SLAF7_HUMAN
ID SLAF7_HUMAN Reviewed; 335 AA.
AC Q9NQ25; A8K3U1; B4DPU4; B4DPY3; B4DWA3; Q8N6Y8; Q8ND32; Q9NY08; Q9NY23;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=SLAM family member 7;
DE AltName: Full=CD2 subset 1;
DE AltName: Full=CD2-like receptor-activating cytotoxic cells;
DE Short=CRACC;
DE AltName: Full=Membrane protein FOAP-12;
DE AltName: Full=Novel Ly9;
DE AltName: Full=Protein 19A;
DE AltName: CD_antigen=CD319;
DE Flags: Precursor;
GN Name=SLAMF7; Synonyms=CS1; ORFNames=UNQ576/PRO1138;
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 TISSUE SPECIFICITY.
RX PubMed=11220635; DOI=10.1007/s002510000274;
RA Boles K.S., Mathew P.A.;
RT "Molecular cloning of CS1, a novel human natural killer cell receptor
RT belonging to the CD2 subset of the immunoglobulin superfamily.";
RL Immunogenetics 52:302-307(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11698418; DOI=10.4049/jimmunol.167.10.5517;
RA Bouchon A., Cella M., Grierson H.L., Cohen J.I., Colonna M.;
RT "Activation of NK cell-mediated cytotoxicity by a SAP-independent receptor
RT of the CD2 family.";
RL J. Immunol. 167:5517-5521(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11802771; DOI=10.1042/0264-6021:3610431;
RA Murphy J.J., Hobby P., Vilarino-Varela J., Bishop B., Iordanidou P.,
RA Sutton B.J., Norton J.D.;
RT "A novel immunoglobulin superfamily receptor (19A) related to CD2 is
RT expressed on activated lymphocytes and promotes homotypic B-cell
RT adhesion.";
RL Biochem. J. 361:431-436(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Macrophage;
RA Fujii Y., Takayama K., Tsuritani K., Yajima Y., Amemiya T., Ukai Y.,
RA Naito K., Kawaguchi A.;
RT "Homo sapiens mRNA for FOAP-12 protein, complete cds.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 6 AND 7).
RC TISSUE=Lung, and Synovium;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
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 [9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal lung, and Fetal spleen;
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 [11]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [12]
RP ALTERNATIVE SPLICING (ISOFORM 3).
RX PubMed=15368295; DOI=10.1002/eji.200424917;
RA Lee J.K., Boles K.S., Mathew P.A.;
RT "Molecular and functional characterization of a CS1 (CRACC) splice variant
RT expressed in human NK cells that does not contain immunoreceptor tyrosine-
RT based switch motifs.";
RL Eur. J. Immunol. 34:2791-2799(2004).
RN [13]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SH2D1A.
RX PubMed=12242590; DOI=10.1007/s00251-002-0483-3;
RA Tovar V., Del Valle J., Zapater N., Martin M., Romero X., Pizcueta P.,
RA Bosch J., Terhorst C., Engel P.;
RT "Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family of
RT leukocyte cell-surface receptors.";
RL Immunogenetics 54:394-402(2002).
RN [14]
RP FUNCTION, AND INTERACTION WITH SH2D1B.
RX PubMed=16339536; DOI=10.4049/jimmunol.175.12.7996;
RA Tassi I., Colonna M.;
RT "The cytotoxicity receptor CRACC (CS-1) recruits EAT-2 and activates the
RT PI3K and phospholipase Cgamma signaling pathways in human NK cells.";
RL J. Immunol. 175:7996-8002(2005).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23695528; DOI=10.1007/s00011-013-0632-1;
RA Kim J.R., Horton N.C., Mathew S.O., Mathew P.A.;
RT "CS1 (SLAMF7) inhibits production of proinflammatory cytokines by activated
RT monocytes.";
RL Inflamm. Res. 62:765-772(2013).
RN [16]
RP INVOLVEMENT IN SYSTEMIC LUPUS ERYTHEMATOSUS.
RX PubMed=23956418; DOI=10.4049/jimmunol.1301022;
RA Hagberg N., Theorell J., Schlums H., Eloranta M.L., Bryceson Y.T.,
RA Roennblom L.;
RT "Systemic lupus erythematosus immune complexes increase the expression of
RT SLAM family members CD319 (CRACC) and CD229 (LY-9) on plasmacytoid
RT dendritic cells and CD319 on CD56(dim) NK cells.";
RL J. Immunol. 191:2989-2998(2013).
