SHPS1_MOUSE
ID SHPS1_MOUSE Reviewed; 513 AA.
AC P97797; A0A0R4J1Z7; E0CYM8; E9QPT7; O08907; O35924; O88555; O88556; P97796;
AC Q8R559; Q9QX57; Q9WTN4;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type substrate 1;
DE Short=SHP substrate 1;
DE Short=SHPS-1;
DE AltName: Full=Brain Ig-like molecule with tyrosine-based activation motifs;
DE Short=Bit;
DE AltName: Full=CD172 antigen-like family member A;
DE AltName: Full=Inhibitory receptor SHPS-1;
DE AltName: Full=MyD-1 antigen;
DE AltName: Full=Signal-regulatory protein alpha-1;
DE Short=Sirp-alpha-1;
DE Short=mSIRP-alpha1;
DE AltName: Full=p84;
DE AltName: CD_antigen=CD172a;
DE Flags: Precursor;
GN Name=Sirpa; Synonyms=Bit, Myd1, Ptpns1, Shps1, Sirp;
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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=9070220; DOI=10.1006/bbrc.1996.6047;
RA Yamao T., Matozaki T., Amano K., Matsuda Y., Takahashi N., Ochi F.,
RA Fujioka Y., Kasuga M.;
RT "Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal
RT localization of genes.";
RL Biochem. Biophys. Res. Commun. 231:61-67(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9073522; DOI=10.1006/geno.1996.4581;
RA Ohnishi H., Kubota M., Sano S.;
RT "BIT (Bit) maps to mouse chromosome 2.";
RL Genomics 40:504-506(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), PROTEIN SEQUENCE OF 32-53
RP AND 422-433 (ISOFORM 2), GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain, and Cerebellum;
RX PubMed=9348339; DOI=10.1523/jneurosci.17-22-08702.1997;
RA Comu S., Weng W., Olinsky S., Ishwad P., Mi Z., Hempel J., Watkins S.,
RA Lagenaur C.F., Narayanan V.;
RT "The murine P84 neural adhesion molecule is SHPS-1, a member of the
RT phosphatase-binding protein family.";
RL J. Neurosci. 17:8702-8710(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), GLYCOSYLATION,
RP PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH PTPN6, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Fetal thymus;
RX PubMed=9712903; DOI=10.1074/jbc.273.35.22719;
RA Veillette A., Thibaudeau E., Latour S.;
RT "High expression of inhibitory receptor SHPS-1 and its association with
RT protein tyrosine phosphatase SHP-1 in macrophages.";
RL J. Biol. Chem. 273:22719-22728(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND
RP GLYCOSYLATION.
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Brain, and Liver;
RX PubMed=10585853; DOI=10.1042/bj3440667;
RA Sano S., Ohnishi H., Kubota M.;
RT "Gene structure of mouse BIT/SHPS-1.";
RL Biochem. J. 344:667-675(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Wang H., Chen Z., Ullrich A.;
RT "Epidermal growth factor-induced association of SHP2 with mouse SIRP-
RT alpha1.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=2303162; DOI=10.1016/0012-1606(90)90249-i;
RA Chuang W., Lagenaur C.F.;
RT "Central nervous system antigen P84 can serve as a substrate for neurite
RT outgrowth.";
RL Dev. Biol. 137:219-232(1990).
RN [11]
RP GLYCOSYLATION, PHOSPHORYLATION BY JAK2 IN RESPONSE TO GROWTH HORMONE, AND
RP INTERACTION WITH JAK2 AND PTPN11.
RX PubMed=9507023; DOI=10.1074/jbc.273.12.7112;
RA Stofega M.R., Wang H., Ullrich A., Carter-Su C.;
RT "Growth hormone regulation of SIRP and SHP-2 tyrosyl phosphorylation and
RT association.";
RL J. Biol. Chem. 273:7112-7117(1998).
RN [12]
RP INTERACTION WITH CD47, AND TISSUE SPECIFICITY.
RX PubMed=9872987; DOI=10.1074/jbc.274.2.559;
RA Jiang P., Lagenaur C.F., Narayanan V.;
RT "Integrin-associated protein is a ligand for the P84 neural adhesion
RT molecule.";
RL J. Biol. Chem. 274:559-562(1999).
RN [13]
RP INTERACTION WITH FGR.
