SLAF1_HUMAN
ID SLAF1_HUMAN Reviewed; 335 AA.
AC Q13291; Q5W172; Q9HBE8; W0HKK7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Signaling lymphocytic activation molecule;
DE AltName: Full=CDw150;
DE AltName: Full=IPO-3;
DE AltName: Full=SLAM family member 1;
DE AltName: CD_antigen=CD150;
DE Flags: Precursor;
GN Name=SLAMF1; Synonyms=SLAM;
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] (ISOFORMS 1; 2 AND 3), AND SUBCELLULAR LOCATION.
RC TISSUE=T-cell;
RX PubMed=7617038; DOI=10.1038/376260a0;
RA Cocks B.G., Chang C.-C.J., Carballido J.M., Yssel H., de Vries J.E.,
RA Aversa G.;
RT "A novel receptor involved in T-cell activation.";
RL Nature 376:260-263(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (MICROBIAL INFECTION)
RP (ISOFORM 4), TISSUE SPECIFICITY (ISOFORM 4), AND SUBCELLULAR LOCATION
RP (ISOFORM 4).
RX PubMed=25710480; DOI=10.1371/journal.pone.0118302;
RA Romanets-Korbut O., Najakshin A.M., Yurchenko M., Malysheva T.A.,
RA Kovalevska L., Shlapatska L.M., Zozulya Y.A., Taranin A.V., Horvat B.,
RA Sidorenko S.P.;
RT "Expression of CD150 in tumors of the central nervous system:
RT identification of a novel isoform.";
RL PLoS ONE 10:E0118302-E0118302(2015).
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., 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [GENOMIC DNA] OF 265-288.
RX PubMed=12629654; DOI=10.1002/jmv.10373;
RA Ferrand V., Li C., Romeo G., Yin L.;
RT "Absence of SLAM mutations in EBV-associated lymphoproliferative disease
RT patients.";
RL J. Med. Virol. 70:131-136(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9091591; DOI=10.1084/jem.185.6.993;
RA Punnonen J., Cocks B.G., Carballido J.M., Bennett B., Peterson D.,
RA Aversa G., de Vries J.E.;
RT "Soluble and membrane-bound forms of signaling lymphocytic activation
RT molecule (SLAM) induce proliferation and Ig synthesis by activated human B
RT lymphocytes.";
RL J. Exp. Med. 185:993-1004(1997).
RN [8]
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 [9]
RP INTERACTION WITH INPP5D.
RX PubMed=10229804;
RA Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A.,
RA Sidorenko S.P.;
RT "CDw150 associates with src-homology 2-containing inositol phosphatase and
RT modulates CD95-mediated apoptosis.";
RL J. Immunol. 162:5719-5727(1999).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH MEASLES VIRUS HN PROTEIN,
RP AND DOMAIN IG-LIKE V-TYPE.
RX PubMed=10972291; DOI=10.1038/35022579;
RA Tatsuo H., Ono N., Tanaka K., Yanagi Y.;
RT "SLAM (CDw150) is a cellular receptor for measles virus.";
RL Nature 406:893-897(2000).
RN [11]
RP INTERACTION WITH INPP5D; PTPN11 AND SH2D1A, MUTAGENESIS OF TYR-269;
RP TYR-281; TYR-307 AND TYR-327, AND DOMAIN ITSM MOTIF.
RX PubMed=11313386; DOI=10.4049/jimmunol.166.9.5480;
RA Shlapatska L.M., Mikhalap S.V., Berdova A.G., Zelensky O.M., Yun T.J.,
RA Nichols K.E., Clark E.A., Sidorenko S.P.;
RT "CD150 association with either the SH2-containing inositol phosphatase or
RT the SH2-containing protein tyrosine phosphatase is regulated by the adaptor
RT protein SH2D1A.";
RL J. Immunol. 166:5480-5487(2001).
RN [12]
RP INTERACTION WITH SH2D1A, PHOSPHORYLATION AT TYR-281; TYR-307 AND TYR-327,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF THR-279; TYR-281; THR-325 AND TYR-327,
RP AND DOMAIN ITSM MOTIF.
RX PubMed=11806999; DOI=10.1182/blood.v99.3.957;
RA Howie D., Simarro M., Sayos J., Guirado M., Sancho J., Terhorst C.;
RT "Molecular dissection of the signaling and costimulatory functions of CD150
RT (SLAM): CD150/SAP binding and CD150-mediated costimulation.";
RL Blood 99:957-965(2002).
RN [13]
RP FUNCTION, AND INTERACTION WITH SH2D1A; SH2D1B; INPP5D; PTPN11 AND FYN.
