ID SLAF5_HUMAN Reviewed; 345 AA. AC Q9UIB8; B2R8T1; B7Z3R8; O15430; O95266; O95660; Q5H9R1; Q6FHA8; Q8WLP1; AC Q8WWI8; Q9UF04; Q9UIB6; Q9UIB7; Q9UIT7; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 05-FEB-2025, entry version 185. DE RecName: Full=SLAM family member 5; DE AltName: Full=Cell surface antigen MAX.3; DE AltName: Full=Hly9-beta; DE AltName: Full=Leukocyte differentiation antigen CD84; DE AltName: Full=Signaling lymphocytic activation molecule 5; DE AltName: CD_antigen=CD84; DE Flags: Precursor; GN Name=CD84; Synonyms=SLAMF5; 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 3), GLYCOSYLATION, AND TISSUE RP SPECIFICITY. RX PubMed=9310491; RA de la Fuente M.A., Pizcueta P., Nadal M., Bosch J., Engel P.; RT "CD84 leukocyte antigen is a new member of the Ig superfamily."; RL Blood 90:2398-2405(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 22-35, RP GLYCOSYLATION, AND TISSUE SPECIFICITY. RX PubMed=10698700; DOI=10.1042/bj3460729; RA Krause S.W., Rehli M., Heinz S., Ebner R., Andreesen R.; RT "Characterization of MAX.3 antigen, a glycoprotein expressed on mature RT macrophages, dendritic cells and blood platelets: identity with CD84."; RL Biochem. J. 346:729-736(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6). RX PubMed=10746783; DOI=10.1034/j.1399-0039.2000.550203.x; RA Palou E., Pirotto F., Sole J., Freed J.H., Peral B., Vilardell C., RA Vilella R., Vives J., Gaya A.; RT "Genomic characterization of CD84 reveals the existence of five isoforms RT differing in their cytoplasmic domains."; RL Tissue Antigens 55:118-127(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7). RC TISSUE=Thalamus, and Umbilical cord blood; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Semen; 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 MRNA] (ISOFORM 3). RC TISSUE=Lymph; 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 [10] RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH SH2D1A AND RP PTPN11. RX PubMed=11389028; DOI=10.1182/blood.v97.12.3867; RA Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P., RA Terhorst C.; RT "Cell surface receptors Ly-9 and CD84 recruit the X-linked RT lymphoproliferative disease gene product SAP."; RL Blood 97:3867-3874(2001). RN [11] RP INTERACTION WITH PTPN6 AND PTPN11. RX PubMed=11414741; DOI=10.1006/clim.2001.5035; RA Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E., Ochs H.D., RA Notarangelo L.D., Duckett C.S.; RT "Distinct interactions of the X-linked lymphoproliferative syndrome gene RT product SAP with cytoplasmic domains of members of the CD2 receptor RT family."; RL Clin. Immunol. 100:15-23(2001). RN [12] RP 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 [13] RP TISSUE SPECIFICITY, HOMODIMERIZATION, AND FUNCTION. RX PubMed=11564780; DOI=10.4049/jimmunol.167.7.3668; RA Martin M., Romero X., de la Fuente M.A., Tovar V., Zapater N., RA Esplugues E., Pizcueta P., Bosch J., Engel P.; RT "CD84 functions as a homophilic adhesion molecule and enhances IFN-gamma RT secretion: adhesion is mediated by Ig-like domain 1."; RL J. Immunol. 167:3668-3676(2001). RN [14] RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND RP INTERACTION WITH SH2D1A AND SH2D1B. RX PubMed=12115647; RX DOI=10.1002/1521-4141(200206)32:6<1640::aid-immu1640>3.0.co;2-s; RA Tangye S.G., van de Weerdt B.C.M., Avery D.T., Hodgkin P.D.; RT "CD84 is up-regulated on a major population of human memory B cells and RT recruits the SH2 domain containing proteins SAP and EAT-2."; RL Eur. J. Immunol. 