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Signaling lymphocytic activation molecule (CDw150) (IPO-3) (SLAM family member 1) (CD antigen CD150)

 SLAF1_HUMAN             Reviewed;         335 AA.
Q13291; Q5W172; Q9HBE8; W0HKK7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 174.
RecName: Full=Signaling lymphocytic activation molecule;
AltName: Full=CDw150;
AltName: Full=IPO-3;
AltName: Full=SLAM family member 1;
AltName: CD_antigen=CD150;
Flags: Precursor;
Name=SLAMF1; Synonyms=SLAM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND SUBCELLULAR
LOCATION.
TISSUE=T-cell;
PubMed=7617038; DOI=10.1038/376260a0;
Cocks B.G., Chang C.-C.J., Carballido J.M., Yssel H., de Vries J.E.,
Aversa G.;
"A novel receptor involved in T-cell activation.";
Nature 376:260-263(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (MICROBIAL INFECTION)
(ISOFORM 4), TISSUE SPECIFICITY (ISOFORM 4), AND SUBCELLULAR LOCATION
(ISOFORM 4).
PubMed=25710480; DOI=10.1371/journal.pone.0118302;
Romanets-Korbut O., Najakshin A.M., Yurchenko M., Malysheva T.A.,
Kovalevska L., Shlapatska L.M., Zozulya Y.A., Taranin A.V., Horvat B.,
Sidorenko S.P.;
"Expression of CD150 in tumors of the central nervous system:
identification of a novel isoform.";
PLoS ONE 10:E0118302-E0118302(2015).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 265-288.
PubMed=12629654; DOI=10.1002/jmv.10373;
Ferrand V., Li C., Romeo G., Yin L.;
"Absence of SLAM mutations in EBV-associated lymphoproliferative
disease patients.";
J. Med. Virol. 70:131-136(2003).
[7]
TISSUE SPECIFICITY.
PubMed=9091591; DOI=10.1084/jem.185.6.993;
Punnonen J., Cocks B.G., Carballido J.M., Bennett B., Peterson D.,
Aversa G., de Vries J.E.;
"Soluble and membrane-bound forms of signaling lymphocytic activation
molecule (SLAM) induce proliferation and Ig synthesis by activated
human B lymphocytes.";
J. Exp. Med. 185:993-1004(1997).
[8]
INTERACTION WITH SH2D1A.
PubMed=9774102; DOI=10.1038/26683;
Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S.,
Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E.,
Aversa G., Terhorst C.;
"The X-linked lymphoproliferative-disease gene product SAP regulates
signals induced through the co-receptor SLAM.";
Nature 395:462-469(1998).
[9]
INTERACTION WITH INPP5D.
PubMed=10229804;
Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A.,
Sidorenko S.P.;
"CDw150 associates with src-homology 2-containing inositol phosphatase
and modulates CD95-mediated apoptosis.";
J. Immunol. 162:5719-5727(1999).
[10]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH MEASLES VIRUS HN
PROTEIN, AND DOMAIN IG-LIKE V-TYPE.
PubMed=10972291; DOI=10.1038/35022579;
Tatsuo H., Ono N., Tanaka K., Yanagi Y.;
"SLAM (CDw150) is a cellular receptor for measles virus.";
Nature 406:893-897(2000).
[11]
INTERACTION WITH INPP5D; PTPN11 AND SH2D1A, MUTAGENESIS OF TYR-269;
TYR-281; TYR-307 AND TYR-327, AND DOMAIN ITSM MOTIF.
PubMed=11313386; DOI=10.4049/jimmunol.166.9.5480;
Shlapatska L.M., Mikhalap S.V., Berdova A.G., Zelensky O.M., Yun T.J.,
Nichols K.E., Clark E.A., Sidorenko S.P.;
"CD150 association with either the SH2-containing inositol phosphatase
or the SH2-containing protein tyrosine phosphatase is regulated by the
adaptor protein SH2D1A.";
J. Immunol. 166:5480-5487(2001).
[12]
INTERACTION WITH SH2D1A, PHOSPHORYLATION AT TYR-281; TYR-307 AND
TYR-327, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-279; TYR-281;
THR-325 AND TYR-327, AND DOMAIN ITSM MOTIF.
