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SLAM family member 5 (Cell surface antigen MAX.3) (Hly9-beta) (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84)

 SLAF5_HUMAN             Reviewed;         345 AA.
Q9UIB8; B2R8T1; B7Z3R8; O15430; O95266; O95660; Q5H9R1; Q6FHA8; Q8WLP1;
Q8WWI8; Q9UF04; Q9UIB6; Q9UIB7; Q9UIT7;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-APR-2021, entry version 166.
RecName: Full=SLAM family member 5;
AltName: Full=Cell surface antigen MAX.3;
AltName: Full=Hly9-beta;
AltName: Full=Leukocyte differentiation antigen CD84;
AltName: Full=Signaling lymphocytic activation molecule 5;
AltName: CD_antigen=CD84;
Flags: Precursor;
Name=CD84; Synonyms=SLAMF5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), GLYCOSYLATION, AND TISSUE
SPECIFICITY.
PubMed=9310491;
de la Fuente M.A., Pizcueta P., Nadal M., Bosch J., Engel P.;
"CD84 leukocyte antigen is a new member of the Ig superfamily.";
Blood 90:2398-2405(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 22-35,
GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=10698700; DOI=10.1042/bj3460729;
Krause S.W., Rehli M., Heinz S., Ebner R., Andreesen R.;
"Characterization of MAX.3 antigen, a glycoprotein expressed on mature
macrophages, dendritic cells and blood platelets: identity with CD84.";
Biochem. J. 346:729-736(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
PubMed=10746783; DOI=10.1034/j.1399-0039.2000.550203.x;
Palou E., Pirotto F., Sole J., Freed J.H., Peral B., Vilardell C.,
Vilella R., Vives J., Gaya A.;
"Genomic characterization of CD84 reveals the existence of five isoforms
differing in their cytoplasmic domains.";
Tissue Antigens 55:118-127(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
TISSUE=Thalamus, and Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Semen;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lymph;
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).
[10]
PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH SH2D1A AND
PTPN11.
PubMed=11389028; DOI=10.1182/blood.v97.12.3867;
Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P.,
Terhorst C.;
"Cell surface receptors Ly-9 and CD84 recruit the X-linked
lymphoproliferative disease gene product SAP.";
Blood 97:3867-3874(2001).
[11]
INTERACTION WITH PTPN6 AND PTPN11.
PubMed=11414741; DOI=10.1006/clim.2001.5035;
Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E., Ochs H.D.,
Notarangelo L.D., Duckett C.S.;
"Distinct interactions of the X-linked lymphoproliferative syndrome gene
product SAP with cytoplasmic domains of members of the CD2 receptor
family.";
Clin. Immunol. 100:15-23(2001).
[12]
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).
[13]
TISSUE SPECIFICITY, HOMODIMERIZATION, AND FUNCTION.
PubMed=11564780; DOI=10.4049/jimmunol.167.7.3668;
Martin M., Romero X., de la Fuente M.A., Tovar V., Zapater N.,
Esplugues E., Pizcueta P., Bosch J., Engel P.;
"CD84 functions as a homophilic adhesion molecule and enhances IFN-gamma
secretion: adhesion is mediated by Ig-like domain 1.";
J. Immunol. 167:3668-3676(2001).
[14]
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND
INTERACTION WITH SH2D1A AND SH2D1B.
PubMed=12115647;
DOI=10.1002/1521-4141(200206)32:6<1640::aid-immu1640>3.0.co;2-s;
Tangye S.G., van de Weerdt B.C.M., Avery D.T., Hodgkin P.D.;
"CD84 is up-regulated on a major population of human memory B cells and
recruits the SH2 domain containing proteins SAP and EAT-2.";
Eur. J. Immunol. 32:1640-1649(2002).
[15]
INTERACTION WITH SH2D1A; SH2D1B; INPP5D AND PTPN11, AND PHOSPHORYLATION AT
TYR-279 AND TYR-316.
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).
[16]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-279 AND TYR-316.