32:1640-1649(2002). RN [15] RP INTERACTION WITH SH2D1A; SH2D1B; INPP5D AND PTPN11, AND PHOSPHORYLATION AT RP TYR-279 AND TYR-316. 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 [16] RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-279 AND TYR-316. RX PubMed=12928397; DOI=10.4049/jimmunol.171.5.2485; RA Tangye S.G., Nichols K.E., Hare N.J., van de Weerdt B.C.M.; RT "Functional requirements for interactions between CD84 and Src homology 2 RT domain-containing proteins and their contribution to human T cell RT activation."; RL J. Immunol. 171:2485-2495(2003). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12962726; DOI=10.1016/s0301-472x(03)00187-5; RA Zaiss M., Hirtreiter C., Rehli M., Rehm A., Kunz-Schughart L.A., RA Andreesen R., Hennemann B.; RT "CD84 expression on human hematopoietic progenitor cells."; RL Exp. Hematol. 31:798-805(2003). RN [18] RP TISSUE SPECIFICITY. RX PubMed=15245368; DOI=10.1111/j.1399-0039.2004.00247.x; RA Romero X., Benitez D., March S., Vilella R., Miralpeix M., Engel P.; RT "Differential expression of SAP and EAT-2-binding leukocyte cell-surface RT molecules CD84, CD150 (SLAM), CD229 (Ly9) and CD244 (2B4)."; RL Tissue Antigens 64:132-144(2004). RN [19] RP FUNCTION, PHOSPHORYLATION AT TYR-296 AND TYR-316, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=16037392; DOI=10.1182/blood-2005-01-0333; RA Nanda N., Andre P., Bao M., Clauser K., Deguzman F., Howie D., Conley P.B., RA Terhorst C., Phillips D.R.; RT "Platelet aggregation induces platelet aggregate stability via SLAM family RT receptor signaling."; RL Blood 106:3028-3034(2005). RN [20] RP FUNCTION, PHOSPHORYLATION AT TYR-296 AND TYR-341, AND TISSUE SPECIFICITY. RX PubMed=22068234; DOI=10.4049/jimmunol.1101626; RA Alvarez-Errico D., Oliver-Vila I., Ainsua-Enrich E., Gilfillan A.M., RA Picado C., Sayos J., Martin M.; RT "CD84 negatively regulates IgE high-affinity receptor signaling in human RT mast cells."; RL J. Immunol. 187:5577-5586(2011). RN [21] RP FUNCTION. RX PubMed=29434592; DOI=10.3389/fimmu.2018.00062; RA Agod Z., Pazmandi K., Bencze D., Vereb G., Biro T., Szabo A., RA Rajnavolgyi E., Bacsi A., Engel P., Lanyi A.; RT "Signaling lymphocyte activation molecule family 5 enhances autophagy and RT fine-tunes cytokine response in monocyte-derived dendritic cells via RT stabilization of interferon regulatory factor 8."; RL Front. Immunol. 9:62-62(2018). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 22-131, SUBUNIT, AND MUTAGENESIS RP OF THR-55; TYR-62; THR-77; HIS-78; ASP-110; ASN-112 AND THR-119. RX PubMed=17563375; DOI=10.1073/pnas.0703893104; RA Yan Q., Malashkevich V.N., Fedorov A., Fedorov E., Cao E., Lary J.W., RA Cole J.L., Nathenson S.G., Almo S.C.; RT "Structure of CD84 provides insight into SLAM family function."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10583-10588(2007). 