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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)

 CD244_HUMAN             Reviewed;         370 AA.
Q9BZW8; Q5VYI2; Q5VYI6; Q5VYI7; Q96T47; Q9NQD2; Q9NQD3; Q9Y288;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-MAY-2004, sequence version 2.
11-DEC-2019, entry version 166.
RecName: Full=Natural killer cell receptor 2B4;
AltName: Full=NK cell activation-inducing ligand;
Short=NAIL;
AltName: Full=NK cell type I receptor protein 2B4;
Short=NKR2B4;
Short=h2B4;
AltName: Full=SLAM family member 4;
Short=SLAMF4;
AltName: Full=Signaling lymphocytic activation molecule 4;
AltName: CD_antigen=CD244;
Flags: Precursor;
Name=CD244; Synonyms=2B4;
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 2), FUNCTION, AND INTERACTION WITH
CD48.
PubMed=10359122;
DOI=10.1002/(sici)1521-4141(199905)29:05<1676::aid-immu1676>3.0.co;2-y;
Nakajima H., Cella M., Langen H., Friedlein A., Colonna M.;
"Activating interactions in human NK cell recognition: the role of 2B4-
CD48.";
Eur. J. Immunol. 29:1676-1683(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS,
TISSUE SPECIFICITY, AND INTERACTION WITH CD48.
PubMed=10556801;
DOI=10.1002/(sici)1521-4141(199911)29:11<3466::aid-immu3466>3.0.co;2-9;
Kubin M.Z., Parshley D.L., Din W., Waugh J.Y., Davis-Smith T., Smith C.A.,
Macduff B.M., Armitage R.J., Chin W., Cassiano L., Borges L., Petersen M.,
Trinchieri G., Goodwin R.G.;
"Molecular cloning and biological characterization of NK cell activation-
inducing ligand, a counterstructure for CD48.";
Eur. J. Immunol. 29:3466-3477(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION, AND INTERACTION
WITH SH2D1A AND PTPN11.
PubMed=10358138;
Tangye S.G., Lazetic S., Woollatt E., Sutherland G.R., Lanier L.L.,
Phillips J.H.;
"Human 2B4, an activating NK cell receptor, recruits the protein tyrosine
phosphatase SHP-2 and the adaptor signaling protein SAP.";
J. Immunol. 162:6981-6985(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH CD48.
TISSUE=Natural killer cell;
PubMed=10458320; DOI=10.1034/j.1399-0039.1999.540103.x;
Boles K.S., Nakajima H., Colonna M., Chuang S.S., Stepp S.E., Bennett M.,
Kumar V., Mathew P.A.;
"Molecular characterization of a novel human natural killer cell receptor
homologous to mouse 2B4.";
Tissue Antigens 54:27-34(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11003394; DOI=10.1007/s002510000237;
Kumaresan P.R., Mathew P.A.;
"Structure of the human natural killer cell receptor 2B4 gene and
identification of a novel alternative transcript.";
Immunogenetics 51:987-992(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, AND INTERACTION
WITH INPP5D.
TISSUE=Lymphoid tissue;
PubMed=10934222; DOI=10.1084/jem.192.3.337;
Parolini S., Bottino C., Falco M., Augugliaro R., Giliani S.,
Franceschini R., Ochs H.D., Wolf H., Bonnefoy J.-Y., Biassoni R.,
Moretta L., Notarangelo L.D., Moretta A.;
"X-linked lymphoproliferative disease: 2B4 molecules displaying inhibitory
rather than activating function are responsible for the inability of
natural killer cells to kill Epstein-Barr virus-infected cells.";
J. Exp. Med. 192:337-346(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Lymphoid tissue;
Biassoni R., Falco M.;
"Activating NK receptor homolog to the murine 2B4.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[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 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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Blood;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-133.