PubMed=12928397; DOI=10.4049/jimmunol.171.5.2485;
Tangye S.G., Nichols K.E., Hare N.J., van de Weerdt B.C.M.;
"Functional requirements for interactions between CD84 and Src homology 2
domain-containing proteins and their contribution to human T cell
activation.";
J. Immunol. 171:2485-2495(2003).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12962726; DOI=10.1016/s0301-472x(03)00187-5;
Zaiss M., Hirtreiter C., Rehli M., Rehm A., Kunz-Schughart L.A.,
Andreesen R., Hennemann B.;
"CD84 expression on human hematopoietic progenitor cells.";
Exp. Hematol. 31:798-805(2003).
[18]
TISSUE SPECIFICITY.
PubMed=15245368; DOI=10.1111/j.1399-0039.2004.00247.x;
Romero X., Benitez D., March S., Vilella R., Miralpeix M., Engel P.;
"Differential expression of SAP and EAT-2-binding leukocyte cell-surface
molecules CD84, CD150 (SLAM), CD229 (Ly9) and CD244 (2B4).";
Tissue Antigens 64:132-144(2004).
[19]
FUNCTION, PHOSPHORYLATION AT TYR-296 AND TYR-316, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16037392; DOI=10.1182/blood-2005-01-0333;
Nanda N., Andre P., Bao M., Clauser K., Deguzman F., Howie D., Conley P.B.,
Terhorst C., Phillips D.R.;
"Platelet aggregation induces platelet aggregate stability via SLAM family
receptor signaling.";
Blood 106:3028-3034(2005).
[20]
FUNCTION, PHOSPHORYLATION AT TYR-296 AND TYR-341, AND TISSUE SPECIFICITY.
PubMed=22068234; DOI=10.4049/jimmunol.1101626;
Alvarez-Errico D., Oliver-Vila I., Ainsua-Enrich E., Gilfillan A.M.,
Picado C., Sayos J., Martin M.;
"CD84 negatively regulates IgE high-affinity receptor signaling in human
mast cells.";
J. Immunol. 187:5577-5586(2011).
[21]
FUNCTION.
PubMed=29434592; DOI=10.3389/fimmu.2018.00062;
Agod Z., Pazmandi K., Bencze D., Vereb G., Biro T., Szabo A.,
Rajnavolgyi E., Bacsi A., Engel P., Lanyi A.;
"Signaling lymphocyte activation molecule family 5 enhances autophagy and
fine-tunes cytokine response in monocyte-derived dendritic cells via
stabilization of interferon regulatory factor 8.";
Front. Immunol. 9:62-62(2018).
[22]
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 22-131, SUBUNIT, AND MUTAGENESIS
OF THR-55; TYR-62; THR-77; HIS-78; ASP-110; ASN-112 AND THR-119.
PubMed=17563375; DOI=10.1073/pnas.0703893104;
Yan Q., Malashkevich V.N., Fedorov A., Fedorov E., Cao E., Lary J.W.,
Cole J.L., Nathenson S.G., Almo S.C.;
"Structure of CD84 provides insight into SLAM family function.";
Proc. Natl. Acad. Sci. U.S.A. 104:10583-10588(2007).
-!- 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. Can
mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and
SH2D1B (By similarity). Increases proliferative responses of activated
T-cells and SH2D1A/SAP does not seem be required for this process.
Homophilic interactions enhance interferon gamma/IFNG secretion in
lymphocytes and induce platelet stimulation via a SH2D1A-dependent
pathway. May serve as a marker for hematopoietic progenitor cells
(PubMed:11564780, PubMed:12115647. PubMed:12928397, PubMed:12962726,
PubMed:16037392) Required for a prolonged T-cell:B-cell contact,
optimal T follicular helper function, and germinal center formation. In
germinal centers involved in maintaining B-cell tolerance and in
preventing autoimmunity (By similarity). In mast cells negatively
regulates high affinity immunoglobulin epsilon receptor signaling;
independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1
(PubMed:22068234). In macrophages enhances LPS-induced MAPK
phosphorylation and NF-kappaB activation and modulates LPS-induced
cytokine secretion; involving ITSM 2 (By similarity). Positively
regulates macroautophagy in primary dendritic cells via stabilization
of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8
(PubMed:29434592). {ECO:0000250|UniProtKB:Q18PI6,
ECO:0000269|PubMed:11564780, ECO:0000269|PubMed:12115647,
ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:12962726,
ECO:0000269|PubMed:16037392, ECO:0000269|PubMed:22068234,
ECO:0000269|PubMed:29434592, ECO:0000305}.
