SLAF1_MOUSE
ID SLAF1_MOUSE Reviewed; 343 AA.
AC Q9QUM4; Q9QXZ3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Signaling lymphocytic activation molecule;
DE AltName: Full=SLAM family member 1;
DE AltName: CD_antigen=CD150;
DE Flags: Precursor;
GN Name=Slamf1; Synonyms=Slam;
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 LONG AND SHORT).
RC STRAIN=BALB/cJ;
RX PubMed=10570270;
RA Castro A.G., Hauser T.M., Cocks B.G., Abrams J., Zurawski S., Churakova T.,
RA Zonin F., Robinson D., Tangye S.G., Aversa G., Nichols K.E., de Vries J.E.,
RA Lanier L.L., O'Garra A.;
RT "Molecular and functional characterization of mouse signaling lymphocytic
RT activation molecule (SLAM): differential expression and responsiveness in
RT Th1 and Th2 cells.";
RL J. Immunol. 163:5860-5870(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND FUNCTION.
RX PubMed=15123745; DOI=10.1084/jem.20031835;
RA Wang N., Satoskar A., Faubion W., Howie D., Okamoto S., Feske S., Gullo C.,
RA Clarke K., Sosa M.R., Sharpe A.H., Terhorst C.;
RT "The cell surface receptor SLAM controls T cell and macrophage functions.";
RL J. Exp. Med. 199:1255-1264(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Wu C., Wang N., Sayos J., Terhorst C.;
RT "Genomic organization of murine Slam.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=9126961;
RA Aversa G., Chang C.C., Carballido J.M., Cocks B.G., de Vries J.E.;
RT "Engagement of the signaling lymphocytic activation molecule (SLAM) on
RT activated T cells results in IL-2-independent, cyclosporin A-sensitive T
RT cell proliferation and IFN-gamma production.";
RL J. Immunol. 158:4036-4044(1997).
RN [5]
RP INTERACTION WITH SH2D1A.
RX PubMed=9774102; DOI=10.1038/26683;
RA Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S.,
RA Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E.,
RA Aversa G., Terhorst C.;
RT "The X-linked lymphoproliferative-disease gene product SAP regulates
RT signals induced through the co-receptor SLAM.";
RL Nature 395:462-469(1998).
RN [6]
RP INTERACTION WITH SH2D1B.
RX PubMed=11689425; DOI=10.1093/emboj/20.21.5840;
RA Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C., Howie D.,
RA Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B., Engel P.,
RA Eck M.J., Terhorst C.;
RT "Structural basis for the interaction of the free SH2 domain EAT-2 with
RT SLAM receptors in hematopoietic cells.";
RL EMBO J. 20:5840-5852(2001).
RN [7]
RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH SH2D1A AND FYN, AND MUTAGENESIS
RP OF TYR-288; TYR-315 AND TYR-335.
RX PubMed=11477403; DOI=10.1038/90615;
RA Latour S., Gish G., Helgason C.D., Humphries R.K., Pawson T., Veillette A.;
RT "Regulation of SLAM-mediated signal transduction by SAP, the X-linked
RT lymphoproliferative gene product.";
RL Nat. Immunol. 2:681-690(2001).
RN [8]
RP FUNCTION.
RX PubMed=12351401; DOI=10.1182/blood-2002-02-0445;
RA Howie D., Okamoto S., Rietdijk S., Clarke K., Wang N., Gullo C.,
RA Bruggeman J.P., Manning S., Coyle A.J., Greenfield E., Kuchroo V.,
RA Terhorst C.;
RT "The role of SAP in murine CD150 (SLAM)-mediated T-cell proliferation and
RT interferon gamma production.";
RL Blood 100:2899-2907(2002).
RN [9]
RP FUNCTION.
RX PubMed=15315965; DOI=10.1182/blood-2004-04-1273;
RA Mikhalap S.V., Shlapatska L.M., Yurchenko O.V., Yurchenko M.Y.,
RA Berdova G.G., Nichols K.E., Clark E.A., Sidorenko S.P.;
RT "The adaptor protein SH2D1A regulates signaling through CD150 (SLAM) in B
RT cells.";
RL Blood 104:4063-4070(2004).
