SGIP1_HUMAN
ID SGIP1_HUMAN Reviewed; 828 AA.
AC Q9BQI5; A6NL81; A6NLD1; Q4LE32; Q5VYE2; Q5VYE3; Q5VYE4; Q68D76; Q6MZY6;
AC Q8IWC2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1;
DE AltName: Full=Endophilin-3-interacting protein;
GN Name=SGIP1;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-131.
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-131.
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP ARG-131.
RC TISSUE=Colon endothelium, and Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS GLN-161
RP AND GLU-575.
RC TISSUE=Hippocampus;
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 [6]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SH3GL3.
RX PubMed=15919751; DOI=10.1210/en.2005-0282;
RA Trevaskis J., Walder K., Foletta V., Kerr-Bayles L., McMillan J.,
RA Cooper A., Lee S., Bolton K., Prior M., Fahey R., Whitecross K.,
RA Morton G.J., Schwartz M.W., Collier G.R.;
RT "Src homology 3-domain growth factor receptor-bound 2-like (endophilin)
RT interacting protein 1, a novel neuronal protein that regulates energy
RT balance.";
RL Endocrinology 146:3757-3764(2005).
RN [7]
RP INTERACTION WITH AMPH; ITSN1 AND REPS1, AND SUBCELLULAR LOCATION.
RX PubMed=20946875; DOI=10.1016/j.bbrc.2010.10.045;
RA Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J.,
RA Rynditch A.;
RT "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated
RT pits.";
RL Biochem. Biophys. Res. Commun. 402:408-413(2010).
RN [8]
RP POLYMORPHISM.
RX PubMed=21407171; DOI=10.1038/ijo.2011.67;
RA Cummings N., Shields K.A., Curran J.E., Bozaoglu K., Trevaskis J.,
RA Gluschenko K., Cai G., Comuzzie A.G., Dyer T.D., Walder K.R., Zimmet P.,
RA Collier G.R., Blangero J., Jowett J.B.;
RT "Genetic variation in SH3-domain GRB2-like (endophilin)-interacting protein
RT 1 has a major impact on fat mass.";
RL Int. J. Obes. Relat. Metab. Disord. 36:201-206(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 552-828 IN COMPLEX WITH PEPTIDES
RP CONTAINING TWO DPF MOTIFS, AND INTERACTION WITH EPS15.
RX PubMed=26822536; DOI=10.1038/srep19565;
RA Shimada A., Yamaguchi A., Kohda D.;
RT "Structural basis for the recognition of two consecutive mutually
RT interacting DPF motifs by the SGIP1 mu homology domain.";
RL Sci. Rep. 6:19565-19565(2016).
CC -!- FUNCTION: May function in clathrin-mediated endocytosis. Has both a
CC membrane binding/tubulating activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a preference for membranes enriched in phosphatidylserine and
CC phosphoinositides and is required for the endocytosis of the
CC transferrin receptor. May also bind tubulin. May play a role in the
CC regulation of energy homeostasis. {ECO:0000250|UniProtKB:Q8VD37}.
CC -!- SUBUNIT: Interacts with proteins essential or regulating the formation
CC of functional clathrin-coated pits (Probable). Interacts with CANX (By
CC similarity). Interacts with AP2A1 (By similarity). Interacts with EPS15
CC (PubMed:26822536). Interacts with SH3GL3 (PubMed:15919751). Interacts
CC with AMPH (PubMed:20946875). Interacts with ITSN1 (via SH3 domains)
CC (PubMed:20946875). Interacts with and REPS1 (PubMed:20946875).
CC {ECO:0000250|UniProtKB:Q8VD37, ECO:0000269|PubMed:15919751,
CC ECO:0000269|PubMed:20946875, ECO:0000269|PubMed:26822536, ECO:0000305}.