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 Isoform 1 mediates NK cell activation through a SH2D1A-independent
CC extracellular signal-regulated ERK-mediated pathway (PubMed:11698418).
CC Positively regulates NK cell functions by a mechanism dependent on
CC phosphorylated SH2D1B. Downstream signaling implicates PLCG1, PLCG2 and
CC PI3K (PubMed:16339536). In addition to heterotypic NK cells-target
CC cells interactions also homotypic interactions between NK cells may
CC contribute to activation. However, in the absence of SH2D1B, inhibits
CC NK cell function. Acts also inhibitory in T-cells (By similarity). May
CC play a role in lymphocyte adhesion (PubMed:11802771). In LPS-activated
CC monocytes negatively regulates production of pro-inflammatory cytokines
CC (PubMed:23695528). {ECO:0000250|UniProtKB:Q8BHK6,
CC ECO:0000269|PubMed:11698418, ECO:0000269|PubMed:11802771,
CC ECO:0000269|PubMed:16339536, ECO:0000269|PubMed:23695528,
CC ECO:0000269|Ref.4}.
CC -!- FUNCTION: Isoform 3 does not mediate any NK cell activation.
CC -!- SUBUNIT: Isoform 1 binds to SH2D1A when its cytoplasmic tail is
CC phosphorylated in the presence of FYN (in vitro); low affinity binding,
CC the physiological relevance of the interaction is questioned. Interacts
CC with SH2D1B; in NK cells (PubMed:16339536). Interacts (via ITSM
CC phosphorylated on Tyr-302) with SH2D1B, PTPN6/SHP-1, PTPN11/SHP-2,
CC INPP5D/SHIP1, CSK and FYN (By similarity).
CC {ECO:0000250|UniProtKB:Q8BHK6, ECO:0000269|PubMed:12242590,
CC ECO:0000269|PubMed:16339536}.
CC -!- INTERACTION:
CC Q9NQ25; Q9NQ25: SLAMF7; NbExp=2; IntAct=EBI-3916159, EBI-3916159;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=19A, CS1-L;
CC IsoId=Q9NQ25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ25-2; Sequence=VSP_013781;
CC Name=3; Synonyms=19A24, CS1-S;
CC IsoId=Q9NQ25-3; Sequence=VSP_013782;
CC Name=4;
CC IsoId=Q9NQ25-4; Sequence=VSP_054540, VSP_054541;
CC Name=5;
CC IsoId=Q9NQ25-5; Sequence=VSP_054542;
CC Name=6;
CC IsoId=Q9NQ25-6; Sequence=VSP_055292;
CC Name=7;
CC IsoId=Q9NQ25-7; Sequence=VSP_013781, VSP_055293;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lymph node, peripheral blood
CC leukocytes, bone marrow, small intestine, stomach, appendix, lung and
CC trachea. Expression was detected in NK cells, activated B-cells, NK-
CC cell line but not in promyelocytic, B-, or T-cell lines. Expressed in
CC monocytes. Isoform 3 is expressed at much lower level than isoform 1.
CC {ECO:0000269|PubMed:11220635, ECO:0000269|PubMed:11698418,
CC ECO:0000269|PubMed:11802771, ECO:0000269|PubMed:12242590,
CC ECO:0000269|PubMed:23695528}.
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}.
CC -!- MISCELLANEOUS: Proposed to be involved in systemic lupus erythematosus
CC (SLE) disease process. {ECO:0000269|PubMed:23956418}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB76561.1; Type=Frameshift; Evidence={ECO:0000305};
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; AF291815; AAK11549.1; -; mRNA.
DR EMBL; AF390894; AAL26989.1; -; mRNA.
DR EMBL; AJ271869; CAB76561.1; ALT_FRAME; mRNA.
DR EMBL; AJ276429; CAB81950.2; -; mRNA.
DR EMBL; AB027233; BAB61022.1; -; mRNA.
DR EMBL; AY358512; AAQ88876.1; -; mRNA.
DR EMBL; AK290706; BAF83395.1; -; mRNA.
DR EMBL; AK298499; BAG60706.1; -; mRNA.
