NCTR3_HUMAN
ID NCTR3_HUMAN Reviewed; 201 AA.
AC O14931; B0S8F2; B0S8F4; B0S8F5; O14930; O14932; O95667; O95668; O95669;
AC Q5ST89; Q5ST90; Q5ST91; Q5ST92; Q5STA3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Natural cytotoxicity triggering receptor 3;
DE AltName: Full=Activating natural killer receptor p30;
DE AltName: Full=Natural killer cell p30-related protein;
DE Short=NK-p30;
DE Short=NKp30;
DE AltName: CD_antigen=CD337;
DE Flags: Precursor;
GN Name=NCR3; Synonyms=1C7, LY117;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH CD3Z, AND FUNCTION.
RC TISSUE=Lymphoid tissue;
RX PubMed=10562324; DOI=10.1084/jem.190.10.1505;
RA Pende D., Parolini S., Pessino A., Sivori S., Augugliaro R., Morelli L.,
RA Marcenaro E., Accame L., Malaspina A., Biassoni R., Bottino C., Moretta L.,
RA Moretta A.;
RT "Identification and molecular characterization of NKp30, a novel triggering
RT receptor involved in natural cytotoxicity mediated by human natural killer
RT cells.";
RL J. Exp. Med. 190:1505-1516(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INTERACTION
RP WITH CD3Z.
RC TISSUE=Peripheral blood;
RA Sato M., Yabe T., Ohashi J., Tsuchiya N., Hanaoka K., Tokunaga K., Juji T.;
RT "Identification of two novel single nucleotide polymorphisms in the NKp30
RT gene in human natural killer cells.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RX PubMed=10202016;
RA Neville M.J., Campbell R.D.;
RT "A new member of the Ig superfamily and a V-ATPase G subunit are among the
RT predicted products of novel genes close to the TNF locus in the human
RT MHC.";
RL J. Immunol. 162:4745-4754(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Spleen;
RX PubMed=8824804; DOI=10.1006/geno.1996.0034;
RA Nalabolu S.R., Shukla H., Nallur G., Parimoo S., Weissman S.M.;
RT "Genes in a 220-kb region spanning the TNF cluster in human MHC.";
RL Genomics 31:215-222(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION IN DENDRITIC CELLS MATURATION.
RX PubMed=15784725; DOI=10.1182/blood-2004-10-4035;
RA Vitale M., Della Chiesa M., Carlomagno S., Pende D., Arico M., Moretta L.,
RA Moretta A.;
RT "NK-dependent DC maturation is mediated by TNFalpha and IFNgamma released
RT upon engagement of the NKp30 triggering receptor.";
RL Blood 106:566-571(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH BAG6.
RX PubMed=18055229; DOI=10.1016/j.immuni.2007.10.010;
RA Pogge von Strandmann E., Simhadri V.R., von Tresckow B., Sasse S.,
RA Reiners K.S., Hansen H.P., Rothe A., Boll B., Simhadri V.L., Borchmann P.,
RA McKinnon P.J., Hallek M., Engert A.;
RT "Human leukocyte antigen-B-associated transcript 3 is released from tumor
RT cells and engages the NKp30 receptor on natural killer cells.";
RL Immunity 27:965-974(2007).
RN [12]
RP INVOLVEMENT IN SUSCEPTIBILITY TO MILD MALARIA.
RX PubMed=17208487; DOI=10.1016/j.micinf.2006.11.002;
RA Delahaye N.F., Barbier M., Fumoux F., Rihet P.;
RT "Association analyses of NCR3 polymorphisms with P. falciparum mild
RT malaria.";
RL Microbes Infect. 9:160-166(2007).
RN [13]
RP FUNCTION IN DENDRITIC CELLS MATURATION, AND INTERACTION WITH BAG6.
RX PubMed=18852879; DOI=10.1371/journal.pone.0003377;
RA Simhadri V.R., Reiners K.S., Hansen H.P., Topolar D., Simhadri V.L.,
RA Nohroudi K., Kufer T.A., Engert A., Pogge von Strandmann E.;
RT "Dendritic cells release HLA-B-associated transcript-3 positive exosomes to
RT regulate natural killer function.";
RL PLoS ONE 3:E3377-E3377(2008).
RN [14]
RP INTERACTION WITH NCR3LG1.