CC -!- INTERACTION:
CC Q9BQI5; Q5T9L3-1: WLS; NbExp=3; IntAct=EBI-2690801, EBI-22114623;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000305|PubMed:20946875}; Peripheral membrane protein
CC {ECO:0000305|PubMed:20946875}; Cytoplasmic side
CC {ECO:0000305|PubMed:20946875}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BQI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQI5-2; Sequence=VSP_020274;
CC Name=3;
CC IsoId=Q9BQI5-3; Sequence=VSP_020274, VSP_020277;
CC Name=4;
CC IsoId=Q9BQI5-4; Sequence=VSP_020273, VSP_020275, VSP_020276;
CC Name=5;
CC IsoId=Q9BQI5-5; Sequence=VSP_020273, VSP_020275, VSP_020276,
CC VSP_020278;
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC {ECO:0000269|PubMed:15919751}.
CC -!- POLYMORPHISM: Genetic variation in SGIP1 is associated with fat mass
CC and SGIP1 may be a determinant of obesity-related traits.
CC {ECO:0000269|PubMed:21407171}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06121.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136561; CAB66496.1; -; mRNA.
DR EMBL; AB210039; BAE06121.1; ALT_INIT; mRNA.
DR EMBL; BX640813; CAE45891.1; -; mRNA.
DR EMBL; CR749541; CAH18344.1; -; mRNA.
DR EMBL; AL139147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040516; AAH40516.1; -; mRNA.
DR CCDS; CCDS30744.1; -. [Q9BQI5-1]
DR CCDS; CCDS76171.1; -. [Q9BQI5-5]
DR RefSeq; NP_001295132.1; NM_001308203.1. [Q9BQI5-5]
DR RefSeq; NP_115667.2; NM_032291.3. [Q9BQI5-1]
DR RefSeq; XP_005271321.1; XM_005271264.3.
DR RefSeq; XP_005271327.1; XM_005271270.4. [Q9BQI5-4]
DR RefSeq; XP_006711037.1; XM_006710974.2.
DR RefSeq; XP_016858000.1; XM_017002511.1.
DR RefSeq; XP_016858001.1; XM_017002512.1.
DR RefSeq; XP_016858023.1; XM_017002534.1.
DR RefSeq; XP_016858024.1; XM_017002535.1.
DR PDB; 5AWR; X-ray; 2.50 A; A=552-828.
DR PDB; 5AWS; X-ray; 2.00 A; A/B=552-828.
DR PDB; 5AWT; X-ray; 2.70 A; A=552-828.
DR PDB; 5AWU; X-ray; 2.70 A; A=552-828.
DR PDB; 6A9Y; X-ray; 2.70 A; A=558-828.
DR PDBsum; 5AWR; -.
DR PDBsum; 5AWS; -.
DR PDBsum; 5AWT; -.
DR PDBsum; 5AWU; -.
DR PDBsum; 6A9Y; -.
DR AlphaFoldDB; Q9BQI5; -.
DR SMR; Q9BQI5; -.
DR BioGRID; 123979; 38.
DR IntAct; Q9BQI5; 5.
DR MINT; Q9BQI5; -.
DR STRING; 9606.ENSP00000360076; -.
DR iPTMnet; Q9BQI5; -.
DR PhosphoSitePlus; Q9BQI5; -.
DR SwissPalm; Q9BQI5; -.
DR BioMuta; SGIP1; -.
DR DMDM; 114152158; -.
DR EPD; Q9BQI5; -.
DR jPOST; Q9BQI5; -.
DR MassIVE; Q9BQI5; -.
DR PaxDb; Q9BQI5; -.
DR PeptideAtlas; Q9BQI5; -.
DR PRIDE; Q9BQI5; -.
DR ProteomicsDB; 78685; -. [Q9BQI5-1]
DR ProteomicsDB; 78686; -. [Q9BQI5-2]
DR ProteomicsDB; 78687; -. [Q9BQI5-3]
DR ProteomicsDB; 78688; -. [Q9BQI5-4]
DR ProteomicsDB; 78689; -. [Q9BQI5-5]
DR Antibodypedia; 51610; 80 antibodies from 19 providers.