PubMed=11806999; DOI=10.1182/blood.V99.3.957;
Howie D., Simarro M., Sayos J., Guirado M., Sancho J., Terhorst C.;
"Molecular dissection of the signaling and costimulatory functions of
CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation.";
Blood 99:957-965(2002).
[13]
FUNCTION, AND INTERACTION WITH SH2D1A; SH2D1B; INPP5D; PTPN11 AND FYN.
PubMed=12458214; DOI=10.1074/jbc.M206649200;
Li C., Iosef C., Jia C.Y., Han V.K., Li S.S.;
"Dual functional roles for the X-linked lymphoproliferative syndrome
gene product SAP/SH2D1A in signaling through the signaling lymphocyte
activation molecule (SLAM) family of immune receptors.";
J. Biol. Chem. 278:3852-3859(2003).
[14]
FUNCTION.
PubMed=16317102; DOI=10.1182/blood-2005-06-2265;
Rethi B., Gogolak P., Szatmari I., Veres A., Erdos E., Nagy L.,
Rajnavoelgyi E., Terhorst C., Lanyi A.;
"SLAM/SLAM interactions inhibit CD40-induced production of
inflammatory cytokines in monocyte-derived dendritic cells.";
Blood 107:2821-2829(2006).
[15]
FUNCTION, AND INTERACTION WITH MAP4K1.
PubMed=20231852; DOI=10.1038/icb.2010.14;
Yurchenko M.Y., Kovalevska L.M., Shlapatska L.M., Berdova G.G.,
Clark E.A., Sidorenko S.P.;
"CD150 regulates JNK1/2 activation in normal and Hodgkin's lymphoma B
cells.";
Immunol. Cell Biol. 88:565-574(2010).
[16]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH BECN1 AND PIK3C3.
PubMed=20818396; DOI=10.1038/ni.1931;
Berger S.B., Romero X., Ma C., Wang G., Faubion W.A., Liao G.,
Compeer E., Keszei M., Rameh L., Wang N., Boes M., Regueiro J.R.,
Reinecker H.C., Terhorst C.;
"SLAM is a microbial sensor that regulates bacterial phagosome
functions in macrophages.";
Nat. Immunol. 11:920-927(2010).
[17]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 273-286 IN COMPLEX WITH
SH2D1B, INTERACTION WITH SH2D1B, AND PHOSPHORYLATION AT TYR-281.
PubMed=11689425; DOI=10.1093/emboj/20.21.5840;
Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C.,
Howie D., Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B.,
Engel P., Eck M.J., Terhorst C.;
"Structural basis for the interaction of the free SH2 domain EAT-2
with SLAM receptors in hematopoietic cells.";
EMBO J. 20:5840-5852(2001).
[18]
STRUCTURE BY NMR OF 276-282 IN COMPLEX WITH SH2D1A, AND DOMAIN ITSM
MOTIF.
PubMed=11823424; DOI=10.1093/emboj/21.3.314;
Hwang P.M., Li C., Morra M., Lillywhite J., Muhandiram D.R.,
Gertler F., Terhorst C., Kay L.E., Pawson T., Forman-Kay J.D.,
Li S.-C.;
"A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain:
structural basis and relevance to the XLP syndrome.";
EMBO J. 21:314-323(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 276-286 IN COMPLEX WITH
SH2D1A AND FYN.
PubMed=12545174; DOI=10.1038/ncb920;
Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F.,
Howie D., Sumegi J., Terhorst C., Eck M.J.;
"SAP couples Fyn to SLAM immune receptors.";
Nat. Cell Biol. 5:155-160(2003).
