SLAF6_HUMAN
ID SLAF6_HUMAN Reviewed; 332 AA.
AC Q96DU3; A6NMW2; B2R8X8; Q14CF0; Q5TAS4; Q5TAS6; Q5TAT3; Q96DV0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=SLAM family member 6;
DE AltName: Full=Activating NK receptor;
DE AltName: Full=NK-T-B-antigen;
DE Short=NTB-A;
DE AltName: CD_antigen=CD352;
DE Flags: Precursor;
GN Name=SLAMF6; Synonyms=KALI; ORFNames=UNQ6123/PRO20080;
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] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH SH2D1A; PTN6 AND PTN11.
RC TISSUE=Lymphoid tissue;
RX PubMed=11489943; DOI=10.1084/jem.194.3.235;
RA Bottino C., Falco M., Parolini S., Marcenaro E., Augugliaro R., Sivori S.,
RA Landi E., Biassoni R., Notarangelo L.D., Moretta L., Moretta A.;
RT "NTB-A, a novel SH2D1A-associated surface molecule contributing to the
RT inability of natural killer cells to kill Epstein-Barr virus-infected B
RT cells in X-linked Lymphoproliferative disease.";
RL J. Exp. Med. 194:235-246(2001).
RN [2]
RP ERRATUM OF PUBMED:11489943.
RA Bottino C., Falco M., Parolini S., Marcenaro E., Augugliaro R., Sivori S.,
RA Landi E., Biassoni R., Notarangelo L.D., Moretta L., Moretta A.;
RL J. Exp. Med. 194:705-705(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [9]
RP PROTEIN SEQUENCE OF 22-36.
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 [10]
RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH SH2D1A AND SH2D1B, AND
RP MUTAGENESIS OF TYR-274; TYR-285 AND TYR-309.
RX PubMed=16920955; DOI=10.4049/jimmunol.177.5.3170;
RA Eissmann P., Watzl C.;
RT "Molecular analysis of NTB-A signaling: a role for EAT-2 in NTB-A-mediated
RT activation of human NK cells.";
RL J. Immunol. 177:3170-3177(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-178.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-274; SER-278 AND TYR-309, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP FUNCTION.
RX PubMed=22989874; DOI=10.1074/jbc.m112.415067;
RA Chatterjee M., Hedrich C.M., Rauen T., Ioannidis C., Terhorst C.,
RA Tsokos G.C.;
RT "CD3-T cell receptor co-stimulation through SLAMF3 and SLAMF6 receptors
RT enhances RORgammat recruitment to the IL17A promoter in human T
RT lymphocytes.";
RL J. Biol. Chem. 287:38168-38177(2012).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22184727; DOI=10.4049/jimmunol.1102773;
RA Chatterjee M., Rauen T., Kis-Toth K., Kyttaris V.C., Hedrich C.M.,
RA Terhorst C., Tsokos G.C.;
RT "Increased expression of SLAM receptors SLAMF3 and SLAMF6 in systemic lupus
RT erythematosus T lymphocytes promotes Th17 differentiation.";
RL J. Immunol. 188:1206-1212(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 24-215, SUBUNIT, DISULFIDE BONDS,
RP AND MUTAGENESIS OF ARG-108; GLN-110 AND SER-112.
RX PubMed=17045824; DOI=10.1016/j.immuni.2006.06.020;
RA Cao E., Ramagopal U.A., Fedorov A., Fedorov E., Yan Q., Lary J.W.,
RA Cole J.L., Nathenson S.G., Almo S.C.;
RT "NTB-A receptor crystal structure: insights into homophilic interactions in
RT the signaling lymphocytic activation molecule receptor family.";
RL Immunity 25:559-570(2006).
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 Triggers cytolytic activity only in natural killer cells (NK)
CC expressing high surface densities of natural cytotoxicity receptors
CC (PubMed:11489943, PubMed:16920955). Positive signaling in NK cells
CC implicates phosphorylation of VAV1. NK cell activation seems to depend
CC on SH2D1B and not on SH2D1A (PubMed:16920955). In conjunction with
CC SLAMF1 controls the transition between positive selection and the
CC subsequent expansion and differentiation of the thymocytic natural
CC killer T (NKT) cell lineage (By similarity). Promotes T-cell
CC differentiation into a helper T-cell Th17 phenotype leading to
CC increased IL-17 secretion; the costimulatory activity requires SH2D1A
CC (PubMed:22184727, PubMed:16920955). Promotes recruitment of RORC to the
CC IL-17 promoter (PubMed:22989874). In conjunction with SLAMF1 and
CC CD84/SLAMF5 may be a negative regulator of the humoral immune response.
CC In the absence of SH2D1A/SAP can transmit negative signals to CD4(+) T-
CC cells and NKT cells. Negatively regulates germinal center formation by
CC inhibiting T-cell:B-cell adhesion; the function probably implicates
CC increased association with PTPN6/SHP-1 via ITSMs in absence of
CC SH2D1A/SAP. However, reported to be involved in maintaining B-cell
CC tolerance in germinal centers and in preventing autoimmunity (By
CC similarity). {ECO:0000250|UniProtKB:Q9ET39,
CC ECO:0000269|PubMed:11489943, ECO:0000269|PubMed:16920955,
CC ECO:0000269|PubMed:22184727, ECO:0000269|PubMed:22989874}.