Lennon G.P., Eccleston D.W., Pridgeon C., Pazmany L., Moots R.J.;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[12]
PROTEIN SEQUENCE OF 22-36.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified
cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8376943; DOI=10.1084/jem.178.4.1397;
Valiante N.M., Trinchieri G.;
"Identification of a novel signal transduction surface molecule on human
cytotoxic lymphocytes.";
J. Exp. Med. 178:1397-1406(1993).
[14]
INTERACTION WITH CD48.
PubMed=9841922; DOI=10.1084/jem.188.11.2083;
Brown M.H., Boles K., van der Merwe P.A., Kumar V., Mathew P.A.,
Barclay A.N.;
"2B4, the natural killer and T cell immunoglobulin superfamily surface
protein, is a ligand for CD48.";
J. Exp. Med. 188:2083-2090(1998).
[15]
FUNCTION.
PubMed=10741393;
DOI=10.1002/1521-4141(200003)30:3<787::aid-immu787>3.0.co;2-i;
Sivori S., Parolini S., Falco M., Marcenaro E., Biassoni R., Bottino C.,
Moretta L., Moretta A.;
"2B4 functions as a co-receptor in human NK cell activation.";
Eur. J. Immunol. 30:787-793(2000).
[16]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=11034353; DOI=10.4049/jimmunol.165.7.3545;
Watzl C., Stebbins C.C., Long E.O.;
"NK cell inhibitory receptors prevent tyrosine phosphorylation of the
activation receptor 2B4 (CD244).";
J. Immunol. 165:3545-3548(2000).
[17]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11714776; DOI=10.4049/jimmunol.167.11.6165;
Speiser D.E., Colonna M., Ayyoub M., Cella M., Pittet M.J., Batard P.,
Valmori D., Guillaume P., Lienard D., Cerottini J.C., Romero P.;
"The activatory receptor 2B4 is expressed in vivo by human CD8+ effector
alpha beta T cells.";
J. Immunol. 167:6165-6170(2001).
[18]
INTERACTION WITH PIK3R1.
PubMed=11815622; DOI=10.1074/jbc.m112029200;
Aoukaty A., Tan R.;
"Association of the X-linked lymphoproliferative disease gene product
SAP/SH2D1A with 2B4, a natural killer cell-activating molecule, is
dependent on phosphoinositide 3-kinase.";
J. Biol. Chem. 277:13331-13337(2002).
[19]
FUNCTION.
PubMed=11917118; DOI=10.1073/pnas.072065999;
Sivori S., Falco M., Marcenaro E., Parolini S., Biassoni R., Bottino C.,
Moretta L., Moretta A.;
"Early expression of triggering receptors and regulatory role of 2B4 in
human natural killer cell precursors undergoing in vitro differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 99:4526-4531(2002).
[20]
INTERACTION WITH SH2D1A; SH2D1B; INPP5D AND PTPN11, AND PHOSPHORYLATION AT
TYR-271; TYR-297; TYR-317 AND TYR-342.
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).
[21]
FUNCTION, DOMAIN ITSM MOTIF, INTERACTION WITH INPP5D; PTPN11; PTPN6; CSK;
FYN AND SH2D1A, AND PHOSPHORYLATION AT TYR-271; TYR-297; TYR-317 AND
TYR-342.
PubMed=15713798; DOI=10.1182/blood-2004-09-3796;
Eissmann P., Beauchamp L., Wooters J., Tilton J.C., Long E.O., Watzl C.;
"Molecular basis for positive and negative signaling by the natural killer
cell receptor 2B4 (CD244).";
Blood 105:4722-4729(2005).
[22]
MUTAGENESIS OF LYS-68 AND GLU-70.
PubMed=16002700; DOI=10.4049/jimmunol.175.2.1005;
Mathew S.O., Kumaresan P.R., Lee J.K., Huynh V.T., Mathew P.A.;
"Mutational analysis of the human 2B4 (CD244)/CD48 interaction: Lys68 and
Glu70 in the V domain of 2B4 are critical for CD48 binding and functional
activation of NK cells.";
J. Immunol. 175:1005-1013(2005).
[23]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
PubMed=19499526; DOI=10.1002/eji.200838733;
Mathew S.O., Rao K.K., Kim J.R., Bambard N.D., Mathew P.A.;
"Functional role of human NK cell receptor 2B4 (CD244) isoforms.";
Eur. J. Immunol. 39:1632-1641(2009).
