OBSCN_MOUSE
ID OBSCN_MOUSE Reviewed; 8886 AA.
AC A2AAJ9; A2AB85; B2FDE7; Q695L2; Q811H7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Obscurin;
DE EC=2.7.11.1 {ECO:0000269|PubMed:23392350};
DE AltName: Full=Obscurin-RhoGEF;
DE AltName: Full=Obscurin-myosin light chain kinase;
DE Short=Obscurin-MLCK;
GN Name=Obscn {ECO:0000312|MGI:MGI:2681862}; Synonyms=Gm878;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAT80900.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7308-8886 (ISOFORM 1).
RX PubMed=15185077; DOI=10.1007/s00427-004-0413-5;
RA Sutter S.B., Raeker M.O., Borisov A.B., Russell M.W.;
RT "Orthologous relationship of obscurin and Unc-89: phylogeny of a novel
RT family of tandem myosin light chain kinases.";
RL Dev. Genes Evol. 214:352-359(2004).
RN [4] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=15289607; DOI=10.1073/pnas.0306880101;
RA Caenepeel S., Charydczak G., Sudarsanam S., Hunter T., Manning G.;
RT "The mouse kinome: discovery and comparative genomics of all mouse protein
RT kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11707-11712(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-3321; SER-3802;
RP SER-4960; SER-5699; THR-5703; SER-5706; THR-5737; SER-5754; SER-6512;
RP THR-6518; SER-6520 AND SER-6522, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ALTERNATIVE SPLICING, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION
RP WITH CDH2 AND ATP1B1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND GLYCOSYLATION.
RX PubMed=23392350; DOI=10.1096/fj.12-221317;
RA Hu L.Y., Kontrogianni-Konstantopoulos A.;
RT "The kinase domains of obscurin interact with intercellular adhesion
RT proteins.";
RL FASEB J. 27:2001-2012(2013).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), FUNCTION (ISOFORMS 2 AND 3),
RP SUBCELLULAR LOCATION (ISOFORMS 2 AND 3), TISSUE SPECIFICITY (ISOFORMS 2 AND
RP 3), DEVELOPMENTAL STAGE (ISOFORMS 2 AND 3), AND IDENTIFICATION IN A COMPLEX
RP WITH DSG2; DESM; GJA1; CDH2; ANK3 AND VCL (ISOFORMS 2 AND 3).
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).
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 (By similarity). Has
CC serine/threonine protein kinase activity and phosphorylates N-cadherin
CC CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1
CC (PubMed:23392350). 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) (By similarity). {ECO:0000250|UniProtKB:Q5VST9,
CC ECO:0000269|PubMed:23392350}.
CC -!- FUNCTION: Isoform 2 and isoform 3: bind phosphatidylinositol
CC bisphosphates (PIP2s) via their PH domains and negatively regulate the
CC PI3K/AKT/mTOR signaling pathway, thus contributing to the regulation of
CC cardiomyocyte size and adhesion. {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:0000269|PubMed:23392350};
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:0000269|PubMed:23392350};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23392350};
CC -!- SUBUNIT: Interacts (via protein kinase domain 1) with CDH2 and (via
CC protein kinase domain 1) with ATP1B1 (PubMed:23392350). Isoform 2 is
CC found in a complex with DSG2, DESM, GJA1, CDH2 and VCL
CC (PubMed:28826662). Isoform 3 is found in a complex with DSG2, DESM,
CC GJA1, CDH2, ANK3 and VCL (PubMed:28826662).
CC {ECO:0000269|PubMed:23392350, ECO:0000269|PubMed:28826662}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:23392350}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:23392350}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:23392350}. Nucleus {ECO:0000269|PubMed:23392350}.
CC Secreted {ECO:0000269|PubMed:23392350}. Note=Colocalizes with CDH2 and
CC ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles.
CC Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. One or
CC both small isoforms, one probably containing protein kinase domain 2
CC and partial protein kinase domain 1 and one containing only protein
CC kinase domain 2, localize to the extracellular side of the sarcolemma.
CC {ECO:0000269|PubMed:23392350}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:28826662}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC {ECO:0000269|PubMed:28826662}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Two additional small isoforms seem to exist.
CC {ECO:0000269|PubMed:23392350};
CC Name=1;
CC IsoId=A2AAJ9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334}; Synonyms=obsc-40
CC {ECO:0000303|PubMed:28826662};
CC IsoId=A2AAJ9-2; Sequence=VSP_060093, VSP_060095, VSP_060096;
CC Name=3 {ECO:0000269|PubMed:15185077}; Synonyms=obsc-80
CC {ECO:0000303|PubMed:28826662};
CC IsoId=A2AAJ9-3; Sequence=VSP_060093, VSP_060094, VSP_060097;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscles including flexor
CC digitorum brevis (FDB), soleus and tibialis anterior muscles, and to a
CC lesser extent in heart muscles (at protein level) (PubMed:23392350).