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 [14]
RP FUNCTION.
RX PubMed=16317102; DOI=10.1182/blood-2005-06-2265;
RA Rethi B., Gogolak P., Szatmari I., Veres A., Erdos E., Nagy L.,
RA Rajnavoelgyi E., Terhorst C., Lanyi A.;
RT "SLAM/SLAM interactions inhibit CD40-induced production of inflammatory
RT cytokines in monocyte-derived dendritic cells.";
RL Blood 107:2821-2829(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH MAP4K1.
RX PubMed=20231852; DOI=10.1038/icb.2010.14;
RA Yurchenko M.Y., Kovalevska L.M., Shlapatska L.M., Berdova G.G., Clark E.A.,
RA Sidorenko S.P.;
RT "CD150 regulates JNK1/2 activation in normal and Hodgkin's lymphoma B
RT cells.";
RL Immunol. Cell Biol. 88:565-574(2010).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH BECN1 AND PIK3C3.
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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 273-286 IN COMPLEX WITH SH2D1B,
RP INTERACTION WITH SH2D1B, AND PHOSPHORYLATION AT TYR-281.
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 [18]
RP STRUCTURE BY NMR OF 276-282 IN COMPLEX WITH SH2D1A, AND DOMAIN ITSM MOTIF.
RX PubMed=11823424; DOI=10.1093/emboj/21.3.314;
RA Hwang P.M., Li C., Morra M., Lillywhite J., Muhandiram D.R., Gertler F.,
RA Terhorst C., Kay L.E., Pawson T., Forman-Kay J.D., Li S.-C.;
RT "A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain:
RT structural basis and relevance to the XLP syndrome.";
RL EMBO J. 21:314-323(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A AND
RP FYN.
RX PubMed=12545174; DOI=10.1038/ncb920;
RA Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F.,
RA Howie D., Sumegi J., Terhorst C., Eck M.J.;
RT "SAP couples Fyn to SLAM immune receptors.";
RL Nat. Cell Biol. 5:155-160(2003).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-81.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:11806999). However, signaling is
CC also regulated by SH2D1A which can simultaneously interact with and
CC recruit FYN which subsequently phosphorylates and activates SLAMF1
CC (PubMed:12458214). Mediates IL-2-independent proliferation of activated
CC T-cells during immune responses and induces IFN-gamma production (By
CC similarity). Downstreaming signaling involves INPP5D, DOK1 and DOK2
CC leading to inhibited IFN-gamma production in T-cells, and PRKCQ, BCL10
CC and NFKB1 leading to increased T-cell activation and Th2 cytokine
CC production (By similarity). Promotes T-cell receptor-induced IL-4
CC secretion by CD4(+) cells (By similarity). Inhibits antigen receptor-
CC mediated production of IFN-gamma, but not IL-2, in CD4(-)/CD8(-) T-
CC cells (By similarity). Required for IL-4 production by germinal centers
CC T follicular helper (T(Fh))cells (By similarity). May inhibit CD40-
CC induced signal transduction in monocyte-derived dendritic cells
CC (PubMed:16317102). May play a role in allergic responses and may
CC regulate allergen-induced Th2 cytokine and Th1 cytokine secretion (By
CC similarity). In conjunction with SLAMF6 controls the transition between
CC positive selection and the subsequent expansion and differentiation of
CC the thymocytic natural killer T (NKT) cell lineage. Involved in the
CC peripheral differentiation of indifferent natural killer T (iNKT) cells
CC toward a regulatory NKT2 type (By similarity). In macrophages involved
CC in down-regulation of IL-12, TNF-alpha and nitric oxide in response to
CC lipopolysaccharide (LPS) (By similarity). In B-cells activates the ERK
CC signaling pathway independently of SH2D1A but implicating both, SYK and
CC INPP5D, and activates Akt signaling dependent on SYK and SH2D1A (By
CC similarity). In B-cells also activates p38 MAPK and JNK1 and JNK2
CC (PubMed:20231852). In conjunction with CD84/SLAMF5 and SLAMF6 may be a
CC negative regulator of the humoral immune response (By similarity).
CC Involved in innate immune response against Gram-negative bacteria in
CC macrophages; probably recognizes OmpC and/or OmpF on the bacterial
CC surface, regulates phagosome maturation and recruitment of the PI3K
CC complex II (PI3KC3-C2) leading to accumulation of PdtIns(3)P and NOX2
CC activity in the phagosomes (PubMed:20818396).