[24]
INTERACTION WITH MHC CLASS I PROTEINS.
PubMed=20164429; DOI=10.4049/jimmunol.0901572;
Betser-Cohen G., Mizrahi S., Elboim M., Alsheich-Bartok O., Mandelboim O.;
"The association of MHC class I proteins with the 2B4 receptor inhibits
self-killing of human NK cells.";
J. Immunol. 184:2761-2768(2010).
[25]
GLYCOSYLATION AT ASN-71; ASN-77 AND ASN-89.
PubMed=21606496; DOI=10.1074/jbc.m111.225334;
Margraf-Schonfeld S., Bohm C., Watzl C.;
"Glycosylation affects ligand binding and function of the activating
natural killer cell receptor 2B4 (CD244) protein.";
J. Biol. Chem. 286:24142-24149(2011).
[26]
INTERACTION WITH SH2D1A; SH2D1B AND INPP5D, AND DOMAIN ITSM MOTIF.
PubMed=24642916; DOI=10.1371/journal.pone.0092184;
Wilson T.J., Garner L.I., Metcalfe C., King E., Margraf S., Brown M.H.;
"Fine specificity and molecular competition in SLAM family receptor
signalling.";
PLoS ONE 9:E92184-E92184(2014).
[27]
INTERACTION WITH SH2D1A AND INPP5D, DOMAIN ITSM MOTIF, AND PHOSPHORYLATION
AT TYR-271 AND TYR-297.
PubMed=26221972; DOI=10.1111/imm.12513;
Margraf S., Garner L.I., Wilson T.J., Brown M.H.;
"A polymorphism in a phosphotyrosine signalling motif of CD229 (Ly9,
SLAMF3) alters SH2 domain binding and T-cell activation.";
Immunology 146:392-400(2015).
-!- FUNCTION: Heterophilic receptor of the signaling lymphocytic activation
molecule (SLAM) family; its ligand is CD48. 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. Acts as activating natural killer (NK) cell receptor
(PubMed:10359122, PubMed:8376943, PubMed:11714776). Activating function
implicates association with SH2D1A and FYN (PubMed:15713798).
Downstreaming signaling involves predominantly VAV1, and, to a lesser
degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of
SH2D1A is proposed to be dependent on INPP5D and to a lesser extent
PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10934222, PubMed:15713798).
Stimulates NK cell cytotoxicity, production of IFN-gamma and granule
exocytosis (PubMed:8376943, PubMed:11714776). Optimal expansion and
activation of NK cells seems to be dependent on the engagement of CD244
with CD48 expressed on neighboring NK cells (By similarity). Acts as
costimulator in NK activation by enhancing signals by other NK
receptors such as NCR3 and NCR1 (PubMed:10741393). At early stages of
NK cell differentiation may function as an inhibitory receptor possibly
ensuring the self-tolerance of developing NK cells (PubMed:11917118).
Involved in the regulation of CD8(+) T-cell proliferation; expression
on activated T-cells and binding to CD488 provides costimulatory-like
function for neighboring T-cells (By similarity). Inhibits inflammatory
responses in dendritic cells (DCs) (By similarity).
{ECO:0000250|UniProtKB:Q07763, ECO:0000269|PubMed:10359122,
ECO:0000269|PubMed:10741393, ECO:0000269|PubMed:10934222,
ECO:0000269|PubMed:11714776, ECO:0000269|PubMed:11917118,
ECO:0000269|PubMed:8376943, ECO:0000305|PubMed:15713798}.