CC Isoform 2 and isoform 3 are expressed in the myocardium (at protein
CC level) (PubMed:28826662). {ECO:0000269|PubMed:23392350,
CC ECO:0000269|PubMed:28826662}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 and isoform 3 are expressed during late
CC embryogenesis and throughout postnatal development in the myocardium
CC (at protein level) (PubMed:28826662). Isoform 3 is the predominant form
CC in mid-embryogenesis (11 dpc), and moderately decreases postnatally and
CC in adulthood (at protein level) (PubMed:28826662). Isoform 2 increases
CC significantly as development progresses (at protein evel)
CC (PubMed:28826662). {ECO:0000269|PubMed:28826662}.
CC -!- PTM: Autophosphorylated by protein kinase domain 1 and 2.
CC {ECO:0000269|PubMed:23392350}.
CC -!- PTM: Two small isoforms, one probably containing protein kinase domain
CC 2 and a partial protein kinase domain 1 and one containing only protein
CC kinase domain 2, are glycosylated. {ECO:0000269|PubMed:23392350}.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks the kinase domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44882.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GL456158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044882; AAH44882.2; ALT_INIT; mRNA.
DR EMBL; BC060226; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY603754; AAT80900.1; -; mRNA.
DR IntAct; A2AAJ9; 2.
DR STRING; 10090.ENSMUSP00000038264; -.
DR iPTMnet; A2AAJ9; -.
DR PhosphoSitePlus; A2AAJ9; -.
DR MaxQB; A2AAJ9; -.
DR PaxDb; A2AAJ9; -.
DR PeptideAtlas; A2AAJ9; -.
DR PRIDE; A2AAJ9; -.
DR ProteomicsDB; 294057; -. [A2AAJ9-1]
DR ProteomicsDB; 294058; -. [A2AAJ9-2]
DR ProteomicsDB; 294059; -. [A2AAJ9-3]
DR Antibodypedia; 11615; 42 antibodies from 15 providers.
DR Ensembl; ENSMUST00000238536; ENSMUSP00000158795; ENSMUSG00000061462. [A2AAJ9-1]
DR MGI; MGI:2681862; Obscn.
DR VEuPathDB; HostDB:ENSMUSG00000061462; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000154756; -.
DR InParanoid; A2AAJ9; -.
DR OMA; VCELVIH; -.
DR PhylomeDB; A2AAJ9; -.
DR PRO; PR:A2AAJ9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2AAJ9; protein.
DR Bgee; ENSMUSG00000061462; Expressed in hindlimb stylopod muscle and 72 other tissues.
DR ExpressionAtlas; A2AAJ9; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0005863; C:striated muscle myosin thick filament; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; 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; IEA:InterPro.
DR GO; GO:0031432; F:titin binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
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; -; 70.
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; 3.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 60.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 64.
DR SMART; SM00408; IGc2; 58.
DR SMART; SM00406; IGv; 13.
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; 66.
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; 56.
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 Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
KW Cytoplasm; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Kinase; Lipid-binding; Magnesium;
KW Membrane; Metal-binding; Muscle protein; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Serine/threonine-protein kinase; SH3 domain; Transferase.
FT CHAIN 1..8886
FT /note="Obscurin"
FT /id="PRO_0000296296"
FT DOMAIN 9..99
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 109..201
