LY9_HUMAN
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 03-AUG-2022, entry version 166.
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}.
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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 BioGRID; 110241; 11.
DR ELM; Q9HBG7; -.
DR IntAct; Q9HBG7; 3.
DR STRING; 9606.ENSP00000263285; -.
DR GlyGen; Q9HBG7; 10 sites, 1 O-linked glycan (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; Q9HBG7; -.
DR PeptideAtlas; Q9HBG7; -.
DR PRIDE; Q9HBG7; -.
DR ProteomicsDB; 81544; -. [Q9HBG7-1]
DR ProteomicsDB; 81545; -. [Q9HBG7-2]
DR ProteomicsDB; 81546; -. [Q9HBG7-3]
DR ProteomicsDB; 81547; -. [Q9HBG7-4]
DR Antibodypedia; 20495; 671 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 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; ICPGPER; -.
DR OrthoDB; 990343at2759; -.
DR PhylomeDB; Q9HBG7; -.
DR TreeFam; TF334964; -.
DR PathwayCommons; Q9HBG7; -.
DR SignaLink; Q9HBG7; -.
DR BioGRID-ORCS; 4063; 9 hits in 1062 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 128 other tissues.
DR ExpressionAtlas; Q9HBG7; baseline and differential.
DR Genevisible; Q9HBG7; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; -; 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 SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
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