CC {ECO:0000250|UniProtKB:Q9QUM4, ECO:0000269|PubMed:16317102,
CC ECO:0000269|PubMed:20231852, ECO:0000269|PubMed:20818396,
CC ECO:0000305|PubMed:11806999, ECO:0000305|PubMed:12458214}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Measles virus;
CC also including isoform 4. {ECO:0000269|PubMed:10972291,
CC ECO:0000269|PubMed:25710480}.
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:11313386,
CC PubMed:11806999, PubMed:12458214). Interacts (via cytoplasmic domain
CC phosphorylated on tyrosine residues) with INPP5D and PTPN11; presence
CC of SH2D1A facilitates binding to INPP5D (PubMed:11313386,
CC PubMed:12458214). Interacts with MAP4K1 (PubMed:20231852). Interacts
CC with PIK3C3, BECN1 and UVRAG; indicative for an association with PI3K
CC complex II (PI3KC3-C2) (PubMed:20818396). {ECO:0000269|PubMed:11313386,
CC ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:11806999,
CC ECO:0000269|PubMed:11823424, ECO:0000269|PubMed:12458214,
CC ECO:0000269|PubMed:12545174, ECO:0000269|PubMed:20231852,
CC ECO:0000269|PubMed:20818396, ECO:0000269|PubMed:9774102}.
CC -!- SUBUNIT: (Microbial infection) Interacts with measles hemagglutinin
CC protein. {ECO:0000269|PubMed:10972291}.
CC -!- INTERACTION:
CC Q13291; Q92918: MAP4K1; NbExp=3; IntAct=EBI-4315002, EBI-881;
CC Q13291; O60880: SH2D1A; NbExp=12; IntAct=EBI-4315002, EBI-6983382;
CC Q13291; O60880-1: SH2D1A; NbExp=2; IntAct=EBI-4315002, EBI-15552052;
CC Q13291; Q13291: SLAMF1; NbExp=2; IntAct=EBI-4315002, EBI-4315002;
CC Q13291; Q786F2: H; Xeno; NbExp=2; IntAct=EBI-4315002, EBI-5323300;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11806999};
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 (PubMed:11806999). {ECO:0000269|PubMed:11806999}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC {ECO:0000305|PubMed:7617038}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC {ECO:0000305|PubMed:25710480}. Note=Overexpressed isoform 4 is detected
CC on the cell surface. In glioma cell lines endogenuous isoform 4 is
CC detetced predominantly in the cytoplasm and colocalized with
CC endoplasmic reticulum and Golgi markers. {ECO:0000269|PubMed:25710480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Long, mCD150;
CC IsoId=Q13291-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, SURslam2, vmSLAM;
CC IsoId=Q13291-2; Sequence=VSP_002568, VSP_002569;
CC Name=3; Synonyms=Secreted, SECslam, sSLAM;
CC IsoId=Q13291-3; Sequence=VSP_002567;
CC Name=4; Synonyms=nCD150;
CC IsoId=Q13291-4; Sequence=VSP_058033;
CC -!- TISSUE SPECIFICITY: Constitutively expressed on peripheral blood memory
CC T-cells, T-cell clones, immature thymocytes and a proportion of B-
CC cells, and is rapidly induced on naive T-cells after activation
CC (PubMed:7617038). Activated B-cells express isoform 1, isoform 3 and a
CC cytoplasmic isoform (PubMed:9091591). Isoform 4 is expressed in B-
CC cells, primary T-cells, dendritic cells and macrophages. Isoform 4 is
CC expressed in tumors of the central nervous system (PubMed:25710480).
CC {ECO:0000269|PubMed:25710480, ECO:0000269|PubMed:7617038,
CC ECO:0000269|PubMed:9091591}.
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). SH2D1A binding is mediated by either three 'prongs' (for high
CC affinity binding involving ITSM 1) or a combination of any two also
CC including non-phosphorylated Tyr-281 of ITSM 1 thus providing a
CC positive feedback loop implicating SH2D1A-dependent recruitment of
CC activating FYN. ITSM 2 needs to be phosphorylated on Tyr-327 for SH2D1A
CC binding. {ECO:0000269|PubMed:11806999, ECO:0000269|PubMed:11823424,
CC ECO:0000305|PubMed:11313386}.
CC -!- PTM: Phosphorylated on tyrosine residues by FYN.
CC {ECO:0000269|PubMed:11806999, ECO:0000269|PubMed:11823424}.
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; U33017; AAA75380.1; -; mRNA.
DR EMBL; KF471075; AHF72732.1; -; mRNA.
DR EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52706.1; -; Genomic_DNA.