RN [10]
RP FUNCTION.
RX PubMed=15539155; DOI=10.1016/j.immuni.2004.09.012;
RA Cannons J.L., Yu L.J., Hill B., Mijares L.A., Dombroski D., Nichols K.E.,
RA Antonellis A., Koretzky G.A., Gardner K., Schwartzberg P.L.;
RT "SAP regulates T(H)2 differentiation and PKC-theta-mediated activation of
RT NF-kappaB1.";
RL Immunity 21:693-706(2004).
RN [11]
RP FUNCTION.
RX PubMed=16528012; DOI=10.1165/rcmb.2005-0294oc;
RA Wang N., Campo M., Ting L., Fleming C., Terhorst C., Finn P.W.;
RT "The costimulatory molecule SLAM is critical for pulmonary allergic
RT responses.";
RL Am. J. Respir. Cell Mol. Biol. 35:206-210(2006).
RN [12]
RP INTERACTION WITH SH2D1A AND FYN.
RX PubMed=16847311; DOI=10.1128/mcb.00357-06;
RA Chen R., Latour S., Shi X., Veillette A.;
RT "Association between SAP and FynT: Inducible SH3 domain-mediated
RT interaction controlled by engagement of the SLAM receptor.";
RL Mol. Cell. Biol. 26:5559-5568(2006).
RN [13]
RP FUNCTION.
RX PubMed=18031695; DOI=10.1016/j.immuni.2007.08.020;
RA Griewank K., Borowski C., Rietdijk S., Wang N., Julien A., Wei D.G.,
RA Mamchak A.A., Terhorst C., Bendelac A.;
RT "Homotypic interactions mediated by Slamf1 and Slamf6 receptors control NKT
RT cell lineage development.";
RL Immunity 27:751-762(2007).
RN [14]
RP FUNCTION.
RX PubMed=18606638; DOI=10.4049/jimmunol.181.2.869;
RA Baev D.V., Caielli S., Ronchi F., Coccia M., Facciotti F., Nichols K.E.,
RA Falcone M.;
RT "Impaired SLAM-SLAM homotypic interaction between invariant NKT cells and
RT dendritic cells affects differentiation of IL-4/IL-10-secreting NKT2 cells
RT in nonobese diabetic mice.";
RL J. Immunol. 181:869-877(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [16]
RP FUNCTION.
RX PubMed=20525889; DOI=10.4049/jimmunol.0903505;
RA Yusuf I., Kageyama R., Monticelli L., Johnston R.J., Ditoro D., Hansen K.,
RA Barnett B., Crotty S.;
RT "Germinal center T follicular helper cell IL-4 production is dependent on
RT signaling lymphocytic activation molecule receptor (CD150).";
RL J. Immunol. 185:190-202(2010).
RN [17]
RP FUNCTION.
RX PubMed=20818396; DOI=10.1038/ni.1931;
RA Berger S.B., Romero X., Ma C., Wang G., Faubion W.A., Liao G., Compeer E.,
RA Keszei M., Rameh L., Wang N., Boes M., Regueiro J.R., Reinecker H.C.,
RA Terhorst C.;
RT "SLAM is a microbial sensor that regulates bacterial phagosome functions in
RT macrophages.";
RL Nat. Immunol. 11:920-927(2010).
RN [18]
RP FUNCTION, AND INTERACTION WITH PIK3C3; BECN1 AND UVRAG.
RX PubMed=22493499; DOI=10.1074/jbc.m112.367060;
RA Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.;
RT "Receptor signaling lymphocyte-activation molecule family 1 (Slamf1)
RT regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by recruiting
RT a Beclin-1/Vps34/ultraviolet radiation resistance-associated gene (UVRAG)
RT complex.";
RL J. Biol. Chem. 287:18359-18365(2012).
RN [19]
RP FUNCTION.