-!- SUBUNIT: Homodimer; via its extracellular domain. Forms a head to tail
dimer with a CD48 molecule from another cell. Interacts with SH2
domain-containing proteins SH2D1A/SAP and SH2D1B/EAT-2. Interacts with
tyrosine-protein phosphatases PTPN6/SHP-1 and PTPN11//SHP-2 via its
phosphorylated cytoplasmic domain, and this interaction is blocked by
SH2D1A. Interacts (via phosphorylated ITSM 1 and 2) with INPP5D/SHIP1.
{ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:11414741,
ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12458214,
ECO:0000269|PubMed:17563375}.
-!- INTERACTION:
Q9UIB8; Q9UIB8: CD84; NbExp=3; IntAct=EBI-6691679, EBI-6691679;
Q9UIB8; O14796: SH2D1B; NbExp=3; IntAct=EBI-6691679, EBI-3923013;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11389028,
ECO:0000269|PubMed:12962726}; Single-pass type I membrane protein
{ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12962726}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=CD84a;
IsoId=Q9UIB8-1; Sequence=Displayed;
Name=2; Synonyms=CD84b;
IsoId=Q9UIB8-2; Sequence=VSP_020852;
Name=3; Synonyms=CD84c;
IsoId=Q9UIB8-3; Sequence=VSP_020851;
Name=4; Synonyms=CD84e;
IsoId=Q9UIB8-4; Sequence=VSP_020854, VSP_020856;
Name=5; Synonyms=CD84d;
IsoId=Q9UIB8-5; Sequence=VSP_020853, VSP_020855;
Name=6; Synonyms=CD84s;
IsoId=Q9UIB8-6; Sequence=VSP_020849, VSP_020850;
Name=7;
IsoId=Q9UIB8-7; Sequence=VSP_020848, VSP_020851;
-!- TISSUE SPECIFICITY: Predominantly expressed in hematopoietic tissues,
such as lymph node, spleen and peripheral leukocytes. Expressed in
macrophages, B-cells, monocytes, platelets, thymocytes, T-cells and
dendritic cells. Highly expressed in memory T-cells. Expressed in mast
cells. {ECO:0000269|PubMed:10698700, ECO:0000269|PubMed:11564780,
ECO:0000269|PubMed:12115647, ECO:0000269|PubMed:12962726,
ECO:0000269|PubMed:15245368, ECO:0000269|PubMed:22068234,
ECO:0000269|PubMed:9310491}.
-!- DEVELOPMENTAL STAGE: Expression is slightly increased in naive B-cells
after the first dividion. By contrast, expression on memory B-cells
decreased with each successive division. {ECO:0000269|PubMed:12115647}.
-!- 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-
containingbinding partners. Especially they mediate the interaction
with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism
is proposed involving threonine (position -2), phosphorylated tyrosine
(position 0) and valine/isoleucine (position +3).
{ECO:0000250|UniProtKB:Q13291, ECO:0000305|PubMed:11313386}.
-!- PTM: Phosphorylated by tyrosine-protein kinase LCK on tyrosine residues
following ligation induced by agonist monoclonal antibody. The
association with SH2D1A is dependent of tyrosine phosphorylation of its
cytoplasmic domain. Phosphorylated on Tyr-296 and Tyr-316 following
platelet aggregation. Phosphorylated on tyrosine residues upon high
affinity immunoglobulin epsilon receptor aggregation in mast cells.