[20]
VARIANT [LARGE SCALE ANALYSIS] PHE-81.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Self-ligand receptor of the signaling lymphocytic
activation molecule (SLAM) family. SLAM receptors triggered by
homo- or heterotypic cell-cell interactions are modulating the
activation and differentiation of a wide variety of immune cells
and thus are involved in the regulation and interconnection of
both innate and adaptive immune response. Activities are
controlled by presence or absence of small cytoplasmic adapter
proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. SLAMF1-induced signal-
transduction events in T-lymphocytes are different from those in
B-cells. Two modes of SLAMF1 signaling seem to exist: one
depending on SH2D1A (and perhaps SH2D1B) and another in which
protein-tyrosine phosphatase 2C (PTPN11)-dependent signal
transduction operates. Initially it has been proposed that
association with SH2D1A prevents binding to inhibitory effectors
including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999).
However, signaling is also regulated by SH2D1A which can
simultaneously interact with and recruit FYN which subsequently
phosphorylates and activates SLAMF1 (PubMed:12458214). Mediates
IL-2-independent proliferation of activated T-cells during immune
responses and induces IFN-gamma production (By similarity).
Downstreaming signaling involves INPP5D, DOK1 and DOK2 leading to
inhibited IFN-gamma production in T-cells, and PRKCQ, BCL10 and
NFKB1 leading to increased T-cell activation and Th2 cytokine
production (By similarity). Promotes T-cell receptor-induced IL-4
secretion by CD4(+) cells (By similarity). Inhibits antigen
receptor-mediated production of IFN-gamma, but not IL-2, in
CD4(-)/CD8(-) T-cells (By similarity). Required for IL-4
production by germinal centers T follicular helper (T(Fh))cells
(By similarity). May inhibit CD40-induced signal transduction in
monocyte-derived dendritic cells (PubMed:16317102). May play a
role in allergic responses and may regulate allergen-induced Th2
cytokine and Th1 cytokine secretion (By similarity). In
conjunction with SLAMF6 controls the transition between positive
selection and the subsequent expansion and differentiation of the
thymocytic natural killer T (NKT) cell lineage. Involved in the
peripheral differentiation of indifferent natural killer T (iNKT)
cells toward a regulatory NKT2 type (By similarity). In
macrophages involved in down-regulation of IL-12, TNF-alpha and
nitric oxide in response to lipopolysaccharide (LPS) (By
similarity). In B-cells activates the ERK signaling pathway
independently of SH2D1A but implicating both, SYK and INPP5D, and
activates Akt signaling dependent on SYK and SH2D1A (By
similarity). In B-cells also activates p38 MAPK and JNK1 and JNK2
(PubMed:20231852). In conjunction with CD84/SLAMF5 and SLAMF6 may
be a negative regulator of the humoral immune response (By
similarity). Involved in innate immune response against Gram-
negative bacteria in macrophages; probably recognizes OmpC and/or
OmpF on the bacterial surface, regulates phagosome maturation and
recruitment of the PI3K complex II (PI3KC3-C2) leading to
accumulation of PdtIns(3)P and NOX2 activity in the phagosomes
(PubMed:20818396). {ECO:0000250|UniProtKB:Q9QUM4,
ECO:0000269|PubMed:16317102, ECO:0000269|PubMed:20231852,
ECO:0000269|PubMed:20818396, ECO:0000305|PubMed:11806999,
ECO:0000305|PubMed:12458214}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Measles
virus; also including isoform 4. {ECO:0000269|PubMed:10972291,
ECO:0000269|PubMed:25710480}.
-!- SUBUNIT: Interacts (via cytoplasmic domain) with SH2D1A and
SH2D1B; SH2D1A mediates association with FYN; SH2D1A binds to
phosphorylated and not phosphorylated ITSM 1 (PubMed:9774102,
PubMed:11313386, PubMed:11806999, PubMed:12458214). Interacts (via
cytoplasmic domain phosphorylated on tyrosine residues) with
INPP5D and PTPN11; presence of SH2D1A facilitates binding to
INPP5D (PubMed:11313386, PubMed:12458214). Interacts with MAP4K1
(PubMed:20231852). Interacts with PIK3C3, BECN1 and UVRAG;
indicative for an association with PI3K complex II (PI3KC3-C2)
(PubMed:20818396). {ECO:0000269|PubMed:11313386,
ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:11806999,
ECO:0000269|PubMed:11823424, ECO:0000269|PubMed:12458214,
ECO:0000269|PubMed:12545174, ECO:0000269|PubMed:20231852,
ECO:0000269|PubMed:20818396, ECO:0000269|PubMed:9774102}.