RX PubMed=25926831; DOI=10.3389/fimmu.2015.00158;
RA Wang N., Halibozek P.J., Yigit B., Zhao H., O'Keeffe M.S., Sage P.,
RA Sharpe A., Terhorst C.;
RT "Negative regulation of humoral immunity due to interplay between the
RT SLAMF1, SLAMF5, and SLAMF6 receptors.";
RL Front. Immunol. 6:158-158(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.
CC SLAMF1-induced signal-transduction events in T-lymphocytes are
CC different from those in B-cells. Two modes of SLAMF1 signaling seem to
CC exist: one depending on SH2D1A (and perhaps SH2D1B) and another in
CC which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal
CC transduction operates. Initially it has been proposed that association
CC with SH2D1A prevents binding to inhibitory effectors including
CC INPP5D/SHIP1 and PTPN11/SHP-2 (By similarity). However, signaling is
CC also regulated by SH2D1A which can simultaneously interact with and
CC recruit FYN which subsequently phosphorylates and activates SLAMF1 (By
CC similarity). Mediates IL-2-independent proliferation of activated T-
CC cells during immune responses and induces IFN-gamma production
CC (PubMed:9126961, PubMed:12351401). Downstreaming signaling involves
CC INPP5D, DOK1 and DOK2 leading to inhibited IFN-gamma production in T-
CC cells, and PRKCQ, BCL10 and NFKB1 leading to increased T-cell
CC activation and Th2 cytokine production (PubMed:11477403,
CC PubMed:16847311, PubMed:15539155). Promotes T-cell receptor-induced IL-
CC 4 secretion by CD4(+) cells (PubMed:15123745). Inhibits antigen
CC receptor-mediated production of IFN-gamma, but not IL-2, in
CC CD4(-)/CD8(-) T-cells (PubMed:11477403). Required for IL-4 production
CC by germinal centers T follicular helper (T(Fh))cells (PubMed:20525889).
CC May inhibit CD40-induced signal transduction in monocyte-derived
CC dendritic cells (By similarity). May play a role in allergic responses
CC and may regulate allergen-induced Th2 cytokine and Th1 cytokine
CC secretion (PubMed:16528012). In conjunction with SLAMF6 controls the
CC transition between positive selection and the subsequent expansion and
CC differentiation of the thymocytic natural killer T (NKT) cell lineage
CC (PubMed:18031695). Involved in the peripheral differentiation of
CC indifferent natural killer T (iNKT) cells toward a regulatory NKT2 type
CC (PubMed:18606638). In macrophages involved in down-regulation of IL-12,
CC TNF-alpha and nitric oxide in response to lipopolysaccharide (LPS)
CC (PubMed:15123745). In B-cells activates the ERK signaling pathway
CC independently of SH2D1A but implicating both, SYK and INPP5D, and
CC activates Akt signaling dependent on SYK and SH2D1A (PubMed:15315965).
CC In conjunction with CD84/SLAMF5 and SLAMF6 may be a negative regulator
CC of the humoral immune response (PubMed:25926831).
CC {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403,
CC ECO:0000269|PubMed:15123745, ECO:0000269|PubMed:15315965,
CC ECO:0000269|PubMed:15539155, ECO:0000269|PubMed:16528012,
CC ECO:0000269|PubMed:16847311, ECO:0000269|PubMed:18031695,
CC ECO:0000269|PubMed:18606638, ECO:0000269|PubMed:25926831,
CC ECO:0000269|PubMed:9126961}.
CC -!- FUNCTION: (Microbial infection) Involved in innate immune response
CC against Gram-negative bacteria in macrophages; probably recognizes OmpC
CC and/or OmpF on the bacterial surface, regulates phagosome maturation
CC and recruitment of the PI3K complex II (PI3KC3-C2) leading to
CC accumulated of PdtIns(3)P and NOX2 activity in the phagosomes
CC (PubMed:20818396, PubMed:22493499). {ECO:0000269|PubMed:20818396,
CC ECO:0000305|PubMed:22493499}.
