ID NCTR3_HUMAN Reviewed; 201 AA. AC O14931; B0S8F2; B0S8F4; B0S8F5; O14930; O14932; O95667; O95668; AC O95669; Q5ST89; Q5ST90; Q5ST91; Q5ST92; Q5STA3; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JAN-2019, entry version 162. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Morelli L., Marcenaro E., Accame L., Malaspina A., Biassoni R., RA Bottino C., Moretta L., Moretta A.; RT "Identification and molecular characterization of NKp30, a novel RT triggering receptor involved in natural cytotoxicity mediated by human RT natural killer cells."; RL J. Exp. Med. 190:1505-1516(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND RP INTERACTION WITH CD3Z. RC TISSUE=Peripheral blood; RA Sato M., Yabe T., Ohashi J., Tsuchiya N., Hanaoka K., Tokunaga K., RA Juji T.; RT "Identification of two novel single nucleotide polymorphisms in the RT NKp30 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 RT the predicted products of novel genes close to the TNF locus in the RT human 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., RA Campbell R.D., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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 RT project: 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., RA Moretta L., Moretta A.; RT "NK-dependent DC maturation is mediated by TNFalpha and IFNgamma RT released 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., RA Borchmann P., McKinnon P.J., Hallek M., Engert A.; RT "Human leukocyte antigen-B-associated transcript 3 is released from RT tumor 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 RT exosomes to 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., RA Haldeman B., Ostrander C.D., Kaifu T., Chabannon C., Moretta A., RA West R., Xu W., 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 RP NCR3LG1, 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 RP NCR3LG1, 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 CC is activated by binding of extracellular ligands including BAG6 CC and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring CC cells 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 CC killing DCs that did not acquire a mature phenotype, and inducing CC the release by NK cells of TNFA and IFNG which promote DC CC maturation. {ECO:0000269|PubMed:10562324, CC ECO:0000269|PubMed:15784725, ECO:0000269|PubMed:18055229, CC 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 CC with and is activated by binding to BAG6. CC {ECO:0000269|PubMed:10562324, ECO:0000269|PubMed:18055229, CC ECO:0000269|PubMed:18852879, ECO:0000269|PubMed:19528259, CC ECO:0000269|PubMed:21422170, ECO:0000269|PubMed:21444796, CC ECO:0000269|Ref.2}. CC -!- INTERACTION: CC Self; NbExp=9; IntAct=EBI-14989262, EBI-14989262; CC P46379:BAG6; NbExp=6; IntAct=EBI-14989262, EBI-347552; CC P46379-1:BAG6; NbExp=5; IntAct=EBI-15013584, EBI-9640181; CC P46379-2:BAG6; NbExp=4; IntAct=EBI-15013584, EBI-10988864; CC P17931:LGALS3; NbExp=3; IntAct=EBI-15098724, EBI-1170392; CC Q68D85:NCR3LG1; NbExp=16; IntAct=EBI-14989262, EBI-14061804; 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 Note=No experimental confirmation available.; CC Name=5; Synonyms=1C7f; CC IsoId=O14931-5; Sequence=VSP_010411, VSP_010413; CC Note=No experimental confirmation available.; CC Name=6; Synonyms=1C7d; CC IsoId=O14931-6; Sequence=VSP_010411, VSP_010412; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Selectively expressed by all resting and CC activated NK cells and weakly expressed in spleen. CC {ECO:0000269|PubMed:10562324, ECO:0000269|Ref.2}. CC -!