ID LY9_HUMAN Reviewed; 655 AA. AC Q9HBG7; A8K7N3; Q14775; Q5VYI3; Q6P2J4; Q9H4N5; Q9NQ24; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 3. DT 27-MAR-2024, entry version 175. DE RecName: Full=T-lymphocyte surface antigen Ly-9; DE AltName: Full=Cell surface molecule Ly-9; DE AltName: Full=Lymphocyte antigen 9; DE AltName: Full=SLAM family member 3; DE Short=SLAMF3; DE AltName: Full=Signaling lymphocytic activation molecule 3; DE AltName: CD_antigen=CD229; DE Flags: Precursor; GN Name=LY9; ORFNames=CDABP0070; 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 [MRNA] (ISOFORM 1), AND VARIANT VAL-602. RX PubMed=10970093; DOI=10.1007/s002510000209; RA Tovar V., de la Fuente M.A., Pizcueta P., Bosch J., Engel P.; RT "Gene structure of the mouse leukocyte cell surface molecule Ly9."; RL Immunogenetics 51:788-793(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Blood; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 32-654 (ISOFORM 2), AND VARIANT VAL-602. RX PubMed=8537117; DOI=10.1007/bf00186599; RA Sandrin M.S., Henning M.M., Lo M.F., Baker E., Sutherland G.R., RA McKenzie I.F.; RT "Isolation and characterization of cDNA clones for Humly9: the human RT homologue of mouse Ly9."; RL Immunogenetics 43:13-19(1996). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-655 (ISOFORM 3). RC TISSUE=Leukemia; RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., RA Margolin J.F.; RT "Pediatric leukemia cDNA sequencing project."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP INTERACTION WITH SH2D1A AND PTPN11, AND PHOSPHORYLATION. RX PubMed=11389028; DOI=10.1182/blood.v97.12.3867; RA Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P., RA Terhorst C.; RT "Cell surface receptors Ly-9 and CD84 recruit the X-linked RT lymphoproliferative disease gene product SAP."; RL Blood 97:3867-3874(2001). RN [9] RP INTERACTION WITH SH2D1A; SH2D1B AND INPP5D, AND PHOSPHORYLATION AT TYR-603. RX PubMed=12458214; DOI=10.1074/jbc.m206649200; RA Li C., Iosef C., Jia C.Y., Han V.K., Li S.S.; RT "Dual functional roles for the X-linked lymphoproliferative syndrome gene RT product SAP/SH2D1A in signaling through the signaling lymphocyte activation RT molecule (SLAM) family of immune receptors."; RL J. Biol. Chem. 278:3852-3859(2003). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [11] RP FUNCTION. RX PubMed=22989874; DOI=10.1074/jbc.m112.415067; RA Chatterjee M., Hedrich C.M., Rauen T., Ioannidis C., Terhorst C., RA Tsokos G.C.; RT "CD3-T cell receptor co-stimulation through SLAMF3 and SLAMF6 receptors RT enhances RORgammat recruitment to the IL17A promoter in human T RT lymphocytes."; RL J. Biol. Chem. 287:38168-38177(2012). RN [12] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=22184727; DOI=10.4049/jimmunol.1102773; RA Chatterjee M., Rauen T., Kis-Toth K., Kyttaris V.C., Hedrich C.M., RA Terhorst C., Tsokos G.C.; RT "Increased expression of SLAM receptors SLAMF3 and SLAMF6 in systemic lupus RT erythematosus T lymphocytes promotes Th17 differentiation."; RL J. Immunol. 188:1206-1212(2012). RN [13] RP INTERACTION WITH SH2D1A AND INPP5D, CHARACTERIZATION OF VARIANT VAL-602, RP DOMAIN, AND PHOSPHORYLATION AT TYR-603. RX PubMed=26221972; DOI=10.1111/imm.12513; RA Margraf S., Garner L.I., Wilson T.J., Brown M.H.; RT "A polymorphism in a phosphotyrosine signalling motif of CD229 (Ly9, RT SLAMF3) alters SH2 domain binding and T-cell activation."; RL Immunology 146:392-400(2015). CC -!- FUNCTION: Self-ligand receptor of the signaling lymphocytic activation CC molecule (SLAM) family. SLAM receptors triggered by homo- or CC heterotypic cell-cell interactions are modulating the activation and CC differentiation of a wide variety of immune cells and thus are involved CC in the regulation and interconnection of both innate and adaptive CC immune response. Activities are controlled by presence or absence of CC small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. May CC participate in adhesion reactions between T lymphocytes and accessory CC cells by homophilic interaction. Promotes T-cell differentiation into a CC helper T-cell Th17 phenotype leading to increased IL-17 secretion; the CC costimulatory activity requires SH2D1A (PubMed:22184727). Promotes CC recruitment of RORC to the IL-17 promoter (PubMed:22989874). May be CC involved in the maintenance of peripheral cell tolerance by serving as CC a negative regulator of the immune response. May disable autoantibody CC responses and inhibit IFN-gamma secretion by CD4(+) T-cells. May CC negatively regulate the size of thymic innate CD8(+) T-cells and the CC development of invariant natural killer T (iNKT) cells (By similarity). CC {ECO:0000250|UniProtKB:Q01965, ECO:0000269|PubMed:22184727, CC ECO:0000269|PubMed:22989874}. CC -!