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 234..320
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 329..415
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 513..610
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 702..793
FT /note="Ig-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 859..951
FT /note="Ig-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 951..1043
FT /note="Ig-like 7"
FT /evidence="ECO:0000255"
FT DOMAIN 1043..1135
FT /note="Ig-like 8"
FT /evidence="ECO:0000255"
FT DOMAIN 1135..1227
FT /note="Ig-like 9"
FT /evidence="ECO:0000255"
FT DOMAIN 1227..1319
FT /note="Ig-like 10"
FT /evidence="ECO:0000255"
FT DOMAIN 1319..1407
FT /note="Ig-like 11"
FT /evidence="ECO:0000255"
FT DOMAIN 1411..1503
FT /note="Ig-like 12"
FT /evidence="ECO:0000255"
FT DOMAIN 1503..1595
FT /note="Ig-like 13"
FT /evidence="ECO:0000255"
FT DOMAIN 1595..1687
FT /note="Ig-like 14"
FT /evidence="ECO:0000255"
FT DOMAIN 1687..1779
FT /note="Ig-like 15"
FT /evidence="ECO:0000255"
FT DOMAIN 1779..1871
FT /note="Ig-like 16"
FT /evidence="ECO:0000255"
FT DOMAIN 1871..1963
FT /note="Ig-like 17"
FT /evidence="ECO:0000255"
FT DOMAIN 1963..2051
FT /note="Ig-like 18"
FT /evidence="ECO:0000255"
FT DOMAIN 2055..2147
FT /note="Ig-like 19"
FT /evidence="ECO:0000255"
FT DOMAIN 2152..2241
FT /note="Ig-like 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2242..2325
FT /note="Ig-like 21"
FT /evidence="ECO:0000255"
FT DOMAIN 2329..2415
FT /note="Ig-like 22"
FT /evidence="ECO:0000255"
FT DOMAIN 2420..2504
FT /note="Ig-like 23"
FT /evidence="ECO:0000255"
FT DOMAIN 2598..2681
FT /note="Ig-like 24"
FT /evidence="ECO:0000255"
FT DOMAIN 2721..2812
FT /note="Ig-like 25"
FT /evidence="ECO:0000255"
FT DOMAIN 2900..2984
FT /note="Ig-like 26"
FT /evidence="ECO:0000255"
FT DOMAIN 3078..3162
FT /note="Ig-like 27"
FT /evidence="ECO:0000255"
FT DOMAIN 3258..3342
FT /note="Ig-like 28"
FT /evidence="ECO:0000255"
FT DOMAIN 3348..3431
FT /note="Ig-like 29"
FT /evidence="ECO:0000255"
FT DOMAIN 3527..3610
FT /note="Ig-like 30"
FT /evidence="ECO:0000255"
FT DOMAIN 3616..3700
FT /note="Ig-like 31"
FT /evidence="ECO:0000255"
FT DOMAIN 3785..3876
FT /note="Ig-like 32"
FT /evidence="ECO:0000255"
FT DOMAIN 3881..3964
FT /note="Ig-like 33"
FT /evidence="ECO:0000255"
FT DOMAIN 4042..4125
FT /note="Ig-like 34"
FT /evidence="ECO:0000255"
FT DOMAIN 4130..4213
FT /note="Ig-like 35"
FT /evidence="ECO:0000255"
FT DOMAIN 4219..4301
FT /note="Ig-like 36"
FT /evidence="ECO:0000255"
FT DOMAIN 4307..4389
FT /note="Ig-like 37"
FT /evidence="ECO:0000255"
FT DOMAIN 4395..4477
FT /note="Ig-like 38"
FT /evidence="ECO:0000255"
FT DOMAIN 4483..4565
FT /note="Ig-like 39"
FT /evidence="ECO:0000255"
FT DOMAIN 4571..4653
FT /note="Ig-like 40"
FT /evidence="ECO:0000255"
FT DOMAIN 4659..4741
FT /note="Ig-like 41"
FT /evidence="ECO:0000255"
FT DOMAIN 4746..4829
FT /note="Ig-like 42"
FT /evidence="ECO:0000255"
FT DOMAIN 4833..4916
FT /note="Ig-like 43"
FT /evidence="ECO:0000255"
FT DOMAIN 4923..5007
FT /note="Ig-like 44"
FT /evidence="ECO:0000255"
FT DOMAIN 5013..5105
FT /note="Ig-like 45"
FT /evidence="ECO:0000255"
FT DOMAIN 5378..5464
FT /note="Ig-like 46"
FT /evidence="ECO:0000255"
FT DOMAIN 5471..5569
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 5557..5659
FT /note="Ig-like 47"
FT /evidence="ECO:0000255"
FT DOMAIN 5821..5850
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 5847..5930