DR EMBL; BC132792; AAI32793.1; -; mRNA.
DR EMBL; AF252305; AAG10434.1; -; Genomic_DNA.
DR CCDS; CCDS1207.1; -. [Q13291-1]
DR CCDS; CCDS81389.1; -. [Q13291-4]
DR PIR; S58892; S58892.
DR RefSeq; NP_001317683.1; NM_001330754.1. [Q13291-4]
DR RefSeq; NP_003028.1; NM_003037.4. [Q13291-1]
DR RefSeq; XP_005245513.1; XM_005245456.3. [Q13291-3]
DR PDB; 1D4T; X-ray; 1.10 A; B=276-286.
DR PDB; 1D4W; X-ray; 1.80 A; C/D=276-286.
DR PDB; 1I3Z; X-ray; 2.15 A; B=273-286.
DR PDB; 1KA6; NMR; -; B=275-282.
DR PDB; 1KA7; NMR; -; B=275-286.
DR PDB; 1M27; X-ray; 2.50 A; B=276-286.
DR PDBsum; 1D4T; -.
DR PDBsum; 1D4W; -.
DR PDBsum; 1I3Z; -.
DR PDBsum; 1KA6; -.
DR PDBsum; 1KA7; -.
DR PDBsum; 1M27; -.
DR AlphaFoldDB; Q13291; -.
DR SMR; Q13291; -.
DR BioGRID; 112395; 130.
DR DIP; DIP-40767N; -.
DR ELM; Q13291; -.
DR IntAct; Q13291; 63.
DR MINT; Q13291; -.
DR STRING; 9606.ENSP00000306190; -.
DR GlyGen; Q13291; 8 sites.
DR iPTMnet; Q13291; -.
DR PhosphoSitePlus; Q13291; -.
DR BioMuta; SLAMF1; -.
DR DMDM; 9297047; -.
DR MassIVE; Q13291; -.
DR PaxDb; Q13291; -.
DR PeptideAtlas; Q13291; -.
DR PRIDE; Q13291; -.
DR ProteomicsDB; 59283; -. [Q13291-1]
DR ProteomicsDB; 59284; -. [Q13291-2]
DR ProteomicsDB; 59285; -. [Q13291-3]
DR Antibodypedia; 3725; 1000 antibodies from 45 providers.
DR DNASU; 6504; -.
DR Ensembl; ENST00000302035.11; ENSP00000306190.6; ENSG00000117090.16. [Q13291-1]
DR Ensembl; ENST00000538290.2; ENSP00000438406.2; ENSG00000117090.16. [Q13291-4]
DR GeneID; 6504; -.
DR KEGG; hsa:6504; -.
DR MANE-Select; ENST00000302035.11; ENSP00000306190.6; NM_003037.5; NP_003028.1.
DR UCSC; uc001fwl.6; human. [Q13291-1]
DR UCSC; uc031vca.2; human.
DR CTD; 6504; -.
DR DisGeNET; 6504; -.
DR GeneCards; SLAMF1; -.
DR HGNC; HGNC:10903; SLAMF1.
DR HPA; ENSG00000117090; Tissue enriched (lymphoid).
DR MIM; 603492; gene.
DR neXtProt; NX_Q13291; -.
DR OpenTargets; ENSG00000117090; -.
DR PharmGKB; PA35803; -.
DR VEuPathDB; HostDB:ENSG00000117090; -.
DR eggNOG; ENOG502SVMG; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_066453_0_0_1; -.
DR InParanoid; Q13291; -.
DR OMA; CRTESKE; -.
DR OrthoDB; 1532935at2759; -.
DR PhylomeDB; Q13291; -.
DR TreeFam; TF334964; -.
DR PathwayCommons; Q13291; -.
DR SignaLink; Q13291; -.
DR SIGNOR; Q13291; -.
DR BioGRID-ORCS; 6504; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; SLAMF1; human.
DR EvolutionaryTrace; Q13291; -.
DR GeneWiki; SLAMF1; -.
DR GenomeRNAi; 6504; -.
DR Pharos; Q13291; Tbio.
DR PRO; PR:Q13291; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13291; protein.
DR Bgee; ENSG00000117090; Expressed in thymus and 111 other tissues.
DR ExpressionAtlas; Q13291; baseline and differential.
DR Genevisible; Q13291; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0003823; F:antigen binding; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
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; IEA:Ensembl.
DR GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; IDA:UniProtKB.
DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR GO; GO:0001787; P:natural killer cell proliferation; IEA:Ensembl.