DR EMBL; AK298548; BAG60745.1; -; mRNA.
DR EMBL; AK301438; BAG62965.1; -; mRNA.
DR EMBL; AL834424; CAD39085.1; -; mRNA.
DR EMBL; AL121985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52704.1; -; Genomic_DNA.
DR EMBL; BC027867; AAH27867.1; -; mRNA.
DR CCDS; CCDS1209.1; -. [Q9NQ25-1]
DR CCDS; CCDS60321.1; -. [Q9NQ25-5]
DR CCDS; CCDS60322.1; -. [Q9NQ25-6]
DR CCDS; CCDS60323.1; -. [Q9NQ25-4]
DR CCDS; CCDS60324.1; -. [Q9NQ25-2]
DR CCDS; CCDS60325.1; -. [Q9NQ25-7]
DR RefSeq; NP_001269517.1; NM_001282588.1. [Q9NQ25-4]
DR RefSeq; NP_001269518.1; NM_001282589.1. [Q9NQ25-6]
DR RefSeq; NP_001269519.1; NM_001282590.1. [Q9NQ25-2]
DR RefSeq; NP_001269520.1; NM_001282591.1. [Q9NQ25-7]
DR RefSeq; NP_001269521.1; NM_001282592.1. [Q9NQ25-5]
DR RefSeq; NP_001269524.1; NM_001282595.1.
DR RefSeq; NP_067004.3; NM_021181.4. [Q9NQ25-1]
DR AlphaFoldDB; Q9NQ25; -.
DR SMR; Q9NQ25; -.
DR BioGRID; 121782; 20.
DR ELM; Q9NQ25; -.
DR IntAct; Q9NQ25; 16.
DR STRING; 9606.ENSP00000357022; -.
DR ChEMBL; CHEMBL3559386; -.
DR DrugBank; DB06317; Elotuzumab.
DR DrugCentral; Q9NQ25; -.
DR GuidetoPHARMACOLOGY; 2850; -.
DR GlyGen; Q9NQ25; 6 sites.
DR iPTMnet; Q9NQ25; -.
DR PhosphoSitePlus; Q9NQ25; -.
DR BioMuta; SLAMF7; -.
DR DMDM; 66774034; -.
DR CPTAC; CPTAC-1763; -.
DR jPOST; Q9NQ25; -.
DR MassIVE; Q9NQ25; -.
DR MaxQB; Q9NQ25; -.
DR PaxDb; Q9NQ25; -.
DR PeptideAtlas; Q9NQ25; -.
DR PRIDE; Q9NQ25; -.
DR ProteomicsDB; 1858; -.
DR ProteomicsDB; 4815; -.
DR ProteomicsDB; 4826; -.
DR ProteomicsDB; 5326; -.
DR ProteomicsDB; 82055; -. [Q9NQ25-1]
DR ProteomicsDB; 82056; -. [Q9NQ25-2]
DR ProteomicsDB; 82057; -. [Q9NQ25-3]
DR TopDownProteomics; Q9NQ25-2; -. [Q9NQ25-2]
DR ABCD; Q9NQ25; 2 sequenced antibodies.
DR Antibodypedia; 4220; 566 antibodies from 34 providers.
DR DNASU; 57823; -.
DR Ensembl; ENST00000359331.8; ENSP00000352281.4; ENSG00000026751.17. [Q9NQ25-5]
DR Ensembl; ENST00000368042.7; ENSP00000357021.3; ENSG00000026751.17. [Q9NQ25-2]
DR Ensembl; ENST00000368043.8; ENSP00000357022.3; ENSG00000026751.17. [Q9NQ25-1]
DR Ensembl; ENST00000441662.6; ENSP00000405605.2; ENSG00000026751.17. [Q9NQ25-6]
DR Ensembl; ENST00000444090.6; ENSP00000416592.2; ENSG00000026751.17. [Q9NQ25-4]
DR Ensembl; ENST00000458602.6; ENSP00000409965.2; ENSG00000026751.17. [Q9NQ25-7]
DR GeneID; 57823; -.
DR KEGG; hsa:57823; -.
DR MANE-Select; ENST00000368043.8; ENSP00000357022.3; NM_021181.5; NP_067004.3.
DR UCSC; uc001fwq.5; human. [Q9NQ25-1]
DR CTD; 57823; -.