-!- SUBUNIT: (Microbial infection) Interacts with measles
hemagglutinin protein. {ECO:0000269|PubMed:10972291}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-4315002, EBI-4315002;
Q786F2:H (xeno); NbExp=2; IntAct=EBI-4315002, EBI-5323300;
Q92918:MAP4K1; NbExp=3; IntAct=EBI-4315002, EBI-881;
O60880:SH2D1A; NbExp=14; IntAct=EBI-4315002, EBI-6983382;
O60880-1:SH2D1A; NbExp=2; IntAct=EBI-4315002, EBI-15552052;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11806999};
Single-pass type I membrane protein. Note=Present on the surface
of B-cells and T-cells. Located at the plasma membrane contacts
between neighboring T-cells (PubMed:11806999).
{ECO:0000269|PubMed:11806999}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted
{ECO:0000305|PubMed:7617038}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane
{ECO:0000305|PubMed:25710480}. Note=Overexpressed isoform 4 is
detected on the cell surface. In glioma cell lines endogenuous
isoform 4 is detetced predominantly in the cytoplasm and
colocalized with endoplasmic reticulum and Golgi markers.
{ECO:0000269|PubMed:25710480}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Long, mCD150;
IsoId=Q13291-1; Sequence=Displayed;
Name=2; Synonyms=Short, SURslam2, vmSLAM;
IsoId=Q13291-2; Sequence=VSP_002568, VSP_002569;
Name=3; Synonyms=Secreted, SECslam, sSLAM;
IsoId=Q13291-3; Sequence=VSP_002567;
Name=4; Synonyms=nCD150;
IsoId=Q13291-4; Sequence=VSP_058033;
-!- TISSUE SPECIFICITY: Constitutively expressed on peripheral blood
memory T-cells, T-cell clones, immature thymocytes and a
proportion of B-cells, and is rapidly induced on naive T-cells
after activation (PubMed:7617038). Activated B-cells express
isoform 1, isoform 3 and a cytoplasmic isoform (PubMed:9091591).
Isoform 4 is expressed in B-cells, primary T-cells, dendritic
cells and macrophages. Isoform 4 is expressed in tumors of the
central nervous system (PubMed:25710480).
{ECO:0000269|PubMed:25710480, ECO:0000269|PubMed:7617038,
ECO:0000269|PubMed:9091591}.
-!- DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs)
with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family
receptors have overlapping specificity for activating and
inhibitory SH2 domain-containing binding partners. Especially they
mediate the interaction with the SH2 domain of SH2D1A and SH2D1B.
For SLAMF1 a 'two-out-of-three-pronged' mechanism is proposed
involving threonine (position -2), phosphorylated tyrosine
(position 0) and valine/isoleucine (position +3). SH2D1A binding
is mediated by either three 'prongs' (for high affinity binding
involving ITSM 1) or a combination of any two also including non-
phosphorylated Tyr-281 of ITSM 1 thus providing a positive
feedback loop implicating SH2D1A-dependent recruitment of
activating FYN. ITSM 2 needs to be phosphorylated on Tyr-327 for
SH2D1A binding. {ECO:0000269|PubMed:11806999,
ECO:0000269|PubMed:11823424, ECO:0000305|PubMed:11313386}.
-!- PTM: Phosphorylated on tyrosine residues by FYN.
{ECO:0000269|PubMed:11806999, ECO:0000269|PubMed:11823424}.
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EMBL; U33017; AAA75380.1; -; mRNA.
EMBL; KF471075; AHF72732.1; -; mRNA.
EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52706.1; -; Genomic_DNA.
EMBL; BC132792; AAI32793.1; -; mRNA.
EMBL; AF252305; AAG10434.1; -; Genomic_DNA.
CCDS; CCDS1207.1; -. [Q13291-1]
CCDS; CCDS81389.1; -. [Q13291-4]
PIR; S58892; S58892.