RX PubMed=19528259; DOI=10.1084/jem.20090681;
RA Brandt C.S., Baratin M., Yi E.C., Kennedy J., Gao Z., Fox B., Haldeman B.,
RA Ostrander C.D., Kaifu T., Chabannon C., Moretta A., West R., Xu W.,
RA Vivier E., Levin S.D.;
RT "The B7 family member B7-H6 is a tumor cell ligand for the activating
RT natural killer cell receptor NKp30 in humans.";
RL J. Exp. Med. 206:1495-1503(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-135 IN COMPLEX WITH NCR3LG1,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=21422170; DOI=10.1084/jem.20102548;
RA Li Y., Wang Q., Mariuzza R.A.;
RT "Structure of the human activating natural cytotoxicity receptor NKp30
RT bound to its tumor cell ligand B7-H6.";
RL J. Exp. Med. 208:703-714(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 18-130, INTERACTION WITH NCR3LG1,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=21444796; DOI=10.1073/pnas.1100622108;
RA Joyce M.G., Tran P., Zhuravleva M.A., Jaw J., Colonna M., Sun P.D.;
RT "Crystal structure of human natural cytotoxicity receptor NKp30 and
RT identification of its ligand binding site.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6223-6228(2011).
CC -!- FUNCTION: Cell membrane receptor of natural killer/NK cells that is
CC activated by binding of extracellular ligands including BAG6 and
CC NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells
CC producing these ligands. It controls, for instance, NK cells
CC cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also
CC promotes myeloid dendritic cells (DC) maturation, both through killing
CC DCs that did not acquire a mature phenotype, and inducing the release
CC by NK cells of TNFA and IFNG which promote DC maturation.
CC {ECO:0000269|PubMed:10562324, ECO:0000269|PubMed:15784725,
CC ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.
CC -!- SUBUNIT: Homodimer in the unliganted form. Interacts with CD3Z.
CC Interacts with and is activated by binding to NCR3LG1. Interacts with
CC and is activated by binding to BAG6. {ECO:0000269|PubMed:10562324,
CC ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879,
CC ECO:0000269|PubMed:19528259, ECO:0000269|PubMed:21422170,
CC ECO:0000269|PubMed:21444796, ECO:0000269|Ref.2}.
CC -!- INTERACTION:
CC O14931; P46379: BAG6; NbExp=6; IntAct=EBI-14989262, EBI-347552;
CC O14931; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-14989262, EBI-18304435;
CC O14931; P17931: LGALS3; NbExp=2; IntAct=EBI-14989262, EBI-1170392;
CC O14931; O14931: NCR3; NbExp=9; IntAct=EBI-14989262, EBI-14989262;
CC O14931; Q68D85: NCR3LG1; NbExp=16; IntAct=EBI-14989262, EBI-14061804;
CC O14931-1; P46379-1: BAG6; NbExp=5; IntAct=EBI-15013584, EBI-9640181;
CC O14931-1; P46379-2: BAG6; NbExp=4; IntAct=EBI-15013584, EBI-10988864;
CC O14931-2; P17931: LGALS3; NbExp=3; IntAct=EBI-15098724, EBI-1170392;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10562324};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=1C7a;
CC IsoId=O14931-1; Sequence=Displayed;
CC Name=2; Synonyms=1C7c;
CC IsoId=O14931-2; Sequence=VSP_010413;
CC Name=3; Synonyms=1C7b;
CC IsoId=O14931-3; Sequence=VSP_010412;
CC Name=4; Synonyms=1C7e;
CC IsoId=O14931-4; Sequence=VSP_010411;
CC Name=5; Synonyms=1C7f;
CC IsoId=O14931-5; Sequence=VSP_010411, VSP_010413;
CC Name=6; Synonyms=1C7d;
CC IsoId=O14931-6; Sequence=VSP_010411, VSP_010412;
CC -!- TISSUE SPECIFICITY: Selectively expressed by all resting and activated
CC NK cells and weakly expressed in spleen. {ECO:0000269|PubMed:10562324,
CC ECO:0000269|Ref.2}.
CC -!- POLYMORPHISM: A genetic variation in NCR3 is associated with mild
CC malaria susceptibility [MIM:609148]. {ECO:0000269|PubMed:17208487}.
CC -!- SIMILARITY: Belongs to the natural cytotoxicity receptor (NCR) family.
CC {ECO:0000305}.
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DR EMBL; AJ223153; CAB54004.1; -; mRNA.
DR EMBL; AB055881; BAB78472.1; -; mRNA.
DR EMBL; Y14768; CAA75063.1; -; Genomic_DNA.
DR EMBL; Y14768; CAA75064.1; -; Genomic_DNA.
DR EMBL; Y14768; CAA75065.1; -; Genomic_DNA.
DR EMBL; Y14768; CAA75066.1; -; Genomic_DNA.
DR EMBL; Y14768; CAA75067.1; -; Genomic_DNA.
DR EMBL; Y14768; CAA75068.1; -; Genomic_DNA.
DR EMBL; AF031136; AAB86578.1; -; mRNA.
DR EMBL; AF031137; AAB86579.1; -; mRNA.
DR EMBL; AF031138; AAB86580.1; -; mRNA.
DR EMBL; AF129756; AAD18088.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63393.1; -; Genomic_DNA.