- POLYMORPHISM: A genetic variation in NCR3 is associated with mild CC malaria susceptibility [MIM:609148]. CC {ECO:0000269|PubMed:17208487}. CC -!- SIMILARITY: Belongs to the natural cytotoxicity receptor (NCR) CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.509513; -. DR PDB; 3NOI; X-ray; 1.84 A; A/B=18-130. DR PDB; 3PV6; X-ray; 2.30 A; B=19-135. DR PDBsum; 3NOI; -. DR PDBsum; 3PV6; -. DR ProteinModelPortal; O14931; -. DR SMR; O14931; -. DR BioGrid; 129224; 2. DR CORUM; O14931; -. DR DIP; DIP-59939N; -. DR IntAct; O14931; 7. DR STRING; 9606.ENSP00000342156; -. DR BioMuta; NCR3; -. DR PaxDb; O14931; -. DR PeptideAtlas; O14931; -. DR PRIDE; O14931; -. DR ProteomicsDB; 48310; -. DR ProteomicsDB; 48311; -. [O14931-2] DR ProteomicsDB; 48312; -. [O14931-3] DR ProteomicsDB; 48313; -. [O14931-4] DR ProteomicsDB; 48314; -. [O14931-5] DR ProteomicsDB; 48315; -. [O14931-6] DR DNASU; 259197; -. DR Ensembl; ENST00000340027; ENSP00000342156; ENSG00000204475. [O14931-1] DR Ensembl; ENST00000376071; ENSP00000365239; ENSG00000204475. [O14931-5] DR Ensembl; ENST00000376072; ENSP00000365240; ENSG00000204475. [O14931-2] DR Ensembl; ENST00000376073; ENSP00000365241; ENSG00000204475. [O14931-3] DR Ensembl; ENST00000383476; ENSP00000372968; ENSG00000206430. [O14931-2] DR Ensembl; ENST00000383477; ENSP00000372969; ENSG00000206430. [O14931-1] DR Ensembl; ENST00000383478; ENSP00000372970; ENSG00000206430. [O14931-3] DR Ensembl; ENST00000400241; ENSP00000383100; ENSG00000206430. [O14931-5] DR Ensembl; ENST00000412603; ENSP00000389419; ENSG00000225211. [O14931-2] DR Ensembl; ENST00000415123; ENSP00000416944; ENSG00000237103. [O14931-1] DR Ensembl; ENST00000418936; ENSP00000402904; ENSG00000237808. [O14931-2] DR Ensembl; ENST00000419086; ENSP00000416105; ENSG00000223833. [O14931-5] DR Ensembl; ENST00000419728; ENSP00000406373; ENSG00000236315. [O14931-5] DR Ensembl; ENST00000420485; ENSP00000412474; ENSG00000237808. [O14931-5] DR Ensembl; ENST00000420556; ENSP00000405306; ENSG00000236315. [O14931-1] DR Ensembl; ENST00000430599; ENSP00000416035; ENSG00000236979. [O14931-1] DR Ensembl; ENST00000432392; ENSP00000409874; ENSG00000236315. [O14931-3] DR Ensembl; ENST00000433654; ENSP00000391177; ENSG00000237808. [O14931-3] DR Ensembl; ENST00000435674; ENSP00000390131; ENSG00000225211. [O14931-1] DR Ensembl; ENST00000436253; ENSP00000395238; ENSG00000223833. [O14931-3] DR Ensembl; ENST00000436623; ENSP00000404747; ENSG00000237103. [O14931-2] DR Ensembl; ENST00000437517; ENSP00000398313; ENSG00000223833. [O14931-1] DR Ensembl; ENST00000438663; ENSP00000415697; ENSG00000225211. [O14931-5] DR Ensembl; ENST00000439584; ENSP00000408960; ENSG00000237103. [O14931-3] DR Ensembl; ENST00000441372; ENSP00000399128; ENSG00000236979. [O14931-2] DR Ensembl; ENST00000446756; ENSP00000411205; ENSG00000236979. [O14931-3] DR Ensembl; ENST00000447248; ENSP00000389071; ENSG00000237808. [O14931-1] DR Ensembl; ENST00000452296; ENSP00000403978; ENSG00000223833. [O14931-2] DR Ensembl; ENST00000453657; ENSP00000409048; ENSG00000236979. [O14931-5] DR