-!- SUBUNIT: Interacts with CD48 (PubMed:9841922). Interacts (via
phosphorylated ITSM 1-4) with SH2D1A (via SH2 domain); SH2D1A probably
mediates association with FYN. Interacts (via phosphorylated ITSM 3)
with PTPN11/SHP-2, INPP5D/SHIP1, PTPN6/SHP-1 and CSK; binding of
SH2D1A/SAP prevents association with PTPN11, PTPN6 and CSK;
conflictingly a similar association has been described for
phosphorylated ITSM 1 also including GRB2 and PLCG1. Interacts weakly
(via phosphorylated ITSM 2) with PTPN11/SHP-2 and CSK (PubMed:10358138,
PubMed:10934222, PubMed:12458214, PubMed:24642916, PubMed:26221972,
PubMed:15713798). Interacts with SH2D1B (PubMed:12458214,
PubMed:24642916). Interacts with PIK3R1; PI3K recruits SH2D1A
(PubMed:11815622). Interacts with MHC class I proteins; the interaction
is proposed to prevent self-killing of NK cells.
{ECO:0000250|UniProtKB:Q07763, ECO:0000269|PubMed:10358138,
ECO:0000269|PubMed:10359122, ECO:0000269|PubMed:10458320,
ECO:0000269|PubMed:10556801, ECO:0000269|PubMed:10934222,
ECO:0000269|PubMed:11815622, ECO:0000269|PubMed:12458214,
ECO:0000269|PubMed:15713798, ECO:0000269|PubMed:20164429,
ECO:0000269|PubMed:24642916, ECO:0000269|PubMed:26221972,
ECO:0000269|PubMed:9841922}.
-!- INTERACTION:
P61769:B2M; NbExp=2; IntAct=EBI-1580565, EBI-714718;
P09326:CD48; NbExp=4; IntAct=EBI-1580565, EBI-714770;
Q92835:INPP5D; NbExp=6; IntAct=EBI-1580565, EBI-1380477;
P19174:PLCG1; NbExp=2; IntAct=EBI-1580565, EBI-79387;
Q06124:PTPN11; NbExp=5; IntAct=EBI-1580565, EBI-297779;
P29350:PTPN6; NbExp=2; IntAct=EBI-1580565, EBI-78260;
O60880:SH2D1A; NbExp=10; IntAct=EBI-1580565, EBI-6983382;
O60880-1:SH2D1A; NbExp=2; IntAct=EBI-1580565, EBI-15552052;
O14796:SH2D1B; NbExp=7; IntAct=EBI-1580565, EBI-3923013;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}.
Note=Receptor engagement results in a recruitment to lipid drafts
essential for the subsequent tyrosine phosphorylation of the ITSMs.
{ECO:0000269|PubMed:11034353}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=H2B4-B;
IsoId=Q9BZW8-1; Sequence=Displayed;
Name=2; Synonyms=H2B4-A;
IsoId=Q9BZW8-2; Sequence=VSP_010397;
Name=3; Synonyms=H2B4;
IsoId=Q9BZW8-3; Sequence=VSP_010397, VSP_010399, VSP_010400;
Name=4; Synonyms=H2B4b;
IsoId=Q9BZW8-4; Sequence=VSP_010398;
-!- TISSUE SPECIFICITY: Expressed in spleen, PBL, followed by lung, liver,
testis and small intestine. Expressed in all natural killer (NK) cells,
monocytes and basophils, TCR-gamma/delta+ T-cells, monocytes,
basophils, and on a subset of CD8(+) T-cells.
{ECO:0000269|PubMed:10556801, ECO:0000269|PubMed:11714776,
ECO:0000269|PubMed:8376943}.
-!- 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-
containing binding 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:0000269|PubMed:15713798,
ECO:0000269|PubMed:26221972}.
-!- PTM: N-linked glycosylation is essential for the binding to its ligand
CD48. Also O-glycosylated, in contrast, O-linked sialylation has a
negative impact on ligand binding. {ECO:0000269|PubMed:21606496}.
-!- PTM: Phosphorylated by FYN and CSK on tyrosine residues following
activation. Coligation with inhibitory receptors such as KIR2DL1
inhibits phosphorylation upon contact of NK cells with sensitive target
cells. {ECO:0000269|PubMed:10358138, ECO:0000269|PubMed:11034353}.