CC -!- SUBUNIT: Homodimer. Interacts with PTN6. Interacts (phosphorylated)
CC with PTN11. Interacts (phosphorylated on tyrosine residues) with
CC SH2D1A/SAP and SH2D1B/EAT2; SH2D1A and SH2D1B can associate with the
CC same SLAMF6 molecule; interaction with SH2D1B is mediated by ITSM 2.
CC {ECO:0000269|PubMed:11489943, ECO:0000269|PubMed:16920955,
CC ECO:0000269|PubMed:17045824}.
CC -!- INTERACTION:
CC Q96DU3; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-14058448, EBI-12244618;
CC Q96DU3; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-14058448, EBI-12256978;
CC Q96DU3; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-14058448, EBI-10266796;
CC Q96DU3; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-14058448, EBI-712367;
CC Q96DU3; O60880: SH2D1A; NbExp=12; IntAct=EBI-14058448, EBI-6983382;
CC Q96DU3; O14796: SH2D1B; NbExp=4; IntAct=EBI-14058448, EBI-3923013;
CC Q96DU3; P55061: TMBIM6; NbExp=3; IntAct=EBI-14058448, EBI-1045825;
CC Q96DU3; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-14058448, EBI-11724433;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96DU3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DU3-2; Sequence=VSP_034620;
CC Name=3;
CC IsoId=Q96DU3-3; Sequence=VSP_043230;
CC -!- TISSUE SPECIFICITY: Expressed by all (resting and activated) natural
CC killer cells (NK), T- and B-lymphocytes (PubMed:11489943). Increased
CC surface expression on T-cells of systemic lupus erythematosus (SLE)
CC patients (PubMed:22184727). {ECO:0000269|PubMed:11489943,
CC ECO:0000269|PubMed:22184727}.
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 with the SH2
CC domain of SH2D1A and SH2D1B. A 'two-out-of-three-pronged' mechanism is
CC proposed involving threonine (position -2), phosphorylated tyrosine
CC (position 0) and valine/isoleucine (position +3).
CC {ECO:0000250|UniProtKB:Q13291}.
CC -!- PTM: Phosphorylation in NK cells upon engagment by SLAMF6-expressing
CC target cells is leading to receptor activation.
CC {ECO:0000269|PubMed:16920955}.
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DR EMBL; AJ277141; CAC59749.1; -; mRNA.
DR EMBL; AJ306388; CAC59750.1; -; mRNA.
DR EMBL; AY358159; AAQ88526.1; -; mRNA.
DR EMBL; AL832854; CAI46161.1; -; mRNA.
DR EMBL; AK125624; BAG54223.1; -; mRNA.
DR EMBL; AK301026; BAG62642.1; -; mRNA.
DR EMBL; AK313549; BAG36325.1; -; mRNA.
DR EMBL; AL138930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52713.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52715.1; -; Genomic_DNA.
DR EMBL; BC113893; AAI13894.1; -; mRNA.
DR EMBL; BC114495; AAI14496.1; -; mRNA.
DR CCDS; CCDS1205.1; -. [Q96DU3-2]
DR CCDS; CCDS53393.1; -. [Q96DU3-3]
DR CCDS; CCDS53394.1; -. [Q96DU3-1]
DR RefSeq; NP_001171643.1; NM_001184714.1. [Q96DU3-1]
DR RefSeq; NP_001171644.1; NM_001184715.1.
DR RefSeq; NP_001171645.1; NM_001184716.1. [Q96DU3-3]
DR RefSeq; NP_443163.1; NM_052931.4. [Q96DU3-2]
DR PDB; 2IF7; X-ray; 3.00 A; A/B/C/D=24-215.
DR PDBsum; 2IF7; -.
DR AlphaFoldDB; Q96DU3; -.
DR SMR; Q96DU3; -.
DR BioGRID; 125378; 15.
DR IntAct; Q96DU3; 13.
DR STRING; 9606.ENSP00000357036; -.
DR GlyGen; Q96DU3; 8 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96DU3; -.
DR PhosphoSitePlus; Q96DU3; -.
DR BioMuta; SLAMF6; -.
DR DMDM; 205830927; -.
DR jPOST; Q96DU3; -.
DR MassIVE; Q96DU3; -.
DR MaxQB; Q96DU3; -.
DR PaxDb; Q96DU3; -.
DR PeptideAtlas; Q96DU3; -.
DR PRIDE; Q96DU3; -.
DR ProteomicsDB; 76325; -. [Q96DU3-1]
DR ProteomicsDB; 76326; -. [Q96DU3-2]
DR ProteomicsDB; 76327; -. [Q96DU3-3]
DR Antibodypedia; 34279; 470 antibodies from 33 providers.
