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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.
20-JUN-2018, entry version 153.
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;
Note=Binds to CD48 with a sronger affinity than isoform 1, and
interactions induces greater cytotoxicity and intracellular
calcium release.;
Name=3; Synonyms=H2B4;
IsoId=Q9BZW8-3; Sequence=VSP_010397, VSP_010399, VSP_010400;
Note=No experimental confirmation available.;
Name=4; Synonyms=H2B4b;
IsoId=Q9BZW8-4; Sequence=VSP_010398;
Note=No experimental confirmation available.;
-!- 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}.
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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]
UniGene; Hs.157872; -.
ProteinModelPortal; Q9BZW8; -.
BioGrid; 119709; 24.
DIP; DIP-40331N; -.
ELM; Q9BZW8; -.
IntAct; Q9BZW8; 16.
MINT; Q9BZW8; -.
STRING; 9606.ENSP00000357012; -.
iPTMnet; Q9BZW8; -.
PhosphoSitePlus; Q9BZW8; -.
BioMuta; CD244; -.
DMDM; 47605541; -.
PaxDb; Q9BZW8; -.
PeptideAtlas; Q9BZW8; -.
PRIDE; Q9BZW8; -.
ProteomicsDB; 79913; -.
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; ENSGT00510000049238; -.
HOVERGEN; HBG050850; -.
InParanoid; Q9BZW8; -.
KO; K06582; -.
OMA; TIYEDVK; -.
OrthoDB; EOG091G0DZW; -.
PhylomeDB; Q9BZW8; -.
TreeFam; TF334964; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
SignaLink; Q9BZW8; -.
ChiTaRS; CD244; human.
GeneWiki; CD244; -.
GenomeRNAi; 51744; -.
PRO; PR:Q9BZW8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000122223; -.
CleanEx; HS_CD244; -.
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; 2.
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;
Complete proteome; 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 {ECO:0000269|PubMed:10556801,
ECO:0000269|PubMed:15340161}.
CHAIN 22 370 Natural killer cell receptor 2B4.
/FTId=PRO_0000014668.
TOPO_DOM 22 229 Extracellular. {ECO:0000255}.
TRANSMEM 230 250 Helical. {ECO:0000255}.
TOPO_DOM 251 370 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 127 Ig-like 1.
DOMAIN 131 215 Ig-like 2.
MOTIF 269 274 ITSM 1. {ECO:0000250|UniProtKB:Q13291}.
MOTIF 295 300 ITSM 2. {ECO:0000250|UniProtKB:Q13291}.
MOTIF 315 320 ITSM 3. {ECO:0000250|UniProtKB:Q13291}.
MOTIF 340 345 ITSM 4. {ECO:0000250|UniProtKB:Q13291}.
MOD_RES 271 271 Phosphotyrosine.
{ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798,
ECO:0000305|PubMed:26221972}.
MOD_RES 297 297 Phosphotyrosine; by FYN.
{ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798,
ECO:0000305|PubMed:26221972}.
MOD_RES 317 317 Phosphotyrosine.
{ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798}.
MOD_RES 342 342 Phosphotyrosine; by FYN.
{ECO:0000305|PubMed:12458214,
ECO:0000305|PubMed:15713798}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21606496}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21606496}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21606496}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 157 199 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 127 131 Missing (in isoform 2 and isoform 3).
{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}.
/FTId=VSP_010397.
VAR_SEQ 128 224 Missing (in isoform 4).
{ECO:0000303|PubMed:10934222}.
/FTId=VSP_010398.
VAR_SEQ 326 334 SGSRKRNHS -> GDRFYSFSG (in isoform 3).
{ECO:0000303|PubMed:10934222}.
/FTId=VSP_010399.
VAR_SEQ 335 370 Missing (in isoform 3).
{ECO:0000303|PubMed:10934222}.
/FTId=VSP_010400.
VARIANT 89 89 N -> D (in dbSNP:rs34846692).
/FTId=VAR_056036.
VARIANT 323 323 S -> F (in dbSNP:rs12064925).
/FTId=VAR_056037.
MUTAGEN 68 68 K->A: Disrupts interaction with CD48;
when associated with A-70.
{ECO:0000269|PubMed:16002700}.
MUTAGEN 70 70 E->A: Disrupts interaction with CD48;
when associated with A-68.
{ECO:0000269|PubMed:16002700}.
CONFLICT 127 133 ESLLPDK -> GMAMCPM (in Ref. 10;
AAK50015). {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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