RX PubMed=10662797; DOI=10.1084/jem.191.3.515;
RA Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M., Lowell C.A.,
RA Lagenaur C.F., Willman C.L.;
RT "Negative regulation of phagocytosis in murine macrophages by the Src
RT kinase family member, Fgr.";
RL J. Exp. Med. 191:515-528(2000).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as
CC docking protein and induces translocation of PTPN6, PTPN11 and other
CC binding partners from the cytosol to the plasma membrane. Supports
CC adhesion of cerebellar neurons, neurite outgrowth and glial cell
CC attachment. May play a key role in intracellular signaling during
CC synaptogenesis and in synaptic function. Involved in the negative
CC regulation of receptor tyrosine kinase-coupled cellular responses
CC induced by cell adhesion, growth factors or insulin. Mediates negative
CC regulation of phagocytosis, mast cell activation and dendritic cell
CC activation. CD47 binding prevents maturation of immature dendritic
CC cells and inhibits cytokine production by mature dendritic cells (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:2303162}.
CC -!- SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in
CC macrophages, where it primarily binds PTPN6. Binds GRB2 vitro. Binds
CC FGR. Binds JAK2 irrespective of its phosphorylation status and forms a
CC stable complex. Binds SCAP1 and/or SCAP2. The resulting complex
CC recruits FYB1. Binds PTK2B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=a;
CC IsoId=P97797-1; Sequence=Displayed;
CC Name=2; Synonyms=a', Large;
CC IsoId=P97797-2; Sequence=VSP_007032;
CC Name=3; Synonyms=b, Small;
CC IsoId=P97797-3; Sequence=VSP_007031;
CC Name=4;
CC IsoId=P97797-4; Sequence=VSP_007031, VSP_007032;
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebral cortex, brain, spinal
CC cord, cerebellum and spleen, and at much lower levels in kidney,
CC thymus, heart, lung and liver. Within the cerebellum, highly expressed
CC throughout the molecular layer, and in synaptic glomeruli in the
CC granule cell layer. Detected in neurons of the hippocampus and dentate
CC gyrus, and in olfactory bulb. Not detected in Purkinje cells. Highly
CC expressed in the plexiform layers, optic fiber layer and the outer
CC segments of the photoreceptor layer in the retina. Highly expressed in
CC macrophages. Isoform 3 is detected at very low levels in all tissues
CC tested. {ECO:0000269|PubMed:2303162, ECO:0000269|PubMed:9348339,
CC ECO:0000269|PubMed:9712903, ECO:0000269|PubMed:9872987}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the CNS of embryos from day 7
CC to 17. {ECO:0000269|PubMed:2303162}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10585853,
CC ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:9348339,
CC ECO:0000269|PubMed:9507023, ECO:0000269|PubMed:9712903}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:9507023,
CC ECO:0000269|PubMed:9712903}.
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DR EMBL; D87967; BAA13520.1; -; mRNA.
DR EMBL; D87968; BAA13521.1; -; mRNA.
DR EMBL; D85785; BAA20376.1; -; mRNA.
DR EMBL; U89694; AAB92591.1; -; mRNA.
DR EMBL; AF072543; AAC24886.1; -; mRNA.
DR EMBL; AF072544; AAC24887.1; -; mRNA.
DR EMBL; AB024507; BAA89290.1; -; Genomic_DNA.
DR EMBL; AB018194; BAA76555.1; -; mRNA.
DR EMBL; AB024507; BAA89289.1; -; Genomic_DNA.
DR EMBL; AF332079; AAK56107.1; -; mRNA.
DR EMBL; AF332080; AAK56108.1; -; mRNA.
DR EMBL; Y10349; CAA71375.1; -; mRNA.
DR EMBL; AL808126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28242.1; -; Genomic_DNA.
DR CCDS; CCDS16729.1; -. [P97797-2]
DR CCDS; CCDS50708.1; -. [P97797-4]
DR CCDS; CCDS71142.1; -. [P97797-1]
DR CCDS; CCDS71143.1; -. [P97797-3]
DR PIR; JC5288; JC5288.
DR PIR; JC5289; JC5289.
DR RefSeq; NP_001171118.1; NM_001177647.2. [P97797-4]
DR RefSeq; NP_001277948.1; NM_001291019.1. [P97797-1]
DR RefSeq; NP_001277949.1; NM_001291020.1. [P97797-1]
DR RefSeq; NP_001277950.1; NM_001291021.1. [P97797-3]
DR RefSeq; NP_031573.2; NM_007547.4. [P97797-2]
DR RefSeq; XP_006499049.1; XM_006498986.3. [P97797-1]
DR RefSeq; XP_017172050.1; XM_017316561.1.