RefSeq; NP_001317683.1; NM_001330754.1. [Q13291-4]
RefSeq; NP_003028.1; NM_003037.4. [Q13291-1]
RefSeq; XP_005245513.1; XM_005245456.3. [Q13291-3]
UniGene; Hs.523660; -.
PDB; 1D4T; X-ray; 1.10 A; B=276-286.
PDB; 1D4W; X-ray; 1.80 A; C/D=276-286.
PDB; 1I3Z; X-ray; 2.15 A; B=273-286.
PDB; 1KA6; NMR; -; B=275-282.
PDB; 1KA7; NMR; -; B=275-286.
PDB; 1M27; X-ray; 2.50 A; B=276-286.
PDB; 2DZF; Model; -; @=1-335.
PDB; 2IE9; Model; -; @=1-335.
PDB; 2IFL; Model; -; @=3-335.
PDB; 2IG5; Model; -; @=1-335.
PDBsum; 1D4T; -.
PDBsum; 1D4W; -.
PDBsum; 1I3Z; -.
PDBsum; 1KA6; -.
PDBsum; 1KA7; -.
PDBsum; 1M27; -.
PDBsum; 2DZF; -.
PDBsum; 2IE9; -.
PDBsum; 2IFL; -.
PDBsum; 2IG5; -.
ProteinModelPortal; Q13291; -.
SMR; Q13291; -.
BioGrid; 112395; 120.
DIP; DIP-40767N; -.
ELM; Q13291; -.
IntAct; Q13291; 11.
MINT; Q13291; -.
STRING; 9606.ENSP00000306190; -.
iPTMnet; Q13291; -.
PhosphoSitePlus; Q13291; -.
BioMuta; SLAMF1; -.
DMDM; 9297047; -.
PaxDb; Q13291; -.
PeptideAtlas; Q13291; -.
PRIDE; Q13291; -.
ProteomicsDB; 59283; -.
ProteomicsDB; 59284; -. [Q13291-2]
ProteomicsDB; 59285; -. [Q13291-3]
DNASU; 6504; -.
Ensembl; ENST00000302035; ENSP00000306190; ENSG00000117090. [Q13291-1]
Ensembl; ENST00000538290; ENSP00000438406; ENSG00000117090. [Q13291-4]
GeneID; 6504; -.
KEGG; hsa:6504; -.
UCSC; uc001fwl.6; human. [Q13291-1]
UCSC; uc031vca.2; human.
CTD; 6504; -.
DisGeNET; 6504; -.
EuPathDB; HostDB:ENSG00000117090.14; -.
GeneCards; SLAMF1; -.
HGNC; HGNC:10903; SLAMF1.
HPA; CAB002438; -.
HPA; HPA069319; -.
MIM; 603492; gene.
neXtProt; NX_Q13291; -.
OpenTargets; ENSG00000117090; -.
PharmGKB; PA35803; -.
eggNOG; ENOG410IFKK; Eukaryota.
eggNOG; ENOG4111DAM; LUCA.
GeneTree; ENSGT00510000048858; -.
HOGENOM; HOG000125310; -.
HOVERGEN; HBG054224; -.
InParanoid; Q13291; -.
KO; K06536; -.
OMA; NIYICTV; -.
OrthoDB; EOG091G0EOO; -.
PhylomeDB; Q13291; -.
TreeFam; TF334964; -.
SIGNOR; Q13291; -.
ChiTaRS; SLAMF1; human.
EvolutionaryTrace; Q13291; -.
GeneWiki; SLAMF1; -.
GenomeRNAi; 6504; -.
PRO; PR:Q13291; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117090; -.
CleanEx; HS_SLAMF1; -.
ExpressionAtlas; Q13291; baseline and differential.
Genevisible; Q13291; HS.
GO; GO:0009986; C:cell surface; IEA:InterPro.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003823; F:antigen binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0046649; P:lymphocyte activation; IEA:InterPro.
GO; GO:0002277; P:myeloid dendritic cell activation involved in immune response; IDA:UniProtKB.