Ensembl; ENST00000455448; ENSP00000415456; ENSG00000237103. [O14931-5] DR Ensembl; ENST00000455825; ENSP00000389396; ENSG00000225211. [O14931-3] DR Ensembl; ENST00000457547; ENSP00000412702; ENSG00000236315. [O14931-2] DR GeneID; 259197; -. DR KEGG; hsa:259197; -. DR UCSC; uc003nuv.3; human. [O14931-1] DR CTD; 259197; -. DR DisGeNET; 259197; -. DR EuPathDB; HostDB:ENSG00000204475.9; -. DR GeneCards; NCR3; -. DR HGNC; HGNC:19077; NCR3. DR MalaCards; NCR3; -. DR MIM; 609148; phenotype. DR MIM; 611550; gene. DR neXtProt; NX_O14931; -. DR OpenTargets; ENSG00000204475; -. DR PharmGKB; PA134883693; -. DR eggNOG; ENOG410J2FC; Eukaryota. DR eggNOG; ENOG410Z2AU; LUCA. DR GeneTree; ENSGT00390000006603; -. DR HOVERGEN; HBG052590; -. DR InParanoid; O14931; -. DR KO; K06743; -. DR OMA; RFLCDHQ; -. DR OrthoDB; 1270941at2759; -. DR PhylomeDB; O14931; -. DR TreeFam; TF337790; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR EvolutionaryTrace; O14931; -. DR GeneWiki; NCR3; -. DR GenomeRNAi; 259197; -. DR PRO; PR:O14931; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000204475; Expressed in 75 organ(s), highest expression level in leukocyte. 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 GO; GO:0050776; P:regulation of immune response; TAS:Reactome. 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 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; Complete proteome; KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; KW Membrane; Polymorphism; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 201 Natural cytotoxicity triggering receptor FT 3. FT /FTId=PRO_0000015032. FT TOPO_DOM 19 135 Extracellular. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TOPO_DOM 157 201 Cytoplasmic. {ECO:0000255}. FT DOMAIN 19 126 Ig-like. FT CARBOHYD 42 42 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 121 121 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 39 108 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:21422170, FT ECO:0000269|PubMed:21444796}. FT VAR_SEQ 66 90 Missing (in isoform 4, isoform 5 and FT isoform 6). FT {ECO:0000303|PubMed:10202016}. FT /FTId=VSP_010411. FT VAR_SEQ 166 201 CLTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG -> Y FT AKSTLSGFPQL (in isoform 3 and isoform 6). FT {ECO:0000303|PubMed:10202016, FT ECO:0000303|PubMed:8824804}. FT /FTId=VSP_010412. FT VAR_SEQ 167 201 LTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG -> HC FT HMGTHCHSSDGPRGVIPEPRCP (in isoform 2 and FT isoform 5). {ECO:0000303|PubMed:10202016, FT ECO:0000303|PubMed:10562324, FT ECO:0000303|PubMed:8824804, FT ECO:0000303|Ref.2}. FT /FTId=VSP_010413. FT VARIANT 103 103 A -> T (in dbSNP:rs11575840). FT /FTId=VAR_044114. FT VARIANT 174 174 R -> S (in dbSNP:rs3179003). FT /FTId=VAR_044115. FT STRAND 25 30 {ECO:0000244|PDB:3NOI}. FT STRAND 35 37 {ECO:0000244|PDB:3NOI}. FT STRAND 51 59 {ECO:0000244|PDB:3NOI}. FT HELIX 62 64 {ECO:0000244|PDB:3PV6}. FT HELIX 66 68 {ECO:0000244|PDB:3PV6}. FT TURN 71 75 {ECO:0000244|PDB:3NOI}. FT HELIX 82 86 {ECO:0000244|PDB:3NOI}. FT STRAND 93 97 {ECO:0000244|PDB:3NOI}. FT HELIX 100 102 {ECO:0000244|PDB:3NOI}. FT STRAND 104 112 {ECO:0000244|PDB:3NOI}. FT TURN 113 115 {ECO:0000244|PDB:3NOI}. FT STRAND 116 119 {ECO:0000244|PDB:3NOI}. FT STRAND 123 128 {ECO:0000244|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 //