DR GO; GO:2000349; P:negative regulation of CD40 signaling pathway; IDA:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; IEA:Ensembl.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0031338; P:regulation of vesicle fusion; IEA:Ensembl.
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 3D-structure; Adaptive immunity; Alternative splicing; Cell adhesion;
KW Cell membrane; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Immunity;
KW Immunoglobulin domain; Innate immunity; Membrane; Phagocytosis;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..335
FT /note="Signaling lymphocytic activation molecule"
FT /id="PRO_0000014959"
FT TOPO_DOM 21..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..138
FT /note="Ig-like V-type"
FT DOMAIN 144..223
FT /note="Ig-like C2-type"
FT MOTIF 279..284
FT /note="ITSM 1"
FT /evidence="ECO:0000269|PubMed:11823424"
FT MOTIF 307..312
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 325..330
FT /note="ITSM 2"
FT /evidence="ECO:0000305|PubMed:11313386,
FT ECO:0000305|PubMed:11806999"
FT MOD_RES 281
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:11689425,
FT ECO:0000269|PubMed:11806999"
FT MOD_RES 307
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:11806999"
FT MOD_RES 327
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:11806999"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 234..263
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7617038"
FT /id="VSP_002567"
FT VAR_SEQ 264..335
FT /note="GKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCTTIYVAATEPVP
FT ESVQETNSITVYASVTLPES -> ATLTTTNQYWSQNVLTQDQERCPGCLPMVKRTITR
FT QQWKKKALRSMPKSRNQVLFRRNLTPSQLRTLAPPYMLLPQSLSQSLSRKQIPSQSMLV
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:25710480"
FT /id="VSP_058033"
FT VAR_SEQ 289..298
FT /note="PLQKKLDSFP -> DTHHQTSDLF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7617038"
FT /id="VSP_002568"
FT VAR_SEQ 299..335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7617038"
FT /id="VSP_002569"
FT VARIANT 11
FT /note="F -> L (in dbSNP:rs2295612)"
FT /id="VAR_021924"
FT VARIANT 81
FT /note="L -> F (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1373814964)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035524"
FT VARIANT 333
FT /note="P -> T (in dbSNP:rs3796504)"
FT /id="VAR_021925"
FT MUTAGEN 269
FT /note="Y->F: No effect on interaction with INPP5D/SHIP-1,
FT PTPN11/SHP-2 and SH2D1A."
FT /evidence="ECO:0000269|PubMed:11313386"
FT MUTAGEN 279
FT /note="T->A: Disrupts interaction with SH2D1A; when
FT associated with A-325."
FT /evidence="ECO:0000269|PubMed:11806999"
FT MUTAGEN 281
FT /note="Y->F: Disrupts interaction with INPP5D/SHIP-1 and
FT PTPN11/SHP-2, no effect on interaction with SH2D1A."
FT /evidence="ECO:0000269|PubMed:11313386,
FT ECO:0000269|PubMed:11806999"
FT MUTAGEN 281
FT /note="Y->F: Disrupts interaction with SH2D1A; when
FT associated with F-327."
FT /evidence="ECO:0000269|PubMed:11806999"
FT MUTAGEN 307
FT /note="Y->F: No effect on interaction with PTPN11/SHP-2 and
FT SH2D1A."
FT /evidence="ECO:0000269|PubMed:11313386"
FT MUTAGEN 325
FT /note="T->A: Disrupts interaction with SH2D1A; when
FT associated with A-279."
FT /evidence="ECO:0000269|PubMed:11806999"
FT MUTAGEN 327
FT /note="Y->F: Disrupts interaction with INPP5D/SHIP-1 and
FT PTPN11/SHP-2, no effect on interaction with SH2D1A."
FT /evidence="ECO:0000269|PubMed:11313386,
FT ECO:0000269|PubMed:11806999"
FT MUTAGEN 327
FT /note="Y->F: Disrupts interaction with SH2D1A; when
FT associated with F-281."
FT /evidence="ECO:0000269|PubMed:11806999"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1D4T"
SQ SEQUENCE 335 AA; 37231 MW; BFB0F27EA31D8C04 CRC64;
MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE RINKSMNKSI
HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL ENLTLGIRES RKEDEGWYLM
TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN KTQENGTCTL ILGCTVEKGD HVAYSWSEKA
GTHPLNPANS SHLLSLTLGP QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSETKPWAV
YAGLLGGVIM ILIMVVILQL RRRGKTNHYQ TTVEKKSLTI YAQVQKPGPL QKKLDSFPAQ
DPCTTIYVAA TEPVPESVQE TNSITVYASV TLPES