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with SH2D1A and SH2D1B;
CC SH2D1A mediates association with FYN; SH2D1A binds to phosphorylated
CC and not phosphorylated ITSM 1 (PubMed:9774102, PubMed:16847311,
CC PubMed:11477403.) Interacts (via cytoplasmic domain phosphorylated on
CC tyrosine residues) with INPP5D and PTPN11; presence of SH2D1A
CC facilitates binding to INPP5D (By similarity). Interacts with MAP4K1
CC (By similarity). Interacts with PIK3C3, BECN1 and UVRAG; indicative for
CC an association with PI3K complex II (PI3KC3-C2) (PubMed:22493499).
CC {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403,
CC ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:16847311,
CC ECO:0000269|PubMed:20525889, ECO:0000269|PubMed:22493499,
CC ECO:0000269|PubMed:9774102}.
CC -!- INTERACTION:
CC Q9QUM4; P39688: Fyn; NbExp=4; IntAct=EBI-7910086, EBI-524514;
CC Q9QUM4; O88890: Sh2d1a; NbExp=3; IntAct=EBI-7910086, EBI-7910438;
CC Q9QUM4; Q14457: BECN1; Xeno; NbExp=8; IntAct=EBI-7910086, EBI-949378;
CC Q9QUM4; Q9P2Y5: UVRAG; Xeno; NbExp=6; IntAct=EBI-7910086, EBI-2952704;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13291};
CC Single-pass type I membrane protein. Note=Present on the surface of B-
CC cells and T-cells. Located at the plasma membrane contacts between
CC neighboring T cells. {ECO:0000250|UniProtKB:Q13291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9QUM4-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9QUM4-2; Sequence=VSP_002570;
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. For SLAMF1 a 'two-out-of-
CC three-pronged' mechanism is proposed involving threonine (position -2),
CC phosphorylated tyrosine (position 0) and valine/isoleucine (position
CC +3). Binding is mediated by either three 'prongs' (for high affinity
CC binding involving ITSM 1) or a combination of any two also including
CC non-phosphorylated Tyr-288 of ITSM 1 thus providing a positive feedback
CC loop implicating SH2D1A-dependent recruitment of activating FYN. ITSM 2
CC needs to be phosphorylated on Tyr-335 for SH2D1A binding.
CC {ECO:0000250|UniProtKB:Q13291}.
CC -!- PTM: Phosphorylated on tyrosine residues by FYN (By similarity).
CC {ECO:0000250|UniProtKB:Q13291, ECO:0000269|PubMed:11477403}.
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DR EMBL; AF149791; AAF22231.1; -; mRNA.
DR EMBL; AF149792; AAF22232.1; -; mRNA.
DR EMBL; AF164523; AAF13818.1; -; Genomic_DNA.
DR EMBL; AF164519; AAF13818.1; JOINED; Genomic_DNA.
DR EMBL; AF164520; AAF13818.1; JOINED; Genomic_DNA.
DR EMBL; AF164521; AAF13818.1; JOINED; Genomic_DNA.
DR EMBL; AF164522; AAF13818.1; JOINED; Genomic_DNA.
DR EMBL; AF160990; AAF14535.1; -; mRNA.
DR CCDS; CCDS15502.1; -. [Q9QUM4-1]
DR RefSeq; NP_038758.2; NM_013730.4. [Q9QUM4-1]
DR AlphaFoldDB; Q9QUM4; -.
DR SMR; Q9QUM4; -.
DR BioGRID; 205139; 2.
DR CORUM; Q9QUM4; -.
DR IntAct; Q9QUM4; 11.
DR MINT; Q9QUM4; -.
DR STRING; 10090.ENSMUSP00000015460; -.
DR GlyGen; Q9QUM4; 9 sites.
DR iPTMnet; Q9QUM4; -.
DR PhosphoSitePlus; Q9QUM4; -.
DR EPD; Q9QUM4; -.
DR jPOST; Q9QUM4; -.
DR MaxQB; Q9QUM4; -.
DR PaxDb; Q9QUM4; -.
DR PRIDE; Q9QUM4; -.