{ECO:0000269|PubMed:11389028, ECO:0000269|PubMed:12115647,
ECO:0000269|PubMed:12928397, ECO:0000269|PubMed:16037392,
ECO:0000269|PubMed:22068234}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10698700,
ECO:0000269|PubMed:9310491}.
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EMBL; U82988; AAB84364.1; -; mRNA.
EMBL; AJ223324; CAA11264.1; -; mRNA.
EMBL; AF054815; AAF21721.1; -; mRNA.
EMBL; AF054816; AAF21722.1; -; mRNA.
EMBL; AF054817; AAF21723.1; -; mRNA.
EMBL; AF054818; AAF21724.1; -; mRNA.
EMBL; AF081189; AAD13155.1; -; Genomic_DNA.
EMBL; AH008972; AAF21784.1; -; Genomic_DNA.
EMBL; AH008376; AAF06840.1; -; Genomic_DNA.
EMBL; U96627; AAD04232.1; -; mRNA.
EMBL; Y12632; CAA73181.1; -; mRNA.
EMBL; AK296290; BAH12304.1; -; mRNA.
EMBL; AK313496; BAG36278.1; -; mRNA.
EMBL; CR541847; CAG46645.1; -; mRNA.
EMBL; CR933666; CAI45963.1; -; mRNA.
EMBL; AL138930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52707.1; -; Genomic_DNA.
EMBL; BC020063; AAH20063.1; -; mRNA.
CCDS; CCDS1206.1; -. [Q9UIB8-3]
CCDS; CCDS53395.1; -. [Q9UIB8-7]
CCDS; CCDS53396.1; -. [Q9UIB8-1]
CCDS; CCDS53397.1; -. [Q9UIB8-5]
CCDS; CCDS81388.1; -. [Q9UIB8-2]
RefSeq; NP_001171808.1; NM_001184879.1. [Q9UIB8-1]
RefSeq; NP_001171810.1; NM_001184881.1. [Q9UIB8-5]
RefSeq; NP_001171811.1; NM_001184882.1. [Q9UIB8-7]
RefSeq; NP_001317671.1; NM_001330742.1. [Q9UIB8-2]
RefSeq; NP_003865.1; NM_003874.3. [Q9UIB8-3]
PDB; 2PKD; X-ray; 2.04 A; A/B/C/D/E/F=22-131.
PDBsum; 2PKD; -.
SMR; Q9UIB8; -.
BioGRID; 114359; 6.
DIP; DIP-60957N; -.
ELM; Q9UIB8; -.
IntAct; Q9UIB8; 4.
MINT; Q9UIB8; -.
STRING; 9606.ENSP00000312367; -.
GlyGen; Q9UIB8; 1 site.
iPTMnet; Q9UIB8; -.
PhosphoSitePlus; Q9UIB8; -.
BioMuta; CD84; -.
DMDM; 74762772; -.
EPD; Q9UIB8; -.
jPOST; Q9UIB8; -.
MassIVE; Q9UIB8; -.
PaxDb; Q9UIB8; -.
PeptideAtlas; Q9UIB8; -.
PRIDE; Q9UIB8; -.
ProteomicsDB; 84484; -. [Q9UIB8-1]
ProteomicsDB; 84485; -. [Q9UIB8-2]
ProteomicsDB; 84486; -. [Q9UIB8-3]
ProteomicsDB; 84487; -. [Q9UIB8-4]
ProteomicsDB; 84488; -. [Q9UIB8-5]
ProteomicsDB; 84489; -. [Q9UIB8-6]
ProteomicsDB; 84490; -. [Q9UIB8-7]
Antibodypedia; 20494; 748 antibodies.
DNASU; 8832; -.
Ensembl; ENST00000311224; ENSP00000312367; ENSG00000066294. [Q9UIB8-1]
Ensembl; ENST00000368048; ENSP00000357027; ENSG00000066294. [Q9UIB8-2]
Ensembl; ENST00000368051; ENSP00000357030; ENSG00000066294. [Q9UIB8-5]
Ensembl; ENST00000368054; ENSP00000357033; ENSG00000066294. [Q9UIB8-3]
Ensembl; ENST00000534968; ENSP00000442845; ENSG00000066294. [Q9UIB8-7]
GeneID; 8832; -.