DR DisGeNET; 57823; -.
DR GeneCards; SLAMF7; -.
DR HGNC; HGNC:21394; SLAMF7.
DR HPA; ENSG00000026751; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR MIM; 606625; gene.
DR neXtProt; NX_Q9NQ25; -.
DR OpenTargets; ENSG00000026751; -.
DR PharmGKB; PA134977110; -.
DR VEuPathDB; HostDB:ENSG00000026751; -.
DR eggNOG; ENOG502SRN2; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_069386_1_1_1; -.
DR InParanoid; Q9NQ25; -.
DR OMA; CMTNLTC; -.
DR OrthoDB; 990343at2759; -.
DR PhylomeDB; Q9NQ25; -.
DR TreeFam; TF334964; -.
DR PathwayCommons; Q9NQ25; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q9NQ25; -.
DR BioGRID-ORCS; 57823; 6 hits in 1067 CRISPR screens.
DR GeneWiki; SLAMF7; -.
DR GenomeRNAi; 57823; -.
DR Pharos; Q9NQ25; Tclin.
DR PRO; PR:Q9NQ25; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NQ25; protein.
DR Bgee; ENSG00000026751; Expressed in granulocyte and 146 other tissues.
DR ExpressionAtlas; Q9NQ25; baseline and differential.
DR Genevisible; Q9NQ25; 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; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
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 SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Innate immunity; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..335
FT /note="SLAM family member 7"
FT /id="PRO_0000014963"
FT TOPO_DOM 23..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..124
FT /note="Ig-like V-type"
FT DOMAIN 131..206
FT /note="Ig-like C2-type"
FT REGION 278..296
FT /note="Interaction with FYN when phosphorylated at Tyr-284"
FT /evidence="ECO:0000250|UniProtKB:Q8BHK6"
FT MOTIF 302..307
FT /note="ITSM"
FT /evidence="ECO:0000250|UniProtKB:Q13291,
FT ECO:0000250|UniProtKB:Q8BHK6"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 145..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 151..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 19..125
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_013781"
FT VAR_SEQ 126..256
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055292"
FT VAR_SEQ 127..165
FT /note="HLSKPKVTMGLQSNKNGTCVTNLTCCMEHGEEDVIYTWK -> NNPKGRSSK
FT YGLLHCGNTEKDGKSPLTAHDARHTKAICL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054540"
FT VAR_SEQ 166..335
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054541"
FT VAR_SEQ 217..256
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055293"
FT VAR_SEQ 258..335
FT /note="YIEEKKRVDICRETPNICPHSGENTEYDTIPHTNRTILKEDPANTVYSTVEI
FT PKKMENPHSLLTMPDTPRLFAYENVI -> NNPKGRSSKYGLLHCGNTEKDGKSPLTAH
FT DARHTKAICL (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_054542"
FT VAR_SEQ 258..296
FT /note="YIEEKKRVDICRETPNICPHSGENTEYDTIPHTNRTILK -> NNPKGRSSK
FT YGLLHCGNTEKDGKSPLTAHDARHTKAICL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11802771,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013782"
FT VARIANT 175
FT /note="H -> Y (in dbSNP:rs35325048)"
FT /id="VAR_049938"
FT VARIANT 302
FT /note="T -> M (in dbSNP:rs2295617)"
FT /id="VAR_049939"
FT CONFLICT 135
FT /note="M -> L (in Ref. 3; CAB81950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37421 MW; D09ABBCFF74BE8D4 CRC64;
MAGSPTCLTL IYILWQLTGS AASGPVKELV GSVGGAVTFP LKSKVKQVDS IVWTFNTTPL
VTIQPEGGTI IVTQNRNRER VDFPDGGYSL KLSKLKKNDS GIYYVGIYSS SLQQPSTQEY
VLHVYEHLSK PKVTMGLQSN KNGTCVTNLT CCMEHGEEDV IYTWKALGQA ANESHNGSIL
PISWRWGESD MTFICVARNP VSRNFSSPIL ARKLCEGAAD DPDSSMVLLC LLLVPLLLSL
FVLGLFLWFL KRERQEEYIE EKKRVDICRE TPNICPHSGE NTEYDTIPHT NRTILKEDPA
NTVYSTVEIP KKMENPHSLL TMPDTPRLFA YENVI