GO; GO:2000349; P:negative regulation of CD40 signaling pathway; IDA:UniProtKB.
GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010407; Sig_lymph_act_molc_N.
Pfam; PF06214; SLAM; 1.
ProDom; PD090491; Sig_lymph_act_molc_N; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell adhesion;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Immunity;
Immunoglobulin domain; Innate immunity; Membrane; Phagocytosis;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 335 Signaling lymphocytic activation
molecule.
/FTId=PRO_0000014959.
TOPO_DOM 21 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 335 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 138 Ig-like V-type.
DOMAIN 144 223 Ig-like C2-type.
MOTIF 279 284 ITSM 1. {ECO:0000269|PubMed:11823424}.
MOTIF 307 312 SH2-binding. {ECO:0000255}.
MOTIF 325 330 ITSM 2. {ECO:0000305|PubMed:11313386,
ECO:0000305|PubMed:11806999}.
MOD_RES 281 281 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:11689425,
ECO:0000269|PubMed:11806999}.
MOD_RES 307 307 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:11806999}.
MOD_RES 327 327 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:11806999}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 158 228 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 164 209 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 234 263 Missing (in isoform 3).
{ECO:0000303|PubMed:7617038}.
/FTId=VSP_002567.
VAR_SEQ 264 335 GKTNHYQTTVEKKSLTIYAQVQKPGPLQKKLDSFPAQDPCT
TIYVAATEPVPESVQETNSITVYASVTLPES -> ATLTTT
NQYWSQNVLTQDQERCPGCLPMVKRTITRQQWKKKALRSMP
KSRNQVLFRRNLTPSQLRTLAPPYMLLPQSLSQSLSRKQIP
SQSMLV (in isoform 4).
{ECO:0000303|PubMed:25710480}.
/FTId=VSP_058033.
VAR_SEQ 289 298 PLQKKLDSFP -> DTHHQTSDLF (in isoform 2).
{ECO:0000303|PubMed:7617038}.
/FTId=VSP_002568.
VAR_SEQ 299 335 Missing (in isoform 2).
{ECO:0000303|PubMed:7617038}.
/FTId=VSP_002569.
VARIANT 11 11 F -> L (in dbSNP:rs2295612).
/FTId=VAR_021924.
VARIANT 81 81 L -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035524.
VARIANT 333 333 P -> T (in dbSNP:rs3796504).
/FTId=VAR_021925.
MUTAGEN 269 269 Y->F: No effect on interaction with
INPP5D/SHIP-1, PTPN11/SHP-2 and SH2D1A.
{ECO:0000269|PubMed:11313386}.
MUTAGEN 279 279 T->A: Disrupts interaction with SH2D1A;
when associated with A-325.
{ECO:0000269|PubMed:11806999}.
MUTAGEN 281 281 Y->F: Disrupts interaction with
INPP5D/SHIP-1 and PTPN11/SHP-2, no effect
on interaction with SH2D1A.
{ECO:0000269|PubMed:11313386,
ECO:0000269|PubMed:11806999}.
MUTAGEN 281 281 Y->F: Disrupts interaction with SH2D1A;
when associated with F-327.
{ECO:0000269|PubMed:11806999}.
MUTAGEN 307 307 Y->F: No effect on interaction with
PTPN11/SHP-2 and SH2D1A.
{ECO:0000269|PubMed:11313386}.
MUTAGEN 325 325 T->A: Disrupts interaction with SH2D1A;
when associated with A-279.
{ECO:0000269|PubMed:11806999}.
MUTAGEN 327 327 Y->F: Disrupts interaction with
INPP5D/SHIP-1 and PTPN11/SHP-2, no effect
on interaction with SH2D1A.
{ECO:0000269|PubMed:11313386,
ECO:0000269|PubMed:11806999}.
MUTAGEN 327 327 Y->F: Disrupts interaction with SH2D1A;
when associated with F-281.
{ECO:0000269|PubMed:11806999}.
STRAND 278 281 {ECO:0000244|PDB:1D4T}.
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


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