KEGG; hsa:8832; -.
UCSC; uc001fwf.5; human. [Q9UIB8-1]
CTD; 8832; -.
DisGeNET; 8832; -.
GeneCards; CD84; -.
HGNC; HGNC:1704; CD84.
HPA; ENSG00000066294; Tissue enhanced (lymphoid).
MIM; 604513; gene.
neXtProt; NX_Q9UIB8; -.
OpenTargets; ENSG00000066294; -.
PharmGKB; PA26242; -.
VEuPathDB; HostDB:ENSG00000066294.14; -.
eggNOG; ENOG502SB7W; Eukaryota.
GeneTree; ENSGT00990000203668; -.
HOGENOM; CLU_069386_1_1_1; -.
InParanoid; Q9UIB8; -.
OMA; SGQNYNL; -.
OrthoDB; 990343at2759; -.
PhylomeDB; Q9UIB8; -.
TreeFam; TF334964; -.
PathwayCommons; Q9UIB8; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
BioGRID-ORCS; 8832; 7 hits in 987 CRISPR screens.
EvolutionaryTrace; Q9UIB8; -.
GeneWiki; CD84; -.
GenomeRNAi; 8832; -.
Pharos; Q9UIB8; Tbio.
PRO; PR:Q9UIB8; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q9UIB8; protein.
Bgee; ENSG00000066294; Expressed in visceral pleura and 202 other tissues.
Genevisible; Q9UIB8; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0032685; P:negative regulation of granulocyte macrophage colony-stimulating factor production; IDA:UniProtKB.
GO; GO:0032701; P:negative regulation of interleukin-18 production; IDA:UniProtKB.
GO; GO:0033004; P:negative regulation of mast cell activation; IDA:UniProtKB.
GO; GO:0043305; P:negative regulation of mast cell degranulation; IDA:UniProtKB.
GO; GO:2001256; P:regulation of store-operated calcium entry; 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; IPR003599; Ig_sub.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Autophagy;
Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1..21
/evidence="ECO:0000269|PubMed:10698700"
CHAIN 22..345
/note="SLAM family member 5"
/id="PRO_0000252029"
TOPO_DOM 22..225
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 226..246
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 247..345
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 26..129
/note="Ig-like V-type"
DOMAIN 135..207
/note="Ig-like C2-type"
MOTIF 277..282
/note="ITSM 1"
/evidence="ECO:0000250|UniProtKB:Q13291"
MOTIF 314..319
/note="ITSM 2"
/evidence="ECO:0000250|UniProtKB:Q13291"
MOD_RES 279
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:12458214"
MOD_RES 296
/note="Phosphotyrosine; by LYN"
/evidence="ECO:0000269|PubMed:16037392,
ECO:0000269|PubMed:22068234"
MOD_RES 316
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:16037392,
ECO:0000305|PubMed:12458214"
MOD_RES 341
/note="Phosphotyrosine; by FES"
/evidence="ECO:0000269|PubMed:22068234"
CARBOHYD 150
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 155..193
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 16..130
/note="WPEAAGKDSEIFTVNGILGESVTFPVNIQEPRQVKIIAWTSKTSVAYVTPGD
SETAPVVTVTHRNYYERIHALGPNYNLVISDLRMEDAGDYKADINTQADPYTTTKRYNL
QIYR -> C (in isoform 7)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005"
/id="VSP_020848"
VAR_SEQ 214..241
/note="DIAMGFRTHHTGLLSVLAMFFLLVLILS -> GNQLCPSLLVSLRDHSEELQ
GLNVGHIL (in isoform 6)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020849"
VAR_SEQ 242..345
/note="Missing (in isoform 6)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020850"
VAR_SEQ 254..271
/note="GRIFPEGSCLNTFTKNPY -> D (in isoform 3 and isoform
7)"
/evidence="ECO:0000303|PubMed:10698700,
ECO:0000303|PubMed:10746783, ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:9310491, ECO:0000303|Ref.4"
/id="VSP_020851"
VAR_SEQ 254..259
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020852"
VAR_SEQ 255..272
/note="RIFPEGSCLNTFTKNPYA -> ASLQGRASEHSLFRSAVC (in isoform
5)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020853"
VAR_SEQ 261..280
/note="SCLNTFTKNPYAASKKTIYT -> KMWKLTFSPPGTEAIYPRFS (in
isoform 4)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020854"
VAR_SEQ 273..345
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020855"
VAR_SEQ 281..345
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:10746783"
/id="VSP_020856"
MUTAGEN 55
/note="T->A: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 62
/note="Y->A: No effect."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 62
/note="Y->D: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 77
/note="T->A: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 78
/note="H->A: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 110
/note="D->A: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 112
/note="N->A: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 119
/note="T->A: Loss of dimerization."