- SUBUNIT: Interacts with SH2D1A, SH2D1B and INPP5D. Interacts (via CC phosphorylated cytoplasmic domain) with PTPN11; the interaction is CC blocked by SH2D1A. {ECO:0000269|PubMed:11389028, CC ECO:0000269|PubMed:12458214, ECO:0000269|PubMed:26221972}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC Cell membrane {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q9HBG7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9HBG7-2; Sequence=VSP_002525; CC Name=3; CC IsoId=Q9HBG7-3; Sequence=VSP_002524, VSP_002525, VSP_002526; CC Name=4; CC IsoId=Q9HBG7-4; Sequence=VSP_043328; CC -!- TISSUE SPECIFICITY: Increased surface expression on T-cells of systemic CC lupus erythematosus (SLE) patients. {ECO:0000269|PubMed:22184727}. CC -!- DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with CC the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors CC have overlapping specificity for activating and inhibitory SH2 domain- CC containing binding partners. Especially they mediate the interaction CC with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism CC is proposed involving threonine (position -2), phosphorylated tyrosine CC (position 0) and valine/isoleucine (position +3). CC {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:26221972}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF244129; AAG14995.1; -; mRNA. DR EMBL; AK292048; BAF84737.1; -; mRNA. DR EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL354714; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52699.1; -; Genomic_DNA. DR EMBL; BC064485; AAH64485.1; -; mRNA. DR EMBL; L42621; AAA92623.1; -; mRNA. DR EMBL; AY007142; AAG02002.1; -; mRNA. DR CCDS; CCDS30916.1; -. [Q9HBG7-1] DR CCDS; CCDS65695.1; -. [Q9HBG7-2] DR RefSeq; NP_001028839.1; NM_001033667.2. DR RefSeq; NP_001248385.1; NM_001261456.1. [Q9HBG7-2] DR RefSeq; NP_002339.2; NM_002348.3. [Q9HBG7-1] DR AlphaFoldDB; Q9HBG7; -. DR SMR; Q9HBG7; -. DR BioGRID; 110241; 11. DR ELM; Q9HBG7; -. DR IntAct; Q9HBG7; 3. DR STRING; 9606.ENSP00000263285; -. DR GlyCosmos; Q9HBG7; 9 sites, 1 glycan. DR GlyGen; Q9HBG7; 10 sites, 2 O-linked glycans (1 site). DR iPTMnet; Q9HBG7; -. DR PhosphoSitePlus; Q9HBG7; -. DR SwissPalm; Q9HBG7; -. DR BioMuta; LY9; -. DR DMDM; 71152965; -. DR jPOST; Q9HBG7; -. DR MassIVE; Q9HBG7; -. DR MaxQB; Q9HBG7; -. DR PaxDb; 9606-ENSP00000263285; -. DR PeptideAtlas; Q9HBG7; -. DR ProteomicsDB; 81544; -. [Q9HBG7-1] DR ProteomicsDB; 81545; -. [Q9HBG7-2] DR ProteomicsDB; 81546; -. [Q9HBG7-3] DR ProteomicsDB; 81547; -. [Q9HBG7-4] DR Antibodypedia; 20495; 708 antibodies from 39 providers. DR DNASU; 4063; -. DR Ensembl; ENST00000263285.11; ENSP00000263285.5; ENSG00000122224.18. [Q9HBG7-1] DR Ensembl; ENST00000368037.9; ENSP00000357016.5; ENSG00000122224.18. [Q9HBG7-2] DR GeneID; 4063; -. DR KEGG; hsa:4063; -. DR MANE-Select; ENST00000263285.11; ENSP00000263285.5; NM_002348.4; NP_002339.2. DR UCSC; uc001fwt.5; human. [Q9HBG7-1] DR AGR; HGNC:6730; -. DR CTD; 4063; -. DR DisGeNET; 4063; -. DR GeneCards; LY9; -. DR HGNC; HGNC:6730; LY9. DR HPA; ENSG00000122224; Tissue enhanced (bone marrow, intestine, lymphoid tissue). DR MIM; 600684; gene. DR neXtProt; NX_Q9HBG7; -. DR OpenTargets; ENSG00000122224; -. DR PharmGKB; PA30494; -. DR VEuPathDB; HostDB:ENSG00000122224; -. DR eggNOG; ENOG502SGRG; Eukaryota. DR GeneTree; ENSGT01030000234540; -. DR HOGENOM; CLU_035502_0_0_1; -. DR InParanoid; Q9HBG7; -. DR OMA; IEHITWS; -. DR OrthoDB; 4608679at2759; -. DR PhylomeDB; Q9HBG7; -. DR TreeFam; TF334964; -. DR PathwayCommons; Q9HBG7; -. DR SignaLink; Q9HBG7; -. DR BioGRID-ORCS; 4063; 9 hits in 1142 CRISPR screens. DR ChiTaRS; LY9; human. DR GeneWiki; LY9; -. DR GenomeRNAi; 4063; -. DR Pharos; Q9HBG7; Tbio. DR PRO; PR:Q9HBG7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9HBG7; Protein. DR Bgee; ENSG00000122224; Expressed in granulocyte and 129 other cell types or tissues. DR ExpressionAtlas; Q9HBG7; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:UniProtKB. DR GO; GO:0042110; P:T cell activation; IBA:GO_Central. DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; IDA:UniProtKB. DR CDD; cd16842; Ig_SLAM-like_N; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR PANTHER; PTHR12080:SF114; T-LYMPHOCYTE SURFACE ANTIGEN LY-9; 1. DR SMART; SM00409; IG; 2. DR SUPFAM; SSF48726; Immunoglobulin; 4. