR
PSSSIQESSS ESEDGDARGE IFDIYVVTAD YLPLGAEQDA ITLREGQYVE VLDAAHPLRW
LVRTKPTKSS PSRQGWVSPA YLDRRLKLSP EWGAAEAPEF PGEAVSEDEY KARLSSVIQE
LLSSEQAFVE ELQFLQSHHL QHLERCPHVP IAVAGQKAVI FRNVRDIGRF HSSFLQELQQ
CDTDDDVAMC FIKNQAAFEQ YLEFLVGRVQ AESVVVSTAI QEFYKKYAEE ALLAGDPSQP
PPPPLQHYLE QPVERVQRYQ ALLKELIRNK ARNRQNCALL EQAYAVVSAL PQRAENKLHV
SLMENYPGTL QALGEPIRQG HFIVWEGAPG ARMPWKGHNR HVFLFRNHLV ICKPRRDSRT
DTVSYVFRNM MKLSSIDLND QVEGDDRAFE VWQEREDSVR KYLLQARTAI IKSSWVKEIC
GIQQRLALPV WRPPDFEEEL ADCTAELGET VKLACRVTGT PKPVISWYKD GKAVQVDPHH
ILIEDPDGSC ALILDSLTGV DSGQYMCFAA SAAGNCSTLG KILVQVPPRF VNKVRASPFV
EGEDAQFTCT IEGAPYPQIR WYKDGALLTT GNKFQTLSEP RSGLLVLVIR AASKEDLGLY
ECELVNRLGS ARASAELRIQ SPMLQAQEQC HREQLVAAVE DTTLERADQE VTSVLKRLLG
PKAPGPSTGD LTGPGPCPRG APALQETGSQ PPVTGTSEAP AVPPRVPQPL LHEGPEQEPE
AIARAQEWTV PIRMEGAAWP GAGTGELLWD VHSHVVRETT QRTYTYQAID THTARPPSMQ
VTIEDVQAQT GGTAQFEAII EGDPQPSVTW YKDSVQLVDS TRLSQQQEGT TYSLVLRHVA
SKDAGVYTCL AQNTGGQVLC KAELLVLGGD NEPDSEKQSH RRKLHSFYEV KEEIGRGVFG
FVKRVQHKGN KILCAAKFIP LRSRTRAQAY RERDILAALS HPLVTGLLDQ FETRKTLILI
LELCSSEELL DRLYRKGVVT EAEVKVYIQQ LVEGLHYLHS HGVLHLDIKP SNILMVHPAR
EDIKICDFGF AQNITPAELQ FSQYGSPEFV SPEIIQQNPV SEASDIWAMG VISYLSLTCS
SPFAGESDRA TLLNVLEGRV SWSSPMAAHL SEDAKDFIKA TLQRAPQARP SAAQCLSHPW
FLKSMPAEEA HFINTKQLKF LLARSRWQRS LMSYKSILVM RSIPELLRGP PDSPSLGVAR
HLCRDTGGSS SSSSSSDNEL APFARAKSLP PSPVTHSPLL HPRGFLRPSA SLPEEAEASE
RSTEAPAPPA SPEGAGPPAA QGCVPRHSVI RSLFYHQAGE SPEHGALAPG SRRHPARRRH
LLKGGYIAGA LPGLREPLME HRVLEEEAAR EEQATLLAKA PSFETALRLP ASGTHLAPGH
SHSLEHDSPS TPRPSSEACG EAQRLPSAPS GGAPIRDMGH PQGSKQLPST GGHPGTAQPE
RPSPDSPWGQ PAPFCHPKQG SAPQEGCSPH PAVAPCPPGS FPPGSCKEAP LVPSSPFLGQ
PQAPPAPAKA SPPLDSKMGP GDISLPGRPK PGPCSSPGSA SQASSSQVSS LRVGSSQVGT
EPGPSLDAEG WTQEAEDLSD STPTLQRPQE QATMRKFSLG GRGGYAGVAG YGTFAFGGDA
GGMLGQGPMW ARIAWAVSQS EEEEQEEARA ESQSEEQQEA RAESPLPQVS ARPVPEVGRA
PTRSSPEPTP WEDIGQVSLV QIRDLSGDAE AADTISLDIS EVDPAYLNLS DLYDIKYLPF
EFMIFRKVPK SAQPEPPSPM AEEELAEFPE PTWPWPGELG PHAGLEITEE SEDVDALLAE
AAVGRKRKWS SPSRSLFHFP GRHLPLDEPA ELGLRERVKA SVEHISRILK GRPEGLEKEG
PPRKKPGLAS FRLSGLKSWD RAPTFLRELS DETVVLGQSV TLACQVSAQP AAQATWSKDG
APLESSSRVL ISATLKNFQL LTILVVVAED LGVYTCSVSN ALGTVTTTGV LRKAERPSSS
PCPDIGEVYA DGVLLVWKPV ESYGPVTYIV QCSLEGGSWT TLASDIFDCC YLTSKLSRGG
TYTFRTACVS KAGMGPYSSP SEQVLLGGPS HLASEEESQG RSAQPLPSTK TFAFQTQIQR
GRFSVVRQCW EKASGRALAA KIIPYHPKDK TAVLREYEAL KGLRHPHLAQ LHAAYLSPRH
LVLILELCSG PELLPCLAER ASYSESEVKD YLWQMLSATQ YLHNQHILHL DLRSENMIIT
EYNLLKVVDL GNAQSLSQEK VLPSDKFKDY LETMAPELLE GQGAVPQTDI WAIGVTAFIM
LSAEYPVSSE GARDLQRGLR KGLVRLSRCY AGLSGGAVAF LRSTLCAQPW GRPCASSCLQ
CPWLTEEGPA CSRPAPVTFP TARLRVFVRN REKRRALLYK RHNLAQVR