DR DNASU; 114836; -.
DR Ensembl; ENST00000368055.1; ENSP00000357034.1; ENSG00000162739.14. [Q96DU3-3]
DR Ensembl; ENST00000368057.8; ENSP00000357036.3; ENSG00000162739.14. [Q96DU3-1]
DR Ensembl; ENST00000368059.7; ENSP00000357038.3; ENSG00000162739.14. [Q96DU3-2]
DR GeneID; 114836; -.
DR KEGG; hsa:114836; -.
DR MANE-Select; ENST00000368057.8; ENSP00000357036.3; NM_001184714.2; NP_001171643.1.
DR UCSC; uc001fwd.2; human. [Q96DU3-1]
DR CTD; 114836; -.
DR DisGeNET; 114836; -.
DR GeneCards; SLAMF6; -.
DR HGNC; HGNC:21392; SLAMF6.
DR HPA; ENSG00000162739; Tissue enriched (lymphoid).
DR MIM; 606446; gene.
DR neXtProt; NX_Q96DU3; -.
DR OpenTargets; ENSG00000162739; -.
DR PharmGKB; PA134959277; -.
DR VEuPathDB; HostDB:ENSG00000162739; -.
DR eggNOG; ENOG502SSRG; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_069386_2_0_1; -.
DR InParanoid; Q96DU3; -.
DR OMA; YLDIRWI; -.
DR OrthoDB; 990343at2759; -.
DR PhylomeDB; Q96DU3; -.
DR TreeFam; TF334964; -.
DR PathwayCommons; Q96DU3; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q96DU3; -.
DR BioGRID-ORCS; 114836; 13 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; Q96DU3; -.
DR GeneWiki; SLAMF6; -.
DR GenomeRNAi; 114836; -.
DR Pharos; Q96DU3; Tbio.
DR PRO; PR:Q96DU3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96DU3; protein.
DR Bgee; ENSG00000162739; Expressed in granulocyte and 95 other tissues.
DR Genevisible; Q96DU3; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; IDA:UniProtKB.
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 InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Innate immunity; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 22..332
FT /note="SLAM family member 6"
FT /id="PRO_0000014961"
FT TOPO_DOM 22..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..120
FT /note="Ig-like V-type"
FT DOMAIN 132..209
FT /note="Ig-like C2-type"
FT MOTIF 283..288
FT /note="ITSM 1"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOTIF 307..312
FT /note="ITSM 2"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOD_RES 274
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17045824"
FT DISULFID 153..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17045824"
FT VAR_SEQ 18..128
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043230"
FT VAR_SEQ 266
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11489943,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_034620"
FT MUTAGEN 108
FT /note="R->A: Inhibits dimerization."
FT /evidence="ECO:0000269|PubMed:17045824"
FT MUTAGEN 110
FT /note="Q->A: Inhibits dimerization."
FT /evidence="ECO:0000269|PubMed:17045824"
FT MUTAGEN 112
FT /note="S->A: Inhibits dimerization."
FT /evidence="ECO:0000269|PubMed:17045824"
FT MUTAGEN 274
FT /note="Y->F: Retains reduced SLAMF6-mediated cytotoxity,
FT disrupts interaction with SH2D1A and retains interaction
FT with SH2D1B; when associated with F-309."
FT /evidence="ECO:0000269|PubMed:16920955"
FT MUTAGEN 285
FT /note="Y->F: Abolishes SLAMF6-mediated cytotoxity, disrupts
FT interaction with SH2D1B and retains interaction with
FT SH2D1A."
FT /evidence="ECO:0000269|PubMed:16920955"
FT MUTAGEN 309
FT /note="Y->F: Reduced SLAMF6-mediated cytotoxity."
FT /evidence="ECO:0000269|PubMed:16920955"
FT MUTAGEN 309
FT /note="Y->F: Retains reduced SLAMF6-mediated cytotoxity,
FT disrupts interaction with SH2D1A and retains interaction
FT with SH2D1B; when associated with F-273."
FT /evidence="ECO:0000269|PubMed:16920955"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2IF7"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2IF7"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:2IF7"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:2IF7"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:2IF7"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2IF7"
SQ SEQUENCE 332 AA; 37345 MW; 46D8141A0D198091 CRC64;
MLWLFQSLLF VFCFGPGNVV SQSSLTPLMV NGILGESVTL PLEFPAGEKV NFITWLFNET
SLAFIVPHET KSPEIHVTNP KQGKRLNFTQ SYSLQLSNLK MEDTGSYRAQ ISTKTSAKLS
SYTLRILRQL RNIQVTNHSQ LFQNMTCELH LTCSVEDADD NVSFRWEALG NTLSSQPNLT
VSWDPRISSE QDYTCIAENA VSNLSFSVSA QKLCEDVKIQ YTDTKMILFM VSGICIVFGF
IILLLLVLRK RRDSLSLSTQ RTQGPAESAR NLEYVSVSPT NNTVYASVTH SNRETEIWTP
RENDTITIYS TINHSKESKP TFSRATALDN VV