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; Q9HBG7; HS. PE 1: Evidence at protein level; KW Adaptive immunity; Alternative splicing; Cell adhesion; Cell membrane; KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; KW Innate immunity; Membrane; Phosphoprotein; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..47 FT /evidence="ECO:0000255" FT CHAIN 48..655 FT /note="T-lymphocyte surface antigen Ly-9" FT /id="PRO_0000014851" FT TOPO_DOM 48..454 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 455..476 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 477..655 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 48..158 FT /note="Ig-like V-type 1" FT DOMAIN 159..235 FT /note="Ig-like C2-type 1" FT DOMAIN 251..363 FT /note="Ig-like V-type 2" FT DOMAIN 364..452 FT /note="Ig-like C2-type 2" FT REGION 521..556 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 633..655 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 601..606 FT /note="ITSM 1" FT /evidence="ECO:0000250|UniProtKB:Q13291" FT MOTIF 624..629 FT /note="ITSM 2" FT /evidence="ECO:0000250|UniProtKB:Q13291" FT COMPBIAS 525..539 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 542..556 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 603 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:12458214, FT ECO:0000305|PubMed:26221972" FT CARBOHYD 68 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 95 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 120 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 169 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 173 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 413 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 424 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 172..242 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 178..222 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 377..446 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 383..427 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 152..193 FT /note="EQLQEPQVTMKSVKVSENFSCNITLMCSVKGAEKSVLYSWTP -> APFIEK FT LSVHVIEGDHRTLLEGSGLESIISTLAEPRVSVREG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043328" FT VAR_SEQ 359..448 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_002524" FT VAR_SEQ 500..513 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:8537117, ECO:0000303|Ref.7" FT /id="VSP_002525" FT VAR_SEQ 524..554 FT /note="PARQQPTPTSDSSSDSNLTTEEDEDRPEVHK -> Q (in isoform 3)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_002526" FT VARIANT 602 FT /note="M -> V (decreases interaction with SH2D1A and INPP5D FT 2-fold, reduced T-cell response; dbSNP:rs509749)" FT /evidence="ECO:0000269|PubMed:10970093, FT ECO:0000269|PubMed:26221972, ECO:0000269|PubMed:8537117" FT /id="VAR_033612" FT CONFLICT 171 FT /note="Missing (in Ref. 1; AAG14995)" FT /evidence="ECO:0000305" SQ SEQUENCE 655 AA; 72139 MW; 84ABA3056D69E80A CRC64; MVAPKSHTDD WAPGPFSSKP QRSQLQIFSS VLQTSLLFLL MGLRASGKDS APTVVSGILG GSVTLPLNIS VDTEIENVIW IGPKNALAFA RPKENVTIMV KSYLGRLDIT KWSYSLCISN LTLNDAGSYK AQINQRNFEV TTEEEFTLFV YEQLQEPQVT MKSVKVSENF SCNITLMCSV KGAEKSVLYS WTPREPHASE SNGGSILTVS RTPCDPDLPY ICTAQNPVSQ RSSLPVHVGQ FCTDPGASRG GTTGETVVGV LGEPVTLPLA LPACRDTEKV VWLFNTSIIS KEREEAATAD PLIKSRDPYK NRVWVSSQDC SLKISQLKIE DAGPYHAYVC SEASSVTSMT HVTLLIYRRL RKPKITWSLR HSEDGICRIS LTCSVEDGGN TVMYTWTPLQ KEAVVSQGES HLNVSWRSSE NHPNLTCTAS NPVSRSSHQF LSENICSGPE RNTKLWIGLF LMVCLLCVGI FSWCIWKRKG RCSVPAFCSS QAEAPADTPE PTAGHTLYSV LSQGYEKLDT PLRPARQQPT PTSDSSSDSN LTTEEDEDRP EVHKPISGRY EVFDQVTQEG AGHDPAPEGQ ADYDPVTPYV TEVESVVGEN TMYAQVFNLQ GKTPVSQKEE SSATIYCSIR KPQVVPPPQQ NDLEIPESPT YENFT //