DR RefSeq; XP_017172057.1; XM_017316568.1. [P97797-3]
DR RefSeq; XP_017172058.1; XM_017316569.1. [P97797-4]
DR PDB; 2YZ1; X-ray; 1.40 A; A/B=32-146.
DR PDBsum; 2YZ1; -.
DR AlphaFoldDB; P97797; -.
DR SMR; P97797; -.
DR BioGRID; 202490; 12.
DR CORUM; P97797; -.
DR IntAct; P97797; 4.
DR STRING; 10090.ENSMUSP00000099491; -.
DR GlyConnect; 2714; 29 N-Linked glycans (13 sites).
DR GlyGen; P97797; 17 sites, 28 N-linked glycans (13 sites).
DR iPTMnet; P97797; -.
DR PhosphoSitePlus; P97797; -.
DR jPOST; P97797; -.
DR MaxQB; P97797; -.
DR PaxDb; P97797; -.
DR PeptideAtlas; P97797; -.
DR PRIDE; P97797; -.
DR ProteomicsDB; 261353; -. [P97797-1]
DR ProteomicsDB; 261354; -. [P97797-2]
DR ProteomicsDB; 261355; -. [P97797-3]
DR ProteomicsDB; 328968; -.
DR ProteomicsDB; 339176; -.
DR ProteomicsDB; 367856; -.
DR ABCD; P97797; 27 sequenced antibodies.
DR DNASU; 19261; -.
DR Ensembl; ENSMUST00000049262; ENSMUSP00000049022; ENSMUSG00000037902. [P97797-1]
DR Ensembl; ENSMUST00000099113; ENSMUSP00000096713; ENSMUSG00000037902. [P97797-3]
DR Ensembl; ENSMUST00000103202; ENSMUSP00000099491; ENSMUSG00000037902. [P97797-2]
DR Ensembl; ENSMUST00000103203; ENSMUSP00000099492; ENSMUSG00000037902. [P97797-2]
DR Ensembl; ENSMUST00000160276; ENSMUSP00000125004; ENSMUSG00000037902. [P97797-4]
DR Ensembl; ENSMUST00000161620; ENSMUSP00000124048; ENSMUSG00000037902. [P97797-1]
DR Ensembl; ENSMUST00000179001; ENSMUSP00000137611; ENSMUSG00000037902. [P97797-2]
DR GeneID; 19261; -.
DR KEGG; mmu:19261; -.
DR UCSC; uc008mhz.1; mouse.
DR CTD; 140885; -.
DR MGI; MGI:108563; Sirpa.
DR VEuPathDB; HostDB:ENSMUSG00000037902; -.
DR eggNOG; ENOG502S1XD; Eukaryota.
DR GeneTree; ENSGT00960000186656; -.
DR HOGENOM; CLU_044430_2_0_1; -.
DR InParanoid; P97797; -.
DR OMA; DNTETHN; -.
DR OrthoDB; 904196at2759; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-2172127; DAP12 interactions.
DR Reactome; R-MMU-391160; Signal regulatory protein family interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 19261; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Sirpa; mouse.
DR EvolutionaryTrace; P97797; -.
DR PRO; PR:P97797; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P97797; protein.
DR Bgee; ENSMUSG00000037902; Expressed in stroma of bone marrow and 266 other tissues.
DR ExpressionAtlas; P97797; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; ISO:MGI.
DR GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR GO; GO:0045309; F:protein phosphorylated amino acid binding; IPI:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:ARUK-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR GO; GO:0097530; P:granulocyte migration; IGI:ARUK-UCL.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0035696; P:monocyte extravasation; ISO:MGI.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; IMP:ARUK-UCL.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:ARUK-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:ARUK-UCL.
DR GO; GO:1903720; P:negative regulation of I-kappaB phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:ARUK-UCL.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:ARUK-UCL.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:ARUK-UCL.