FT /note="Ig-like 48"
FT /evidence="ECO:0000255"
FT DOMAIN 6077..6166
FT /note="Ig-like 49"
FT /evidence="ECO:0000255"
FT DOMAIN 6209..6298
FT /note="Ig-like 50"
FT /evidence="ECO:0000255"
FT DOMAIN 6320..6416
FT /note="Ig-like 51"
FT /evidence="ECO:0000255"
FT DOMAIN 6549..6616
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 6642..6826
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 6844..6953
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 6963..7046
FT /note="Ig-like 52"
FT /evidence="ECO:0000255"
FT DOMAIN 7057..7147
FT /note="Ig-like 53"
FT /evidence="ECO:0000255"
FT DOMAIN 7306..7394
FT /note="Ig-like 54"
FT /evidence="ECO:0000255"
FT DOMAIN 7416..7669
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 8380..8464
FT /note="Ig-like 55"
FT /evidence="ECO:0000255"
FT DOMAIN 8474..8566
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 8590..8842
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 135..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5700..5736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5977..5996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6504..6546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7200..7257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7717..7810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7879..8106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 8150..8180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5700..5728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6523..6539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7230..7257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7734..7749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7882..7896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7903..7917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7968..8039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8058..8078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 7535
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523"
FT ACT_SITE 8709
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523"
FT BINDING 6924
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:0000250|UniProtKB:Q5VST9"
FT BINDING 6929
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:0000250|UniProtKB:Q5VST9"
FT BINDING 7422..7430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 7445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 8596..8604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 8619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5703
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5737
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6518
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 7779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VST9"
FT MOD_RES 8161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VST9"
FT DISULFID 30..81
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 257..309
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..402
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 885..935
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 977..1027
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1069..1119
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1161..1211
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1253..1303
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1345..1395
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1437..1487