-!- MISCELLANEOUS: [Isoform 2]: Binds to CD48 with a sronger affinity than
isoform 1, and interactions induces greater cytotoxicity and
intracellular calcium release. {ECO:0000305}.
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EMBL; AF105261; AAD32538.1; -; mRNA.
EMBL; AF117711; AAF28833.1; -; mRNA.
EMBL; AF145782; AAD38951.1; -; mRNA.
EMBL; AF107761; AAD37838.1; -; mRNA.
EMBL; AF242540; AAK00233.1; -; mRNA.
EMBL; AJ245376; CAC00648.1; -; mRNA.
EMBL; AJ245377; CAC00649.1; -; mRNA.
EMBL; AJ245375; CAC00647.1; -; mRNA.
EMBL; AL354714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52691.1; -; Genomic_DNA.
EMBL; CH471121; EAW52692.1; -; Genomic_DNA.
EMBL; CH471121; EAW52693.1; -; Genomic_DNA.
EMBL; BC028073; AAH28073.1; -; mRNA.
EMBL; BC053985; AAH53985.1; -; mRNA.
EMBL; AF363452; AAK50015.1; -; mRNA.
CCDS; CCDS1210.1; -. [Q9BZW8-2]
CCDS; CCDS53398.1; -. [Q9BZW8-4]
CCDS; CCDS53399.1; -. [Q9BZW8-1]
RefSeq; NP_001160135.1; NM_001166663.1. [Q9BZW8-1]
RefSeq; NP_001160136.1; NM_001166664.1. [Q9BZW8-4]
RefSeq; NP_057466.1; NM_016382.3. [Q9BZW8-2]
RefSeq; XP_011507924.1; XM_011509622.2. [Q9BZW8-3]
SMR; Q9BZW8; -.
BioGrid; 119709; 25.
DIP; DIP-40331N; -.
ELM; Q9BZW8; -.
IntAct; Q9BZW8; 33.
MINT; Q9BZW8; -.
STRING; 9606.ENSP00000357012; -.
iPTMnet; Q9BZW8; -.
PhosphoSitePlus; Q9BZW8; -.
BioMuta; CD244; -.
DMDM; 47605541; -.
MassIVE; Q9BZW8; -.
PaxDb; Q9BZW8; -.
PeptideAtlas; Q9BZW8; -.
PRIDE; Q9BZW8; -.
ProteomicsDB; 79913; -. [Q9BZW8-1]
ProteomicsDB; 79914; -. [Q9BZW8-2]
ProteomicsDB; 79915; -. [Q9BZW8-3]
ProteomicsDB; 79916; -. [Q9BZW8-4]
DNASU; 51744; -.
Ensembl; ENST00000322302; ENSP00000313619; ENSG00000122223. [Q9BZW8-4]
Ensembl; ENST00000368033; ENSP00000357012; ENSG00000122223. [Q9BZW8-1]
Ensembl; ENST00000368034; ENSP00000357013; ENSG00000122223. [Q9BZW8-2]
Ensembl; ENST00000492063; ENSP00000432636; ENSG00000122223. [Q9BZW8-3]
GeneID; 51744; -.
KEGG; hsa:51744; -.
UCSC; uc001fxa.4; human. [Q9BZW8-1]
CTD; 51744; -.
DisGeNET; 51744; -.
EuPathDB; HostDB:ENSG00000122223.12; -.
GeneCards; CD244; -.
HGNC; HGNC:18171; CD244.
MalaCards; CD244; -.
MIM; 605554; gene.
neXtProt; NX_Q9BZW8; -.
OpenTargets; ENSG00000122223; -.
PharmGKB; PA134905192; -.
eggNOG; ENOG410IKYZ; Eukaryota.
eggNOG; ENOG410Y74Q; LUCA.
GeneTree; ENSGT00950000182746; -.