DR DNASU; 84251; -.
DR Ensembl; ENST00000237247.10; ENSP00000237247.6; ENSG00000118473.23. [Q9BQI5-3]
DR Ensembl; ENST00000371037.9; ENSP00000360076.3; ENSG00000118473.23. [Q9BQI5-1]
DR Ensembl; ENST00000371039.5; ENSP00000360078.1; ENSG00000118473.23. [Q9BQI5-5]
DR Ensembl; ENST00000683257.1; ENSP00000507967.1; ENSG00000118473.23. [Q9BQI5-4]
DR Ensembl; ENST00000684539.1; ENSP00000507311.1; ENSG00000118473.23. [Q9BQI5-4]
DR Ensembl; ENST00000684664.1; ENSP00000508234.1; ENSG00000118473.23. [Q9BQI5-5]
DR GeneID; 84251; -.
DR KEGG; hsa:84251; -.
DR MANE-Select; ENST00000371037.9; ENSP00000360076.3; NM_032291.4; NP_115667.2.
DR UCSC; uc001dcr.4; human. [Q9BQI5-1]
DR CTD; 84251; -.
DR DisGeNET; 84251; -.
DR GeneCards; SGIP1; -.
DR HGNC; HGNC:25412; SGIP1.
DR HPA; ENSG00000118473; Tissue enriched (retina).
DR MIM; 611540; gene.
DR neXtProt; NX_Q9BQI5; -.
DR OpenTargets; ENSG00000118473; -.
DR PharmGKB; PA134909202; -.
DR VEuPathDB; HostDB:ENSG00000118473; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000156301; -.
DR HOGENOM; CLU_007107_1_0_1; -.
DR InParanoid; Q9BQI5; -.
DR OMA; NWRCELA; -.
DR OrthoDB; 638761at2759; -.
DR PhylomeDB; Q9BQI5; -.
DR TreeFam; TF328986; -.
DR PathwayCommons; Q9BQI5; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9BQI5; -.
DR BioGRID-ORCS; 84251; 14 hits in 1074 CRISPR screens.
DR ChiTaRS; SGIP1; human.
DR GeneWiki; SGIP1; -.
DR GenomeRNAi; 84251; -.
DR Pharos; Q9BQI5; Tbio.
DR PRO; PR:Q9BQI5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BQI5; protein.
DR Bgee; ENSG00000118473; Expressed in stromal cell of endometrium and 129 other tissues.
DR ExpressionAtlas; Q9BQI5; baseline and differential.
DR Genevisible; Q9BQI5; HS.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:2000253; P:positive regulation of feeding behavior; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; ISS:UniProtKB.
DR CDD; cd09266; SGIP1_MHD; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR037984; SGIP1_MHD.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coated pit; Endocytosis; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..828
FT /note="SH3-containing GRB2-like protein 3-interacting
FT protein 1"
FT /id="PRO_0000248395"
FT DOMAIN 559..827
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..567
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000269|PubMed:26822536,
FT ECO:0007744|PDB:5AWU"
FT REGION 593..595
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000269|PubMed:26822536,
FT ECO:0007744|PDB:5AWU"
FT REGION 649..828
FT /note="Necessary and sufficient to mediate interaction with
FT CANX"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT REGION 667..670
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000269|PubMed:26822536,
FT ECO:0007744|PDB:5AWT, ECO:0007744|PDB:5AWU"
FT REGION 813..818
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000269|PubMed:26822536,
FT ECO:0007744|PDB:5AWT, ECO:0007744|PDB:5AWU"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 247
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT VAR_SEQ 34..57
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020273"
FT VAR_SEQ 35..57
FT /note="PSPHEPPYNSKAECAREGGKKVS -> GKKKTQKTQLLLTSCFWLRALSLTL
FT SQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_020274"
FT VAR_SEQ 154..161
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020275"