DR ProteomicsDB; 261407; -. [Q9QUM4-1]
DR ProteomicsDB; 261408; -. [Q9QUM4-2]
DR Antibodypedia; 3725; 1000 antibodies from 45 providers.
DR DNASU; 27218; -.
DR Ensembl; ENSMUST00000015460; ENSMUSP00000015460; ENSMUSG00000015316. [Q9QUM4-1]
DR GeneID; 27218; -.
DR KEGG; mmu:27218; -.
DR UCSC; uc007dpc.1; mouse. [Q9QUM4-1]
DR CTD; 6504; -.
DR MGI; MGI:1351314; Slamf1.
DR VEuPathDB; HostDB:ENSMUSG00000015316; -.
DR eggNOG; ENOG502SVMG; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_066453_0_0_1; -.
DR InParanoid; Q9QUM4; -.
DR OMA; DHVAYNW; -.
DR PhylomeDB; Q9QUM4; -.
DR TreeFam; TF334964; -.
DR BioGRID-ORCS; 27218; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9QUM4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QUM4; protein.
DR Bgee; ENSMUSG00000015316; Expressed in blood and 34 other tissues.
DR ExpressionAtlas; Q9QUM4; baseline and differential.
DR Genevisible; Q9QUM4; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IMP:MGI.
DR GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; ISO:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:0001787; P:natural killer cell proliferation; IMP:UniProtKB.
DR GO; GO:2000349; P:negative regulation of CD40 signaling pathway; ISO:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:MGI.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IDA:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IMP:MGI.
DR GO; GO:0031338; P:regulation of vesicle fusion; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010407; Sig_lymph_act_molc_N.
DR Pfam; PF06214; SLAM; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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; Phagocytosis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..343
FT /note="Signaling lymphocytic activation molecule"
FT /id="PRO_0000014960"
FT TOPO_DOM 25..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..138
FT /note="Ig-like V-type"
FT DOMAIN 145..228
FT /note="Ig-like C2-type"
FT REGION 320..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 286..291
FT /note="ITSM 1"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOTIF 313..318
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 333..338
FT /note="ITSM 2"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT COMPBIAS 325..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOD_RES 315
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOD_RES 335
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 167..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 296..343
FT /note="PQEKKLHDALTDQDPCTTIYVAATEPAPESVQEPNPTTVYASVTLPES ->
FT VRSMPHLAGVSVIFRTGFLIAALHTTMVLQGLLE (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10570270"
FT /id="VSP_002570"
FT MUTAGEN 288
FT /note="Y->A: Greatly reduces SLAMF1:SH2D1A-mediated
FT intracellular tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:11477403"
FT MUTAGEN 315
FT /note="Y->A: Abolishes SLAMF1:SH2D1A-mediated intracellular
FT tyrosine phosphorylation, no effect on interaction with
FT SH2D1A; when associated with A-335."
FT /evidence="ECO:0000269|PubMed:11477403"
FT MUTAGEN 335
FT /note="Y->A: Abolishes SLAMF1:SH2D1A-mediated intracellular
FT tyrosine phosphorylation, no effect on interaction with
FT SH2D1A; when associated with A-315."
FT /evidence="ECO:0000269|PubMed:11477403"
SQ SEQUENCE 343 AA; 38094 MW; 7980470157E834C4 CRC64;
MDPKGSLSWR ILLFLSLAFE LSYGTGGGVM DCPVILQKLG QDTWLPLTNE HQINKSVNKS
VRILVTMATS PGSKSNKKIV SFDLSKGSYP DHLEDGYHFQ SKNLSLKILG NRRESEGWYL
VSVEENVSVQ QFCKQLKLYE QVSPPEIKVL NKTQENENGT CSLLLACTVK KGDHVTYSWS
DEAGTHLLSR ANRSHLLHIT LSNQHQDSIY NCTASNPVSS ISRTFNLSSQ ACKQESSSES
SPWMQYTLVP LGVVIIFILV FTAIIMMKRQ GKSNHCQPPV EEKSLTIYAQ VQKSGPQEKK
LHDALTDQDP CTTIYVAATE PAPESVQEPN PTTVYASVTL PES