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1529..1579
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1621..1671
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1713..1763
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1805..1855
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1897..1947
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1989..2039
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2081..2131
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2263..2313
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2620..2669
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2743..2793
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2922..2972
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3100..3150
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3280..3330
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3369..3419
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3549..3599
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3638..3688
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3815..3864
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3903..3952
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4064..4113
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4152..4201
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4240..4289
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4328..4377
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4416..4465
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4504..4553
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4592..4641
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4680..4729
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4768..4817
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4856..4906
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4945..4995
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5034..5086
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5590..5643
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5868..5920
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 6098..6150
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 6984..7036
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 7078..7131
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 8401..8453
FT /evidence="ECO:0000250|UniProtKB:Q5VST9,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..6831
FT /note="Missing (in isoform 3 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_060093"
FT VAR_SEQ 7170..7563
FT /note="DTSVEGSAHSAQDGADQQAASVLWRLLGSEALGPSPGDLPNTRQSEPPAFEE
FT AASQIPGAASGTPEVSQPGTHKGLEQETTSSGSQGWTVPIRVEGTAWPGAGTGQLLLDV
FT HSQVIMETTQRTYVCQAPDTGVTRAPSMQVTIEDVQVQVGDMAQFDAVIEGHPPPIVTW
FT YKGSTQLTSSARLSQRQDGTTYSLVLTDVAPHDAGVYTCVANNAGGQVLCKAELLVHGG
FT DKLDAENQVYRRKLHSFYDVQEEIGRGVFGFVKRVQHKGNKMFCAAKFIPLRSKTRAQA
FT YQERDILATLGHPLVTGLLDQFETRKTLILILELCSSEELLDRLFKKGVVTEAEVKVYI
FT QQLVEGLHYLHSHGILHLDIKPPNILMVHPAREDIKICDFGFAQKIT -> VTEQETKV
FT PKKTVIIEETITTVVKSPRGRRQSPGKSPSRSPSRRSASPRRPGLLAPERLYPPGTSPS
FT RRLEVEQGRKAPVPALYVTEAEVHAPASQSQPKWLEVEETIEVRVKKTGSRGASPVREM
FT TSRGEGILFTLPGGIPGRDPNANNSNNKSVYQEARTWGPAVVHVGEPFIFQVDSVGNVD
FT WVAASPEPEQVRASQKEENTERQEGCSDGDENTFLMEEPQDTDSLQGRDPKILTHNGRV
FT LTLADLEDYVPQEGETFGCGDSTPSTPDEPPCEVSVLQREISEPTVGQPVLLNVGRPPG
FT TGATPSFFRPGSQVHSPESVSFLLREAWSGPVSAAPWTSSFHTHVQSSVDGSHGSFKTE
FT VSTQTVSFGAVGETVTLHIDPDGGEAPGPSQG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_060094"