DR GO; GO:0071641; P:negative regulation of macrophage inflammatory protein 1 alpha production; IMP:ARUK-UCL.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IMP:ARUK-UCL.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:ARUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:ARUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0032675; P:regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 2.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00407; IGc1; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3-binding; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT CHAIN 32..513
FT /note="Tyrosine-protein phosphatase non-receptor type
FT substrate 1"
FT /id="PRO_0000014942"
FT TOPO_DOM 32..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..137
FT /note="Ig-like V-type"
FT DOMAIN 149..248
FT /note="Ig-like C1-type 1"
FT DOMAIN 255..343
FT /note="Ig-like C1-type 2"
FT REGION 444..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 440..443
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 450..455
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 464..467
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 481..484
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 505..508
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 440
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000255"
FT MOD_RES 464
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000255"
FT MOD_RES 481
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P97710"
FT MOD_RES 505
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P97710"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 171..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 274..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 147..364
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585853,
FT ECO:0000303|PubMed:9348339, ECO:0000303|PubMed:9712903"
FT /id="VSP_007031"
FT VAR_SEQ 425..428
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585853,
FT ECO:0000303|PubMed:9070220, ECO:0000303|PubMed:9073522,
FT ECO:0000303|PubMed:9348339, ECO:0000303|PubMed:9712903"
FT /id="VSP_007032"
FT CONFLICT 6
FT /note="Missing (in Ref. 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="R -> L (in Ref. 3; AAB92591)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="A -> V (in Ref. 1; BAA13520/BAA13521, 5; BAA89289/
FT BAA89290, 6; AAK56107 and 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="K -> T (in Ref. 2; BAA20376)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="L -> V (in Ref. 2; BAA20376)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="V -> I (in Ref. 2; BAA20376)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> V (in Ref. 2; BAA20376)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="R -> K (in Ref. 1; BAA13520/BAA13521, 3; AAB92591,
FT 5; BAA89289/BAA89290, 6; AAK56107 and 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..77
FT /note="PSRL -> KAGC (in Ref. 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="P -> Q (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290 and 6; AAK56107)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> T (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="Y -> H (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="V -> F (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> V (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="R -> T (in Ref. 1; BAA13520/BAA13521, 5; BAA89289/
FT BAA89290, 6; AAK56107 and 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="T -> A (in Ref. 1; BAA13520/BAA13521, 5; BAA89289/
FT BAA89290, 6; AAK56107 and 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="A -> E (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="I -> T (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="K -> R (in Ref. 2; BAA20376 and 3; AAB92591)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="S -> P (in Ref. 1; BAA13520/BAA13521, 5; BAA89289/
FT BAA89290, 6; AAK56107 and 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..156
FT /note="VSG -> YPV (in Ref. 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="D -> Y (in Ref. 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> H (in Ref. 1; BAA13520/BAA13521, 3; AAB92591,
FT 5; BAA89289/BAA89290 and 6; AAK56107)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="N -> H (in Ref. 1; BAA13520/BAA13521, 3; AAB92591,
FT 5; BAA89289/BAA89290, 6; AAK56107 and 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> P (in Ref. 2; BAA20376)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> D (in Ref. 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="F -> L (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> G (in Ref. 1; BAA13520/BAA13521, 2; BAA20376,
FT 3; AAB92591, 5; BAA89289/BAA89290, 6; AAK56107 and 7;
FT CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..458
FT /note="EKKPAPRAPEP -> RRKPAPGSLEFL (in Ref. 7; CAA71375)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="S -> N (in Ref. 2; BAA20376 and 3; AAB92591)"
FT /evidence="ECO:0000305"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2YZ1"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2YZ1"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:2YZ1"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2YZ1"
SQ SEQUENCE 513 AA; 56414 MW; F3C483B0DC99BD9A CRC64;
MEPAGPAPGR LGPLLLCLLL SASCFCTGAT GKELKVTQPE KSVSVAAGDS TVLNCTLTSL
LPVGPIRWYR GVGPSRLLIY SFAGEYVPRI RNVSDTTKRN NMDFSIRISN VTPADAGIYY
CVKFQKGSSE PDTEIQSGGG TEVYVLAKPS PPEVSGPADR GIPDQKVNFT CKSHGFSPRN
ITLKWFKDGQ ELHPLETTVN PSGKNVSYNI SSTVRVVLNS MDVNSKVICE VAHITLDRSP
LRGIANLSNF IRVSPTVKVT QQSPTSMNQV NLTCRAERFY PEDLQLIWLE NGNVSRNDTP
KNLTKNTDGT YNYTSLFLVN SSAHREDVVF TCQVKHDQQP AITRNHTVLG FAHSSDQGSM
QTFPDNNATH NWNVFIGVGV ACALLVVLLM AALYLLRIKQ KKAKGSTSST RLHEPEKNAR
EITQVQSLIQ DTNDINDITY ADLNLPKEKK PAPRAPEPNN HTEYASIETG KVPRPEDTLT
YADLDMVHLS RAQPAPKPEP SFSEYASVQV QRK