/evidence="ECO:0000269|PubMed:17563375"
MUTAGEN 279
/note="Y->F: Reduced tyrosine phosphorylation, reduced
binding of SH2D1B and loss of binding of SH2D1A."
/evidence="ECO:0000269|PubMed:12928397"
MUTAGEN 316
/note="Y->F: Reduced tyrosine phosphorylation and reduced
binding of SH2D1B. Loss of phosphorylation and loss of
binding of SH2D1A and SH2D1B; when associated with F-279."
/evidence="ECO:0000269|PubMed:12928397"
CONFLICT 311
/note="P -> S (in Ref. 4; CAG46645)"
/evidence="ECO:0000305"
STRAND 27..32
/evidence="ECO:0007744|PDB:2PKD"
STRAND 37..39
/evidence="ECO:0007744|PDB:2PKD"
STRAND 49..64
/evidence="ECO:0007744|PDB:2PKD"
STRAND 68..70
/evidence="ECO:0007744|PDB:2PKD"
STRAND 73..76
/evidence="ECO:0007744|PDB:2PKD"
HELIX 79..81
/evidence="ECO:0007744|PDB:2PKD"
STRAND 85..87
/evidence="ECO:0007744|PDB:2PKD"
TURN 89..91
/evidence="ECO:0007744|PDB:2PKD"
STRAND 94..96
/evidence="ECO:0007744|PDB:2PKD"
HELIX 101..103
/evidence="ECO:0007744|PDB:2PKD"
STRAND 105..115
/evidence="ECO:0007744|PDB:2PKD"
STRAND 118..129
/evidence="ECO:0007744|PDB:2PKD"
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


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Related Genes :
[CD84 SLAMF5] SLAM family member 5 (Cell surface antigen MAX.3) (Hly9-beta) (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84)
[Cd84 Slamf5] SLAM family member 5 (Leukocyte differentiation antigen CD84) (Signaling lymphocytic activation molecule 5) (CD antigen CD84)
[LY9 CDABP0070] T-lymphocyte surface antigen Ly-9 (Cell surface molecule Ly-9) (Lymphocyte antigen 9) (SLAM family member 3) (SLAMF3) (Signaling lymphocytic activation molecule 3) (CD antigen CD229)
[Ly9 Ly-9] T-lymphocyte surface antigen Ly-9 (Cell surface molecule Ly-9) (Lymphocyte antigen 9) (SLAM family member 3) (SLAMF3) (Signaling lymphocytic activation molecule 3) (CD antigen CD229)
[Slamf1 Slam] Signaling lymphocytic activation molecule (SLAM family member 1) (CD antigen CD150)
[SLAMF1 SLAM] Signaling lymphocytic activation molecule (CDw150) (IPO-3) (SLAM family member 1) (CD antigen CD150)
[Cd244 2b4 Nmrk] Natural killer cell receptor 2B4 (NK cell type I receptor protein 2B4) (NKR2B4) (Non-MHC restricted killing associated) (SLAM family member 4) (SLAMF4) (Signaling lymphocytic activation molecule 4) (CD antigen CD244)
[Cd48 Bcm-1] CD48 antigen (BCM1 surface antigen) (BLAST-1) (HM48-1) (MRC OX-45 surface antigen) (SLAM family member 2) (SLAMF2) (Signaling lymphocytic activation molecule 2) (sgp-60) (CD antigen CD48)
[SH2D1A DSHP SAP] SH2 domain-containing protein 1A (Duncan disease SH2-protein) (Signaling lymphocytic activation molecule-associated protein) (SLAM-associated protein) (T-cell signal transduction molecule SAP)