InParanoid; Q9BZW8; -.
KO; K06582; -.
OMA; CQVTLSC; -.
OrthoDB; 1532935at2759; -.
PhylomeDB; Q9BZW8; -.
TreeFam; TF334964; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
SignaLink; Q9BZW8; -.
GeneWiki; CD244; -.
GenomeRNAi; 51744; -.
Pharos; Q9BZW8; Tbio.
PRO; PR:Q9BZW8; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q9BZW8; protein.
Bgee; ENSG00000122223; Expressed in 96 organ(s), highest expression level in leukocyte.
Genevisible; Q9BZW8; HS.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0002323; P:natural killer cell activation involved in immune response; IDA:UniProtKB.
GO; GO:0071663; P:positive regulation of granzyme B production; IDA:UniProtKB.
GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IDA:UniProtKB.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR024304; NK_rcpt_2B4.
InterPro; IPR024303; NK_rcpt_2B4_Ig_dom.
PANTHER; PTHR12080:SF56; PTHR12080:SF56; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF11465; Receptor_2B4; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Cell membrane;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Innate immunity; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1..21
/evidence="ECO:0000269|PubMed:10556801,
ECO:0000269|PubMed:15340161"
CHAIN 22..370
/note="Natural killer cell receptor 2B4"
/id="PRO_0000014668"
TOPO_DOM 22..229
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 230..250
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 251..370
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 22..127
/note="Ig-like 1"
DOMAIN 131..215
/note="Ig-like 2"
MOTIF 269..274
/note="ITSM 1"
/evidence="ECO:0000250|UniProtKB:Q13291"
MOTIF 295..300
/note="ITSM 2"
/evidence="ECO:0000250|UniProtKB:Q13291"
MOTIF 315..320
/note="ITSM 3"
/evidence="ECO:0000250|UniProtKB:Q13291"
MOTIF 340..345
/note="ITSM 4"
/evidence="ECO:0000250|UniProtKB:Q13291"
MOD_RES 271
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798, ECO:0000305|PubMed:26221972"
MOD_RES 297
/note="Phosphotyrosine; by FYN"
/evidence="ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798, ECO:0000305|PubMed:26221972"
MOD_RES 317
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798"
MOD_RES 342
/note="Phosphotyrosine; by FYN"
/evidence="ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798"
CARBOHYD 71
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:21606496"
CARBOHYD 77
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:21606496"
CARBOHYD 89
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:21606496"
CARBOHYD 164
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 181
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 192
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 200
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 213
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 157..199
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 127..131
/note="Missing (in isoform 2 and isoform 3)"
/evidence="ECO:0000303|PubMed:10358138,
ECO:0000303|PubMed:10359122, ECO:0000303|PubMed:10458320,
ECO:0000303|PubMed:10556801, ECO:0000303|PubMed:10934222,
ECO:0000303|PubMed:15489334, ECO:0000303|Ref.7"
/id="VSP_010397"
VAR_SEQ 128..224
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:10934222"
/id="VSP_010398"
VAR_SEQ 326..334
/note="SGSRKRNHS -> GDRFYSFSG (in isoform 3)"
/evidence="ECO:0000303|PubMed:10934222"
/id="VSP_010399"
VAR_SEQ 335..370
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:10934222"
/id="VSP_010400"
VARIANT 89
/note="N -> D (in dbSNP:rs34846692)"
/id="VAR_056036"
VARIANT 323
/note="S -> F (in dbSNP:rs12064925)"
/id="VAR_056037"
MUTAGEN 68
/note="K->A: Disrupts interaction with CD48; when
associated with A-70."
/evidence="ECO:0000269|PubMed:16002700"
MUTAGEN 70
/note="E->A: Disrupts interaction with CD48; when
associated with A-68."