FT VAR_SEQ 272..438
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020276"
FT VAR_SEQ 437
FT /note="T -> TSDGKTEAQRYQVICPSLQAGGNELDSY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020277"
FT VAR_SEQ 524..543
FT /note="ENEQPSLVWFDRGKFYLTFE -> VSEDDVFYDKLPSFERRCETPA (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020278"
FT VARIANT 112
FT /note="E -> Q (in dbSNP:rs17490057)"
FT /id="VAR_027297"
FT VARIANT 131
FT /note="K -> R (in dbSNP:rs7526812)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2"
FT /id="VAR_027298"
FT VARIANT 161
FT /note="P -> Q (in dbSNP:rs17855645)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027299"
FT VARIANT 575
FT /note="K -> E (in dbSNP:rs17854026)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027300"
FT CONFLICT 81
FT /note="L -> V (in Ref. 3; CAH18344)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="Q -> R (in Ref. 3; CAH18344)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="A -> V (in Ref. 3; CAH18344)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="L -> S (in Ref. 3; CAH18344)"
FT /evidence="ECO:0000305"
FT STRAND 560..575
FT /evidence="ECO:0007829|PDB:5AWS"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 583..597
FT /evidence="ECO:0007829|PDB:5AWS"
FT TURN 599..602
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 612..616
FT /evidence="ECO:0007829|PDB:5AWS"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:5AWS"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:5AWS"
FT HELIX 649..662
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 667..678
FT /evidence="ECO:0007829|PDB:5AWS"
FT HELIX 682..685
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 687..696
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 698..709
FT /evidence="ECO:0007829|PDB:5AWS"
FT HELIX 711..713
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 720..728
FT /evidence="ECO:0007829|PDB:5AWS"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:5AWT"
FT STRAND 733..741
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:5AWS"
FT TURN 747..750
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 751..760
FT /evidence="ECO:0007829|PDB:5AWS"
FT TURN 764..767
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 768..779
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 787..795
FT /evidence="ECO:0007829|PDB:5AWS"
FT STRAND 802..827
FT /evidence="ECO:0007829|PDB:5AWS"
SQ SEQUENCE 828 AA; 89109 MW; 86D2B6AE3099CDEA CRC64;
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGIQPSPHEP PYNSKAECAR EGGKKVSKKS
NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
IKPLQSKDIL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
PTPELISKKP PDDTTALAPL FGPPLESAFD EQKTEVLLDQ PEIWGSGQPI NPSMESPKLT
RPFPTGTPPP LPPKNVPATP PRTGSPLTIG PGNDQSATEV KIEKLPSIND LDSIFGPVLS
PKSVAVNAEE KWVHFSDTSP EHVTPELTPR EKVVSPPATP DNPADSPAPG PLGPPGPTGP
PGPPGPPRNV LSPLNLEEVQ KKVAEQTFIK DDYLETISSP KDFGLGQRAT PPPPPPPTYR
TVVSSPGPGS GPGPGTTSGA SSPARPATPL VPCRSTTPPP PPPRPPSRPK LPPGKPGVGD
VSRPFSPPIH SSSPPPIAPL ARAESTSSIS STNSLSAATT PTVENEQPSL VWFDRGKFYL
TFEGSSRGPS PLTMGAQDTL PVAAAFTETV NAYFKGADPS KCIVKITGEM VLSFPAGITR
HFANNPSPAA LTFRVINFSR LEHVLPNPQL LCCDNTQNDA NTKEFWVNMP NLMTHLKKVS
EQKPQATYYN VDMLKYQVSA QGIQSTPLNL AVNWRCEPSS TDLRIDYKYN TDAMTTAVAL
NNVQFLVPID GGVTKLQAVL PPAVWNAEQQ RILWKIPDIS QKSENGGVGS LLARFQLSEG
PSKPSPLVVQ FTSEGSTLSG CDIELVGAGY RFSLIKKRFA AGKYLADN