FT VAR_SEQ 7170..7176
FT /note="DTSVEGS -> ERRPSPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_060095"
FT VAR_SEQ 7177..8886
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_060096"
FT VAR_SEQ 7564..8886
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_060097"
FT CONFLICT 7655
FT /note="R -> Q (in Ref. 3; AAT80900)"
FT /evidence="ECO:0000305"
FT CONFLICT 8513
FT /note="G -> E (in Ref. 3; AAT80900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 8886 AA; 966591 MW; 8AF41AB644D02324 CRC64;
MDHSFSGAPR FLTRPKAFVV SVGKDATLSC QIVGNPTPHV SWEKDRQPVE AGARFRLAQD
GDVYRLTILD LALGDSGQYV CRARNAIGEA FAAVGLRVDS EGTCAEQAPH FLLRPTSIRV
REGADATFRC RVGGSPQPAV SWSKDGRRLG PPDAPHVRVE EHGESSALRI RSARPRDGGT
YEVRAENPLG SASAAAALVV DSDAEVAGPP GTSTATLLAH LQQRREAMRA EGIPPSPPGA
GTRTCTVTEG KHARLSCFVT GEPKPETVWK KDGQLVTEGR RHVVYEDEQE NFVLKILFCK
QSDRGLYTCT ASNLVGQTYS SVLVVVREPT VPFKKRLQDL EVREKESATF QCEVAQPATE
AAWFKEETRL WASAKYDIEE EGTERRLTVR NVSADDDAVY ICETTEGSRT VAELSVQGNL
TRKLPRKTAV RTGDTAIFWV ELAVPEGPVR WLRNQEEMVA GGRVAITAEG TCHTLTIFQC
TLEDMGEVAF VSGGCRTTTQ FCVSAPRRPP LYPPADPVVK AKTESSVTLS WSAPPHGDRP
VTIDGYVLEK RKLGAYAWSR CHEAGWLATT EFTITGVAEE GDFQFRVSAI NHFGQGPYLE
FPGTMHLVPM LAVKTPLKAV EAVEGGEVTF SVDLTVASSG EWFLDGEALK ASSIYVIRCD
RTRHMLTIRE VPARLHGAQL KFVANGIETS IQMVVRAALG LPSSKLPAAA AREVLAQLHE
EAQLLAELSD QAAAVTWLKD GRELSLGPKY EMQVSAGRRA LLVRDVAQDD AGLYECVSRG
SRTAYQLLVQ DITDGYRDWG PAGPQKHMCK CAGAKIARYL GSSCYRFLQY DKGVWHWLEA
ALDTRQGKGT SSCSLHEKPK LVFAKGQQAH SEVKAEAGNS ATLSCEVTQA QTEVTWFKDG
KKLSSSSKVR MEASGCSRRL VVQQAGKADA GEYSCEAGGQ KLSFRLDVAE PKLVFAKGQQ
AHSEVKAEAG ASATLSCEVA QAQTEVTWFK DGKKLSSSSK VRMEASGCSR RLVVQQAGKA
DAGEYSCEAG GQKLSFRLDV AEPKMVFAKE QQARSEVKAE AGASATLSCE VAQAQTEVTW
FKDGKKLSSS SKVRMEASGC SRRLVVQQAG KADAGEYSCE AGGQKLSFRL DVTEPKLVFA
KEQQARSEVK AEVGNSATLS CEVAQAQTEV TWFKDGKKLS SSSKVRMEAS GCSRRLVVQQ
AGKADAGEYS CEAGGQKLSF RLDVAEPKLV FAKEQQARSE VKAEAGNSAT LSCEVAQAQT
EVTWFKDGKK LSSSSKVRME ASGCSRRLVV QQAGKADAGE YSCEAGGQKL SFHLDVTEPK
LVFAKEQQAH SEVKAEAGAS ATLSCEVAQA QTEVTWFKDG KKLSSSSKVR MEASGCSRRL
VVQQAGKADA GEYSCEAEGQ KLSFRLDVAE PKLVFAKEQQ ARSEVKAEAG ASATLSCEVA
QAQTEVTWFK DGKKLSSSSK VRVEASGCSR RLVVQQAGKA DAGEYSCEAG GQKLSFRLDV
AEPKLVFAKE QQANSEVKAE AGASATLSCE VAQAQTEVTW FKDGKKLSSS SKVRVEASGC
SRRLVVQQAG KADAGEYSCE AGGQKLSFRL DVAEPKLAFA KEQQAHSEVK AEAGASATLS
CEVAQAQTEV TWFKDGKKLS SSSKVRVEAS GCSRRLVVQQ AGKADAGEYS CEAGGQKLSF
RLDVAEPKLA FAKEQQAHSE VKAEAGASAT LSCEVAQAQT EVTWFKDGKK LSSSSKVRVE
ASGCSRRLVV QQAGKADAGE YSCEAGGQKL SFRLDVAEPK LAFAKEQQAH SEVKAEAGAS
ATLSCEVAQA QTEVTWFKDG KKLSSSSKVR VEASGCSRRL VVQQAGKADA GEYSCEAGGQ
KLFFRLDVAE PKLMFAKEQQ AHSEVKAEAG ASATLSCEVA QAQTEVTWFK DGKKLSSSSK
VRVEASGCSR RLVVQQAGKA DAGEYSCEAG GQKLSFRLDV AEPKLVFAKE QQAHSEVKAE
AGASATLSCE VAQAQTEVTW FKDGKKLSSS SKVRVEASGC SRRLVVQQVG KADAGEYSCE
ARGQKLSFRL DVADTRLMFA KEQQARTEVK AEAGNSATLS CEVAQAQTEV TWFKDGKKLS
SSSKVRVEAS GCSRRLVVQQ AGKADAGEYS CEAGGQKLSF RLDVAEAESQ IPERPSRREP
LVVKEHETII LTATIAAPSV AAVTWLKDGV EIRRSKRHEA TSLGDTHTLT VRGAQVLDSA
IYSCRVGKEG QDFPVQVEEV AAKFSKPLEP VEGELGGTVM LVCELSPEQA EVVWRCGNTQ
LRPGKRFQMT SEGPRRTLTV SGLREDDAEE YVCESRDDRT SARLTVKVPR VVKFTSGLSA
MVAEEGQEAT FQCVVSPSDA GVTWYKDGMQ LQPSEKFVMV ESGASRSLTI LGLTLEDAGQ
VTVEAEGASS SAALRVREAP VLFKKKLEPQ TVEERTSVTL EVELTRPWPE VKWTRNAAVL
TPSENVEIRA EGARHCLVLR SVGFADRGFF GCETPDDKTQ AKLNVEMRQV RLVRGLQEVE
AKEQGTASMD VELSHAEVEG SWTRDGLRLQ PGPKCHLAVQ GPVHILTLSA LQPQDSGLVA
FRAEGVHTSA RLIVTELPVS FTRVLQDVVA TQKEKVTLEC ELSRPVDVRW LKDGVELRAG