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. Can CC mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and CC SH2D1B (By similarity). Increases proliferative responses of activated CC T-cells and SH2D1A/SAP does not seem be required for this process. CC Homophilic interactions enhance interferon gamma/IFNG secretion in CC lymphocytes and induce platelet stimulation via a SH2D1A-dependent CC pathway. May serve as a marker for hematopoietic progenitor cells CC (PubMed:11564780, PubMed:12115647, PubMed:12928397, PubMed:12962726, CC PubMed:16037392) Required for a prolonged T-cell:B-cell contact, CC optimal T follicular helper function, and germinal center formation. In CC germinal centers involved in maintaining B-cell tolerance and in CC preventing autoimmunity (By similarity). In mast cells negatively CC regulates high affinity immunoglobulin epsilon receptor signaling; CC independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 CC (PubMed:22068234). In macrophages enhances LPS-induced MAPK CC phosphorylation and NF-kappaB activation and modulates LPS-induced CC cytokine secretion; involving ITSM 2 (By similarity). Positively CC regulates macroautophagy in primary dendritic cells via stabilization CC of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8 CC (PubMed:29434592). {ECO:0000250|UniProtKB:Q18PI6, CC ECO:0000269|PubMed:11564780, ECO:0000269|PubMed:12115647, CC ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:12962726, CC ECO:0000269|PubMed:16037392, ECO:0000269|PubMed:22068234, CC ECO:0000269|PubMed:29434592, ECO:0000305}. CC -!- SUBUNIT: Homodimer; via its extracellular domain. Forms a head to tail CC dimer with a CD48 molecule from another cell. Interacts with SH2 CC domain-containing proteins SH2D1A/SAP and SH2D1B/EAT-2. Interacts with CC tyrosine-protein phosphatases PTPN6/SHP-1 and PTPN11//SHP-2 via its CC phosphorylated cytoplasmic domain, and this interaction is blocked by CC SH2D1A. Interacts (via phosphorylated ITSM 1 and 2) with INPP5D/SHIP1. CC {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:11414741, CC ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12458214, CC ECO:0000269|PubMed:17563375}. CC -!- INTERACTION: CC Q9UIB8; Q9UIB8: CD84; NbExp=3; IntAct=EBI-6691679, EBI-6691679; CC Q9UIB8; O14796: SH2D1B; NbExp=3; IntAct=EBI-6691679, EBI-3923013; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389028, CC ECO:0000269|PubMed:12962726}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12962726}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=CD84a; CC IsoId=Q9UIB8-1; Sequence=Displayed; CC Name=2; Synonyms=CD84b; CC IsoId=Q9UIB8-2; Sequence=VSP_020852; CC Name=3; Synonyms=CD84c; CC IsoId=Q9UIB8-3; Sequence=VSP_020851; CC Name=4; Synonyms=CD84e; CC IsoId=Q9UIB8-4; Sequence=VSP_020854, VSP_020856; CC Name=5; Synonyms=CD84d; CC IsoId=Q9UIB8-5; Sequence=VSP_020853, VSP_020855; CC Name=6; Synonyms=CD84s; CC IsoId=Q9UIB8-6; Sequence=VSP_020849, VSP_020850; CC Name=7; CC IsoId=Q9UIB8-7; Sequence=VSP_020848, VSP_020851; CC -!- TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues, CC such as lymph node, spleen and peripheral leukocytes. Expressed in CC macrophages, B-cells, monocytes, platelets, thymocytes, T-cells and CC dendritic cells. Highly expressed in memory T-cells. Expressed in mast CC cells. {ECO:0000269|PubMed:10698700, ECO:0000269|PubMed:11564780, CC ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12962726, CC ECO:0000269|PubMed:15245368, ECO:0000269|PubMed:22068234, CC ECO:0000269|PubMed:9310491}. CC -!- DEVELOPMENTAL STAGE: Expression is slightly increased in naive B-cells CC after the first dividion. By contrast, expression on memory B-cells CC decreased with each successive division. {ECO:0000269|PubMed:12115647}. 