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 24-JAN-2024, entry version 181. 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; 22. 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 GlyCosmos; Q9NQ25; 6 sites, No reported glycans. 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; 9606-ENSP00000357022; -. DR PeptideAtlas; 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; 655 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 AGR; HGNC:21394; -. 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; DSIVWIF; -. DR OrthoDB; 5265037at2759; -. 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 1153 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 147 other cell types or tissues. DR ExpressionAtlas; Q9NQ25; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. 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; Immunoglobulins; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR PANTHER; PTHR12080:SF46; SLAM FAMILY MEMBER 7; 1. DR Pfam; PF07686; V-set; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q9NQ25; HS. 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 //