KAIGIVAQGT CRSLVIYRCE TGDQGVYVCD ALDAQTSASL RVQGRTYTLI FRRVLAEDAG
EVKFVAENAE SRAHLRVKEL PVTLLRPLRD KIAMEKHRGV LECQVSRASA QVRWFKGGVE
LQSGPKYEVV SDGLYRKLVI NDVQPEDEDT YTCDAGNVKT SAQFFVEEQS ITIVRGLKDM
TVMEPAPAWF ECETSIPSVR PPKWLLGKTV LQAGGNVGLE QDGTVHRLTL HKTCSTMTGP
VHFTIGKSRS SAQLVVSDIP VVLTRPLEPK AGRELQSVVL SCDFRPAPKA VQWYKDDTPL
SPSEKFKMAL EGQMAELRIL RLTPADAGVY RCQAGSAQSS AEVTVEAREV TVIQPLQDAE
AMEEGRVCFS CELSHKDEDI EWSLNGTPLY NDSFHEISHE GCLHTLVLKS VRQADTGTVC
ATSPKVSVSA RLVVKGKPVV FLKALDDVSA EERGTLTLQC EVSDPEARVV WRKDGVELGP
SDKYDFLHKA GARGLTVHDL SHEDAGLYTC QVGSKETQSK VSVHDLHVGI TKRLKTVEVL
EGESCSFECV LSHESPSDPA VWTVGGKTVG GSGHFHAVRQ GRKYTLTVKD AALSDAGEVV
FSVLGLTSKA SLIIRERPVD ITKPLEDQRT TLGEDVMLSC ELSRAGTSVR WLKDGKAIRK
SQKYDLLSEG TRAVLVVRKA SLKDSGEYTC ETEASKSTAK LCVEEKANRF TEELADLQVE
EKGRAVFTCK TEHPASVVTW RKGLLELRAS GKHVPSQEGL TLKLTINALE RTDSDTYTCD
IGQARTQARL LVHGQKVRVI EDLEDTAVQE GSSAKFCCRI APADYGPVHW FLDKTPLHSN
ELNEITVQPG GYHVLTLRQL ALKDSGTVYF EAGDQRTSAA LRVTEKPSIF SRPLTDVTVT
EGEDLTLVCE TTTVDSSVRW TKDGKTLRPS ARCQLSHEGC QAQLLITATT PQDGGRYKCE
IGGASSSSIV RVHALPVRFR ESLKDVEVPE GKAATLRCVL SSVAAPVEWR HGDDVLKSSN
KYSLRQEGAV LELVIRDLQP QDSGQYSCSF GDQTTSATLT VKTSSAQFVG KLRNKEATEG
TTVTLRCELT KEAPVEWKKG TETLRNGDKY SLKQDGAVCE LQICSLLVAD AGEYSCVCGQ
EKTSATLTVK ALLVHFVRRL RSKEATEGDT TTLQCELSKA APVEWRKGTE TLRDGDRYSL
KQDGAVCELQ IRSLTIADAG EYLCTCGQEK TSATLTVRAL PAKFKDSLKN EEATEGTTAT
LSCELSKAAP VTWKKGPKTL QSGDKYVLRQ DGAVCGLQIH GLTMADAGEY SCVCGQEKTS
ATLTVRGLPA KFIEDLRSQE ATEGATAILR CELSKAAPVE WRKGSETLKD GDRYTLRQDG
AVCELQIRGL AVVDTGTYSS LPTKFTEGLR NEEATEGTMA TLRCQMSKAA PVEWRKGSET
LRDGDRYSLR QDGAMCELQI RGLTIEDSGE YTCVCGQEKT SATLSVKALP SRFIEDLRSQ
EATEGTMATL RCQMSKTAPV EWKKGSETLR DGGRYSLRQD GPVCELQICD LAVEDAGEYS
CVCGQEKTSA TLSIKALPPR FIEDLRSQEA TEGTMATLRC QMSKAAPVEW RKGSETLGDG
GRYSLRQNGA VCELQIHDLA VEDTGEYSCV CGQEKTSATL NVKALPPRFI EDLRSQEATE
GTMATLRCQM SKAAPVEWRK GSETLRDGGR YSLRQDGAVC ELQIHDLDVE DAGQYSCVCG
QEKTSAVLTV DALPPKFTEG LKKEEATEGT MVTLRCQMSK EATVEWRKGA KTLSDGGRYS
LRQDGAMCEL QICGLAVEDA GEYSCVCGQE KTSATLSVKA LPPRFIEDLR SQEATEGTMA
TLRCQMSKAA PVEWRKGSET LRDGDRYSLR QDGAVCELQI RDLAVEDAGE YLCVCGQEKT
SATLSVKALP PRFIEDLRSQ EATEGTMATL RCQMSKAAPV EWRKGSKTLR DGDRYSLRQD
GAMCELQICD LAVEDTGDYS CVCGQEKTSA TLSVKALPPR FIEDLRSQEA REGTVATLRC
RMSKAAPVEW RKGSETLKDG DRYSLRQEGN LCELQIRDLA VEDTEEYSCV CGQEKTSATL
SVKALPAKFI EDLRSQEAPE SSTVTLRCKL SKKASVVWKK GSETLRNGAR YSLRQDGAVC
ELEIRDLTVE DTGEYSCTCG QERTSATLSI MAPQVVFQQP LQNLQAEEGS MASLRCELSV
PNAAMVWSKG GLELQGDTRR EARQQGCVAE LLLRDLRRED AGEYSCTCGS QTTSATLMVT
AAPVRFLREL QAQDVDEGAT ARLRCELSRE AVSVEWRKGS LQLFPCAKYQ MVQEGTTAEL
LVHGVEQEDA GEYTCDAGHT QSIARLSVRA PKPKFKTDLQ STEQEAGGTA RLCCQLSEAE
PGTPVQWLKE GVELHVGSKY EMRRQGAVCE LLIHGLEAKD TGEYACLVGG QKTLASLRVK
EPEVTIVRGL VDMEVQADED VEFTCKVSQA GATDVQWHLQ GLPLQSNEVT EVAVLADGCT
HVLQLKGVTL EDAGTVSFHV GGLSSSAQLT VRVPEVTVLE PLKDVQLSEG QDAHFRCRLS
RASGQEARWA LGGVPLQCNE MNDITVEQGT LYLLTLHKVT LEDAGTITLQ VGSCSSEAQL
KVTAKNTVLR GLENVDALEG GEALFECQLS QPEVAAHTWL LDDEPVHTSE KVEVVYFENG
LRHLLLLKNL KPQDSCRVTF LAGDVVTSAF LTVRGWRLEV LEPPHDASVK AGMQVRFTCI
LSEAVPVGEA TWYINGAAIQ PDDTDWTVTT DGSHHALTLS NAQPQHAGEV TFAARDAVAS
ARLSVLALPD PPEDAEVVGR SDHSVTLSWV APMSDGGGGL CGYRVEMKEA STGQWQLCHD
LVPGPECVVD DLVPGKTYRF RVAAVGPAGA GEPVHLPQMV KIAPAPAPAP APAPAPAPET
RQAVVGEDIC LELEVAADGG EVVWHKGTER IQPGGHFEVL SRGQRQMLVI KGFRTEDQGE
YRCGPIQGLP SSGAATFNVV MTSGSGDEVP AQPSLPPEAA QEGDLHLLWE ALARKRRMSR
EPTLDSISEL PEEDSRVQHL RQEAEETAPD LSEGYSTADE LARTGEADLS HTSSDDESRA