[CD69 CLEC2C] Early activation antigen CD69 (Activation inducer molecule) (AIM) (BL-AC/P26) (C-type lectin domain family 2 member C) (EA1) (Early T-cell activation antigen p60) (GP32/28) (Leukocyte surface antigen Leu-23) (MLR-3) (CD antigen CD69)
[CD244 2B4] Natural killer cell receptor 2B4 (NK cell activation-inducing ligand) (NAIL) (NK cell type I receptor protein 2B4) (NKR2B4) (h2B4) (SLAM family member 4) (SLAMF4) (Signaling lymphocytic activation molecule 4) (CD antigen CD244)
[SLAMF6 KALI UNQ6123/PRO20080] SLAM family member 6 (Activating NK receptor) (NK-T-B-antigen) (NTB-A) (CD antigen CD352)
[Slamf6 Ly108] SLAM family member 6 (Lymphocyte antigen 108) (CD antigen CD352)
[Slamf7] SLAM family member 7 (Leukocyte cell-surface antigen) (Novel Ly9) (CD antigen CD319)
[BSG UNQ6505/PRO21383] Basigin (5F7) (Collagenase stimulatory factor) (Extracellular matrix metalloproteinase inducer) (EMMPRIN) (Hepatoma-associated antigen) (HAb18G) (Leukocyte activation antigen M6) (OK blood group antigen) (Tumor cell-derived collagenase stimulatory factor) (TCSF) (CD antigen CD147)
[SLC3A2 MDU1] 4F2 cell-surface antigen heavy chain (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98)
[SELP GMRP GRMP] P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P)
[SLAMF1 SLAM] Signaling lymphocytic activation molecule (CD antigen CD150)
[Selp Grmp] P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P)
[CD40LG CD40L TNFSF5 TRAP] CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
[SELL LNHR LYAM1] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte surface antigen Leu-8) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (TQ1) (gp90-MEL) (CD antigen CD62L)
[ITGAL CD11A] Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD antigen CD11a)
[SELP] P-selectin (CD62 antigen-like family member P) (CD62P antigen) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62)
[Selp] P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P)
[Sirpa Bit Myd1 Ptpns1 Shps1 Sirp] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (mSIRP-alpha1) (p84) (CD antigen CD172a)
[SIRPA BIT MFR MYD1 PTPNS1 SHPS1 SIRP] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory protein alpha-2) (Sirp-alpha-2) (Signal-regulatory protein alpha-3) (Sirp-alpha-3) (p84) (CD antigen CD172a)
[CD19] B-lymphocyte antigen CD19 (B-lymphocyte surface antigen B4) (Differentiation antigen CD19) (T-cell surface antigen Leu-12) (CD antigen CD19)
[LILRB1 ILT2 LIR1 MIR7] Leukocyte immunoglobulin-like receptor subfamily B member 1 (LIR-1) (Leukocyte immunoglobulin-like receptor 1) (CD85 antigen-like family member J) (Immunoglobulin-like transcript 2) (ILT-2) (Monocyte/macrophage immunoglobulin-like receptor 7) (MIR-7) (CD antigen CD85j)
[CD40 TNFRSF5] Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (Bp50) (CD40L receptor) (CDw40) (CD antigen CD40)
[SELE ELAM1] E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E)

Bibliography :