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 containingbinding 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, ECO:0000305|PubMed:11313386}. CC -!- PTM: Phosphorylated by tyrosine-protein kinase LCK on tyrosine residues CC following ligation induced by agonist monoclonal antibody. The CC association with SH2D1A is dependent of tyrosine phosphorylation of its CC cytoplasmic domain. Phosphorylated on Tyr-296 and Tyr-316 following CC platelet aggregation. Phosphorylated on tyrosine residues upon high CC affinity immunoglobulin epsilon receptor aggregation in mast cells. CC {ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12115647, CC ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:16037392, CC ECO:0000269|PubMed:22068234}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10698700, CC ECO:0000269|PubMed:9310491}. 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; U82988; AAB84364.1; -; mRNA. DR EMBL; AJ223324; CAA11264.1; -; mRNA. DR EMBL; AF054815; AAF21721.1; -; mRNA. DR EMBL; AF054816; AAF21722.1; -; mRNA. DR EMBL; AF054817; AAF21723.1; -; mRNA. DR EMBL; AF054818; AAF21724.1; -; mRNA. DR EMBL; AF081189; AAD13155.1; -; Genomic_DNA. DR EMBL; AH008972; AAF21784.1; -; Genomic_DNA. DR EMBL; AH008376; AAF06840.1; -; Genomic_DNA. DR EMBL; U96627; AAD04232.1; -; mRNA. DR EMBL; Y12632; CAA73181.1; -; mRNA. DR EMBL; AK296290; BAH12304.1; -; mRNA. DR EMBL; AK313496; BAG36278.1; -; mRNA. DR EMBL; CR541847; CAG46645.1; -; mRNA. DR EMBL; CR933666; CAI45963.1; -; mRNA. DR EMBL; AL138930; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52707.1; -; Genomic_DNA. DR EMBL; BC020063; AAH20063.1; -; mRNA. DR CCDS; CCDS1206.1; -. [Q9UIB8-3] DR CCDS; CCDS53395.1; -. [Q9UIB8-7] DR CCDS; CCDS53396.1; -. [Q9UIB8-1] DR CCDS; CCDS53397.1; -. [Q9UIB8-5] DR CCDS; CCDS81388.1; -. [Q9UIB8-2] DR RefSeq; NP_001171808.1; NM_001184879.1. [Q9UIB8-1] DR RefSeq; NP_001171810.1; NM_001184881.1. [Q9UIB8-5] DR RefSeq; NP_001171811.1; NM_001184882.1. [Q9UIB8-7] DR RefSeq; NP_001317671.1; NM_001330742.1. [Q9UIB8-2] DR RefSeq; NP_003865.1; NM_003874.3. [Q9UIB8-3] DR PDB; 2PKD; X-ray; 2.04 A; A/B/C/D/E/F=22-131. DR PDBsum; 2PKD; -. DR AlphaFoldDB; Q9UIB8; -. DR SMR; Q9UIB8; -. DR BioGRID; 114359; 7. DR DIP; DIP-60957N; -. DR ELM; Q9UIB8; -. DR IntAct; Q9UIB8; 4. DR MINT; Q9UIB8; -. DR STRING; 9606.ENSP00000312367; -. DR GlyCosmos; Q9UIB8; 1 site, No reported glycans. DR GlyGen; Q9UIB8; 1 site. DR iPTMnet; Q9UIB8; -. DR PhosphoSitePlus; Q9UIB8; -. DR BioMuta; CD84; -. DR DMDM; 74762772; -. DR MassIVE; Q9UIB8; -. DR PaxDb; 9606-ENSP00000312367; -. DR PeptideAtlas; Q9UIB8; -. DR ProteomicsDB; 84484; -. [Q9UIB8-1] DR ProteomicsDB; 84485; -. [Q9UIB8-2] DR ProteomicsDB; 84486; -. [Q9UIB8-3] DR ProteomicsDB; 84487; -. [Q9UIB8-4] DR ProteomicsDB; 84488; -. [Q9UIB8-5] DR ProteomicsDB; 84489; -. [Q9UIB8-6] DR ProteomicsDB; 84490; -. [Q9UIB8-7] DR Antibodypedia; 20494; 794 antibodies from 42 providers. DR DNASU; 8832; -. DR Ensembl; ENST00000311224.8; ENSP00000312367.4; ENSG00000066294.15. [Q9UIB8-1] DR Ensembl; ENST00000368048.7; ENSP00000357027.3; ENSG00000066294.15. [Q9UIB8-2] DR Ensembl; ENST00000368051.3; ENSP00000357030.3; ENSG00000066294.15. [Q9UIB8-5] DR Ensembl; ENST00000368054.8; ENSP00000357033.4; ENSG00000066294.15. [Q9UIB8-3] DR Ensembl; ENST00000534968.5; ENSP00000442845.1; ENSG00000066294.15. [Q9UIB8-7] DR GeneID; 8832; -. DR