GTPSLVTYLK KAGGPGISPL ASKHEAQVTT SVKPQKQQEP VVPTCPPPGD LSAADLMDPS
LDKAAVKIQA AFKGYKVRKE MKQQEGPVFS RTFGDTEAQV GDVLRLECVL ATKTDMRACW
LKDGIELTDG RHYHIDQLKD GTCSLLVTGL APTDSGRYTC QVSTKSGRVS HSACVVVSGT
ESEAESSSGG ELDDAFRRAA RRLHRLFRTK SPAELSEEEL FLSADEGPGE PEEPADWQTY
REDENFVCIR FESLAEARQA VTCFRNMFAT MGIGVEISLG EQGPRGVEMR IGKVAPTVTP
AVPLAKTPGL QTSDAAPVFL TELQNQDVQD GYPMSFDCVV TGQPVPSVRW FKDGKLLEED
DHYMINEDQQ GGHQLIITAV VPADMGVYRC LAENSMGVSS TKAELRVELT STDYDTAADA
TETSSYFSAQ GYLSSREQEG TESDEGQLPQ VLEELKDLQV APGTRLAKFQ LKVKGYPAPK
LYWFKDGQPL TTSDHIRMTD KKTLHTLEIV SVTREDSGQY AAYISNAVGA AYSSARLLVR
GPSEPEEKPA SDVHERLVPP RILEKFTPKK VKRGSSITFS VKVEGHPAPS VHWLKEEAEK
GVLWIGPDTP GYTMASSSKQ HSLVLLDVGR QHQGTYTCIA TNPAGQALCS ASLHISGLAK
EEEQERVKEA LISSFLQGTS QAVSAQMSES AGFADLVGQS KGESLVAEEA HSHLSLAEVG
TEEFLQKLTS QITEMVSAKI SQAKLQVPGG DSDEETKTPS ASPRHGRSRP SSSVQESSSE
SEDGDSRGEI FDIYVVTADY LPLGAEQDAI ILREGQYVEV LDSAHPLRWL VRTKPTKSSP
SRQGWVSPAY LDKRLKLSPE WGPTEAPEFP GEAVSEDEYR TRLSSVIQEL LSSEQAFVGE
LQFLESHHMK HLERSPRVPA AVASQKTVIF RNVQDISHFH SSFLKELQGC GTDDDVAMCF
IKNQEAFEKY LEFLVGRVQA ESVVVSTPVQ EFYKKYAEET LSAKDPTQPP PPPLQHYLEQ
PVERVQKYQA LLKELIRNKA RNRQNCALLE QAYAVVSALP QRAENKLHVS LMENYPGTLE
ALGEPIRQGH FIVWEGAPGA RMPWKGHNRH VFLFRNYLVI CKPRRDSRTD TFSYVFRNMM
KLSSIDLNDQ VEGDDRAFEV WHEREDSVRK YLLQARTVII KNSWVKEICG IQQRLAQPVW
RPPEFEEELA DCTAELGETV KLACRVTGTP KPIVSWYKDG KPVEVDPHHI LIEDPDGSCT
LILDNLTGID SGQYMCFAAS AAGNASTLGK ILVQVPPRFV NKVRATPFVE GEDAQITCTV
EGAPYPQIRW YKDGTLLAPG NRYRMLNEPR SGVLVLVIQA ASKEDLGHYE CELVNRLGST
RGGGELYMQS PALRARDQHH REQIVAAVED TSVEGSAHSA QDGADQQAAS VLWRLLGSEA
LGPSPGDLPN TRQSEPPAFE EAASQIPGAA SGTPEVSQPG THKGLEQETT SSGSQGWTVP
IRVEGTAWPG AGTGQLLLDV HSQVIMETTQ RTYVCQAPDT GVTRAPSMQV TIEDVQVQVG
DMAQFDAVIE GHPPPIVTWY KGSTQLTSSA RLSQRQDGTT YSLVLTDVAP HDAGVYTCVA
NNAGGQVLCK AELLVHGGDK LDAENQVYRR KLHSFYDVQE EIGRGVFGFV KRVQHKGNKM
FCAAKFIPLR SKTRAQAYQE RDILATLGHP LVTGLLDQFE TRKTLILILE LCSSEELLDR
LFKKGVVTEA EVKVYIQQLV EGLHYLHSHG ILHLDIKPPN ILMVHPARED IKICDFGFAQ
KITPSEPQYS KYGSPEFVSP EIIEQNPVSE GSDIWAMGVI SYLSLTCSSP FAGESDRATL
LNVLEGRVSW SSPTAAHLSE DAKDFIKATL QRTPRARPST SQCLAHPWFL KSMPAEEAHF
INTKQLKFLL ARSRWQRSLM SYKSILVMRS IPELLQGPPD SPSLGVARHL RGEASGASSS
SSSSDNELAP FARAKSLPPS PVTHSPLLHP RGFLRPSASL PEETEASMPT ADAAVPASPQ
SAGPPASPGC VPRHSVISSL FYQQAGEGAE RGNKTSGAKR HPARRRHLLK GGYIARALPG
LREPLMEYSL LEEEAAREEQ ASLMTKTPSF ETALRLPSSS VREVPGRSHS LDNPPVTTGP
SPEACKEQLL FPPSTGLTHE TTAKDRGHKE GFLQESVPFP PMSGDSRPGK QEGSSQDSCR
GKPASSCHSE LGSGSQEGCG PPSSQSLGSL PPQSLKKELS TSCGPLFSEQ PQAAPFPTQV
SPLLGSEKEP QDGSLSEGPV PVPSSSPGSA SQVDASLDTE GLSEAGDTCD FTPPPQRPQE
QATTRKFSLE SRGGYAGVAG YGTFAFGGDA GGMLGQGPLW ARMAWAVSQS SEEQDEAATE
SPQPLESLGP IAEASGVPLR TSPSLTPWEE VEQVSLVQIR DLSGDAEAAD TISLDISEVD
PAYLNLSDLY DIKYLPFEFM IFRRVPKPIE QPESPGSETE AGQGLADFLE EAAWPWPGEL
GLRAGLEITE EPEEPGDLEA LLGEAAVGRK RKWSPSRGLF QFPGRCLSGE EPVELGLRQR
VKASMAHISR ILKGRPEGPE REGPPRKKAG LASFRLSGLK GRDQELSDEA VVLGQSVTLA
CQVLAQPTAQ ATWSKDGVLL ESSGHLLISS TLKNFQLLTI LVVKEEDLGT YTCCVSNPLG
TAVTTGVLRK AERPSSSPRP EVGELYKDAV LLVWKPVESC GPVTYIVQCC IEGGSWTTLA
SDISDCCYLT GKLSRGGMYI FRTACVSKAG MGPYSSPSEQ VLLGGPNHLA SEEESSRGRP
AQLLPSTKTF AFQMQIRRGR FSVVRQCREK ASGRALAAKI VPYQPEDKTA VLREYEALKR
LHHPHLAQLH AAYLSPRHLV LILELCSGPE LLPSLAERES YSESDVKDYL WQMLSATQYL
HAQHILHLDL RSENMMVTEY NLLKVIDLGN AQSLDQEKVP APENFKDYLE TMAPELLEGQ
GAVPQTDIWA IGVTAFIMLS GEYPESSEGT RDLQKGLRKG LIRLSRCYAG LSGGAVAFLQ
SSLCAQPWGR PCASTCLQCG WLTEEGPTGS RPTPVTFPTV RLRAFVRERE KRRALLYKKH
NLAQVR