DR EMBL; AL662801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR942185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03439.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03440.1; -; Genomic_DNA.
DR EMBL; BC052582; AAH52582.1; -; mRNA.
DR CCDS; CCDS34397.1; -. [O14931-1]
DR CCDS; CCDS47401.1; -. [O14931-3]
DR CCDS; CCDS47402.1; -. [O14931-2]
DR RefSeq; NP_001138938.1; NM_001145466.1. [O14931-3]
DR RefSeq; NP_001138939.1; NM_001145467.1. [O14931-2]
DR RefSeq; NP_667341.1; NM_147130.2. [O14931-1]
DR RefSeq; XP_006715112.1; XM_006715049.3. [O14931-1]
DR RefSeq; XP_011512761.1; XM_011514459.2. [O14931-4]
DR PDB; 3NOI; X-ray; 1.84 A; A/B=18-130.
DR PDB; 3PV6; X-ray; 2.30 A; B=19-135.
DR PDB; 6YJP; X-ray; 3.10 A; A/B=19-130.
DR PDBsum; 3NOI; -.
DR PDBsum; 3PV6; -.
DR PDBsum; 6YJP; -.
DR AlphaFoldDB; O14931; -.
DR SMR; O14931; -.
DR BioGRID; 129224; 141.
DR CORUM; O14931; -.
DR DIP; DIP-59939N; -.
DR IntAct; O14931; 7.
DR STRING; 9606.ENSP00000342156; -.
DR GlyGen; O14931; 2 sites.
DR BioMuta; NCR3; -.
DR MassIVE; O14931; -.
DR PaxDb; O14931; -.
DR PeptideAtlas; O14931; -.
DR PRIDE; O14931; -.
DR Antibodypedia; 49169; 477 antibodies from 29 providers.
DR DNASU; 259197; -.
DR Ensembl; ENST00000340027.10; ENSP00000342156.5; ENSG00000204475.10. [O14931-1]
DR Ensembl; ENST00000376071.4; ENSP00000365239.4; ENSG00000204475.10. [O14931-5]
DR Ensembl; ENST00000376072.7; ENSP00000365240.3; ENSG00000204475.10. [O14931-2]
DR Ensembl; ENST00000376073.8; ENSP00000365241.4; ENSG00000204475.10. [O14931-3]
DR Ensembl; ENST00000383476.6; ENSP00000372968.2; ENSG00000206430.8. [O14931-2]
DR Ensembl; ENST00000383477.8; ENSP00000372969.4; ENSG00000206430.8. [O14931-1]
DR Ensembl; ENST00000383478.8; ENSP00000372970.4; ENSG00000206430.8. [O14931-3]
DR Ensembl; ENST00000400241.7; ENSP00000383100.3; ENSG00000206430.8. [O14931-5]
DR Ensembl; ENST00000412603.5; ENSP00000389419.1; ENSG00000225211.6. [O14931-2]
DR Ensembl; ENST00000415123.6; ENSP00000416944.2; ENSG00000237103.6. [O14931-1]
DR Ensembl; ENST00000418936.6; ENSP00000402904.2; ENSG00000237808.6. [O14931-2]
DR Ensembl; ENST00000419086.6; ENSP00000416105.2; ENSG00000223833.6. [O14931-5]
DR Ensembl; ENST00000419728.6; ENSP00000406373.2; ENSG00000236315.6. [O14931-5]
DR Ensembl; ENST00000420485.6; ENSP00000412474.2; ENSG00000237808.6. [O14931-5]
DR Ensembl; ENST00000420556.6; ENSP00000405306.2; ENSG00000236315.6. [O14931-1]
DR Ensembl; ENST00000430599.6; ENSP00000416035.2; ENSG00000236979.6. [O14931-1]
DR Ensembl; ENST00000432392.6; ENSP00000409874.2; ENSG00000236315.6. [O14931-3]
DR Ensembl; ENST00000433654.6; ENSP00000391177.2; ENSG00000237808.6. [O14931-3]
DR Ensembl; ENST00000435674.6; ENSP00000390131.2; ENSG00000225211.6. [O14931-1]
DR Ensembl; ENST00000436253.6; ENSP00000395238.2; ENSG00000223833.6. [O14931-3]
DR Ensembl; ENST00000436623.5; ENSP00000404747.1; ENSG00000237103.6. [O14931-2]
DR Ensembl; ENST00000437517.6; ENSP00000398313.2; ENSG00000223833.6. [O14931-1]
DR Ensembl; ENST00000438663.6; ENSP00000415697.2; ENSG00000225211.6. [O14931-5]
DR Ensembl; ENST00000439584.6; ENSP00000408960.2; ENSG00000237103.6. [O14931-3]
DR Ensembl; ENST00000441372.5; ENSP00000399128.1; ENSG00000236979.6. [O14931-2]
DR Ensembl; ENST00000446756.6; ENSP00000411205.2; ENSG00000236979.6. [O14931-3]
DR Ensembl; ENST00000447248.6; ENSP00000389071.2; ENSG00000237808.6. [O14931-1]
DR Ensembl; ENST00000452296.6; ENSP00000403978.2; ENSG00000223833.6. [O14931-2]
DR Ensembl; ENST00000453657.6; ENSP00000409048.2; ENSG00000236979.6. [O14931-5]
DR Ensembl; ENST00000455448.6; ENSP00000415456.2; ENSG00000237103.6. [O14931-5]
DR Ensembl; ENST00000455825.6; ENSP00000389396.2; ENSG00000225211.6. [O14931-3]
DR Ensembl; ENST00000457547.5; ENSP00000412702.1; ENSG00000236315.6. [O14931-2]
DR GeneID; 259197; -.