KEGG; hsa:8832; -. DR MANE-Select; ENST00000368054.8; ENSP00000357033.4; NM_003874.4; NP_003865.1. [Q9UIB8-3] DR UCSC; uc001fwf.5; human. [Q9UIB8-1] DR AGR; HGNC:1704; -. DR CTD; 8832; -. DR DisGeNET; 8832; -. DR GeneCards; CD84; -. DR HGNC; HGNC:1704; CD84. DR HPA; ENSG00000066294; Tissue enhanced (lymphoid). DR MIM; 604513; gene. DR neXtProt; NX_Q9UIB8; -. DR OpenTargets; ENSG00000066294; -. DR PharmGKB; PA26242; -. DR VEuPathDB; HostDB:ENSG00000066294; -. DR eggNOG; ENOG502SB7W; Eukaryota. DR GeneTree; ENSGT01030000234540; -. DR HOGENOM; CLU_069386_1_1_1; -. DR InParanoid; Q9UIB8; -. DR OMA; YTYVMVT; -. DR OrthoDB; 8741746at2759; -. DR PhylomeDB; Q9UIB8; -. DR TreeFam; TF334964; -. DR PathwayCommons; Q9UIB8; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR SignaLink; Q9UIB8; -. DR BioGRID-ORCS; 8832; 10 hits in 1149 CRISPR screens. DR EvolutionaryTrace; Q9UIB8; -. DR GeneWiki; CD84; -. DR GenomeRNAi; 8832; -. DR Pharos; Q9UIB8; Tbio. DR PRO; PR:Q9UIB8; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UIB8; protein. DR Bgee; ENSG00000066294; Expressed in tibia and 170 other cell types or tissues. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0032685; P:negative regulation of granulocyte macrophage colony-stimulating factor production; IDA:UniProtKB. DR GO; GO:0032701; P:negative regulation of interleukin-18 production; IDA:UniProtKB. DR GO; GO:0033004; P:negative regulation of mast cell activation; IDA:UniProtKB. DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IDA:UniProtKB. DR GO; GO:2001256; P:regulation of store-operated calcium entry; IDA:UniProtKB. DR GO; GO:0042110; P:T cell activation; IBA:GO_Central. DR CDD; cd16842; Ig_SLAM-like_N; 1. DR FunFam; 2.60.40.10:FF:000470; SLAM family member 7; 1. DR FunFam; 2.60.40.10:FF:000820; SLAM family member 7; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR015631; CD2/SLAM_rcpt. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR PANTHER; PTHR12080:SF103; SLAM FAMILY MEMBER 5; 1. DR Pfam; PF13927; Ig_3; 1. DR SMART; SM00409; IG; 2. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Autophagy; KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; Membrane; KW Phosphoprotein; Proteomics identification; Receptor; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:10698700" FT CHAIN 22..345 FT /note="SLAM family member 5" FT /id="PRO_0000252029" FT TOPO_DOM 22..225 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 226..246 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 247..345 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 26..129 FT /note="Ig-like V-type" FT DOMAIN 135..207 FT /note="Ig-like C2-type" FT REGION 326..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 277..282 FT /note="ITSM 1" FT /evidence="ECO:0000250|UniProtKB:Q13291" FT MOTIF 314..319 FT /note="ITSM 2" FT /evidence="ECO:0000250|UniProtKB:Q13291" FT COMPBIAS 328..345 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 279 FT /note="Phosphotyrosine" FT /evidence="ECO:0000305|PubMed:12458214" FT MOD_RES 296 FT /note="Phosphotyrosine; by LYN" FT /evidence="ECO:0000269|PubMed:16037392, FT ECO:0000269|PubMed:22068234" FT MOD_RES 316 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:16037392, FT ECO:0000305|PubMed:12458214" FT MOD_RES 341 FT /note="Phosphotyrosine; by FES" FT /evidence="ECO:0000269|PubMed:22068234" FT CARBOHYD 150 