/evidence="ECO:0000269|PubMed:16002700"
CONFLICT 127..133
/note="ESLLPDK -> GMAMCPM (in Ref. 10; AAK50015)"
/evidence="ECO:0000305"
SEQUENCE 370 AA; 41616 MW; 959FF8DBB0BACC87 CRC64;
MLGQVVTLIL LLLLKVYQGK GCQGSADHVV SISGVPLQLQ PNSIQTKVDS IAWKKLLPSQ
NGFHHILKWE NGSLPSNTSN DRFSFIVKNL SLLIKAAQQQ DSGLYCLEVT SISGKVQTAT
FQVFVFESLL PDKVEKPRLQ GQGKILDRGR CQVALSCLVS RDGNVSYAWY RGSKLIQTAG
NLTYLDEEVD INGTHTYTCN VSNPVSWESH TLNLTQDCQN AHQEFRFWPF LVIIVILSAL
FLGTLACFCV WRRKRKEKQS ETSPKEFLTI YEDVKDLKTR RNHEQEQTFP GGGSTIYSMI
QSQSSAPTSQ EPAYTLYSLI QPSRKSGSRK RNHSPSFNST IYEVIGKSQP KAQNPARLSR
KELENFDVYS


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Related Genes :
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[KIR2DS2 CD158J NKAT5] Killer cell immunoglobulin-like receptor 2DS2 (CD158 antigen-like family member J) (MHC class I NK cell receptor) (NK receptor 183 ActI) (Natural killer-associated transcript 5) (NKAT-5) (p58 natural killer cell receptor clone CL-49) (p58 NK receptor CL-49) (CD antigen CD158j)
[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)
[SLAMF6 KALI UNQ6123/PRO20080] SLAM family member 6 (Activating NK receptor) (NK-T-B-antigen) (NTB-A) (CD antigen CD352)
[Klrk1 Nkg2d Nkrp2] NKG2-D type II integral membrane protein (Killer cell lectin-like receptor subfamily K member 1) (NK cell receptor D) (NK lectin-like receptor) (NKLLR) (NKG2-D-activating NK receptor) (NKR-P2) (CD antigen CD314)
[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)
[KIR2DS5 CD158G NKAT9] Killer cell immunoglobulin-like receptor 2DS5 (CD158 antigen-like family member G) (MHC class I NK cell receptor) (Natural killer-associated transcript 9) (NKAT-9) (CD antigen CD158g)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[CD160 BY55] CD160 antigen (Natural killer cell receptor BY55) (CD antigen CD160) [Cleaved into: CD160 antigen, soluble form]
[Cd160 By55] CD160 antigen (Natural killer cell receptor BY55) (CD antigen CD160) [Cleaved into: CD160 antigen, soluble form]
[Slamf7] SLAM family member 7 (Leukocyte cell-surface antigen) (Novel Ly9) (CD antigen CD319)
[KIR3DS1 NKAT10] Killer cell immunoglobulin-like receptor 3DS1 (MHC class I NK cell receptor) (Natural killer-associated transcript 10) (NKAT-10)
[KIR2DS1 CD158H] Killer cell immunoglobulin-like receptor 2DS1 (CD158 antigen-like family member H) (MHC class I NK cell receptor Eb6 ActI) (CD antigen CD158h)
[CD300A CMRF35H IGSF12 HSPC083] CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CMRF-35-H9) (CMRF35-H9) (CMRF35-H) (IRC1/IRC2) (Immunoglobulin superfamily member 12) (IgSF12) (Inhibitory receptor protein 60) (IRp60) (NK inhibitory receptor) (CD antigen CD300a)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[SLAMF1 SLAM] Signaling lymphocytic activation molecule (CD antigen CD150)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Clec9a Dngr-1] C-type lectin domain family 9 member A (Dendritic cell natural killer lectin group receptor 1) (CD antigen CD370)
[SLAMF7 CS1 UNQ576/PRO1138] SLAM family member 7 (CD2 subset 1) (CD2-like receptor-activating cytotoxic cells) (CRACC) (Membrane protein FOAP-12) (Novel Ly9) (Protein 19A) (CD antigen CD319)
[CD4] T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (CD antigen CD4)

Bibliography :