DR KEGG; hsa:259197; -.
DR MANE-Select; ENST00000340027.10; ENSP00000342156.5; NM_147130.3; NP_667341.1.
DR UCSC; uc003nuv.3; human. [O14931-1]
DR CTD; 259197; -.
DR DisGeNET; 259197; -.
DR GeneCards; NCR3; -.
DR HGNC; HGNC:19077; NCR3.
DR HPA; ENSG00000204475; Group enriched (bone marrow, intestine, lymphoid tissue).
DR MalaCards; NCR3; -.
DR MIM; 609148; phenotype.
DR MIM; 611550; gene.
DR neXtProt; NX_O14931; -.
DR OpenTargets; ENSG00000204475; -.
DR PharmGKB; PA134883693; -.
DR VEuPathDB; HostDB:ENSG00000204475; -.
DR eggNOG; ENOG502SGFD; Eukaryota.
DR GeneTree; ENSGT00390000006603; -.
DR HOGENOM; CLU_132406_0_0_1; -.
DR InParanoid; O14931; -.
DR OMA; PEIHTQE; -.
DR OrthoDB; 1270941at2759; -.
DR PhylomeDB; O14931; -.
DR TreeFam; TF337790; -.
DR PathwayCommons; O14931; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; O14931; -.
DR BioGRID-ORCS; 259197; 11 hits in 1067 CRISPR screens.
DR EvolutionaryTrace; O14931; -.
DR GeneWiki; NCR3; -.
DR GenomeRNAi; 259197; -.
DR Pharos; O14931; Tbio.
DR PRO; PR:O14931; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O14931; protein.
DR Bgee; ENSG00000204475; Expressed in granulocyte and 90 other tissues.
DR ExpressionAtlas; O14931; baseline and differential.
DR Genevisible; O14931; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008037; P:cell recognition; TAS:BHF-UCL.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 1.
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 InterPro; IPR043226; NCR3.
DR PANTHER; PTHR47904; PTHR47904; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..201
FT /note="Natural cytotoxicity triggering receptor 3"
FT /id="PRO_0000015032"
FT TOPO_DOM 19..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..126
FT /note="Ig-like"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21422170, ECO:0000269|PubMed:21444796"
FT VAR_SEQ 66..90
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10202016"
FT /id="VSP_010411"
FT VAR_SEQ 166..201
FT /note="CLTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG -> YAKSTLSGFPQL
FT (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10202016,
FT ECO:0000303|PubMed:8824804"
FT /id="VSP_010412"
FT VAR_SEQ 167..201
FT /note="LTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG -> HCHMGTHCHSSDG
FT PRGVIPEPRCP (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10202016,
FT ECO:0000303|PubMed:10562324, ECO:0000303|PubMed:8824804,
FT ECO:0000303|Ref.2"
FT /id="VSP_010413"
FT VARIANT 103
FT /note="A -> T (in dbSNP:rs11575840)"
FT /id="VAR_044114"
FT VARIANT 174
FT /note="R -> S (in dbSNP:rs3179003)"
FT /id="VAR_044115"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3NOI"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3NOI"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:3NOI"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3PV6"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3PV6"
FT TURN 71..75
FT /evidence="ECO:0007829|PDB:3NOI"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:3NOI"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3NOI"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3NOI"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:3NOI"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3NOI"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3NOI"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:3NOI"
SQ SEQUENCE 201 AA; 21593 MW; 2855AE4D6902D429 CRC64;
MAWMLLLILI MVHPGSCALW VSQPPEIRTL EGSSAFLPCS FNASQGRLAI GSVTWFRDEV
VPGKEVRNGT PEFRGRLAPL ASSRFLHDHQ AELHIRDVRG HDASIYVCRV EVLGLGVGTG
NGTRLVVEKE HPQLGAGTVL LLRAGFYAVS FLSVAVGSTV YYQGKCLTWK GPRRQLPAVV
PAPLPPPCGS SAHLLPPVPG G