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 155..193 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 16..130 FT /note="WPEAAGKDSEIFTVNGILGESVTFPVNIQEPRQVKIIAWTSKTSVAYVTPGD FT SETAPVVTVTHRNYYERIHALGPNYNLVISDLRMEDAGDYKADINTQADPYTTTKRYNL FT QIYR -> C (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005" FT /id="VSP_020848" FT VAR_SEQ 214..241 FT /note="DIAMGFRTHHTGLLSVLAMFFLLVLILS -> GNQLCPSLLVSLRDHSEELQ FT GLNVGHIL (in isoform 6)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020849" FT VAR_SEQ 242..345 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020850" FT VAR_SEQ 254..271 FT /note="GRIFPEGSCLNTFTKNPY -> D (in isoform 3 and isoform FT 7)" FT /evidence="ECO:0000303|PubMed:10698700, FT ECO:0000303|PubMed:10746783, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:9310491, ECO:0000303|Ref.4" FT /id="VSP_020851" FT VAR_SEQ 254..259 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020852" FT VAR_SEQ 255..272 FT /note="RIFPEGSCLNTFTKNPYA -> ASLQGRASEHSLFRSAVC (in isoform FT 5)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020853" FT VAR_SEQ 261..280 FT /note="SCLNTFTKNPYAASKKTIYT -> KMWKLTFSPPGTEAIYPRFS (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020854" FT VAR_SEQ 273..345 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020855" FT VAR_SEQ 281..345 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10746783" FT /id="VSP_020856" FT MUTAGEN 55 FT /note="T->A: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 62 FT /note="Y->A: No effect." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 62 FT /note="Y->D: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 77 FT /note="T->A: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 78 FT /note="H->A: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 110 FT /note="D->A: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 112 FT /note="N->A: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 119 FT /note="T->A: Loss of dimerization." FT /evidence="ECO:0000269|PubMed:17563375" FT MUTAGEN 279 FT /note="Y->F: Reduced tyrosine phosphorylation, reduced FT binding of SH2D1B and loss of binding of SH2D1A." FT /evidence="ECO:0000269|PubMed:12928397" FT MUTAGEN 316 FT /note="Y->F: Reduced tyrosine phosphorylation and reduced FT binding of SH2D1B. Loss of phosphorylation and loss of FT binding of SH2D1A and SH2D1B; when associated with F-279." FT /evidence="ECO:0000269|PubMed:12928397" FT CONFLICT 311 FT /note="P -> S (in Ref. 4; CAG46645)" FT /evidence="ECO:0000305" FT STRAND 27..32 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 49..64 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 73..76 FT /evidence="ECO:0007829|PDB:2PKD" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:2PKD" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:2PKD" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 105..115 FT /evidence="ECO:0007829|PDB:2PKD" FT STRAND 118..129 FT /evidence="ECO:0007829|PDB:2PKD" SQ SEQUENCE 345 AA; 38782 MW; DA06BC5A682E62DE CRC64; MAQHHLWILL LCLQTWPEAA GKDSEIFTVN GILGESVTFP VNIQEPRQVK IIAWTSKTSV AYVTPGDSET APVVTVTHRN YYERIHALGP NYNLVISDLR MEDAGDYKAD INTQADPYTT TKRYNLQIYR RLGKPKITQS LMASVNSTCN VTLTCSVEKE EKNVTYNWSP LGEEGNVLQI FQTPEDQELT YTCTAQNPVS NNSDSISARQ LCADIAMGFR THHTGLLSVL AMFFLLVLIL SSVFLFRLFK RRQGRIFPEG SCLNTFTKNP YAASKKTIYT YIMASRNTQP AESRIYDEIL QSKVLPSKEE PVNTVYSEVQ FADKMGKAST QDSKPPGTSS YEIVI //