NCTR3_PANTR
ID NCTR3_PANTR Reviewed; 201 AA.
AC P61484;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Natural cytotoxicity triggering receptor 3;
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;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoid tissue;
RA Biassoni R.;
RT "Characterization of natural killer receptors in chimpanzees.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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 that promote DC maturation.
CC {ECO:0000250|UniProtKB:O14931}.
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:0000250|UniProtKB:O14931}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14931};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the natural cytotoxicity receptor (NCR) family.
CC {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; AJ516006; CAD56759.1; -; mRNA.
DR RefSeq; NP_001009016.1; NM_001009016.1.
DR AlphaFoldDB; P61484; -.
DR SMR; P61484; -.
DR STRING; 9598.ENSPTRP00000030663; -.
DR PaxDb; P61484; -.
DR GeneID; 449613; -.
DR KEGG; ptr:449613; -.
DR CTD; 259197; -.
DR eggNOG; ENOG502SGFD; Eukaryota.
DR HOGENOM; CLU_132406_0_0_1; -.
DR InParanoid; P61484; -.
DR OrthoDB; 1030635at2759; -.
DR TreeFam; TF337790; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; ISS:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW 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_0000015035"
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"
SQ SEQUENCE 201 AA; 21656 MW; 3768ACC768E8D749 CRC64;
MAWMLLLILI MVHPGSCALW VSQPPEIRTL EGSSAFLPCS FNASQGRLAI GSVTWFRDEV
VPGKEVRNET PEFRGRLAPL ASSRFLHDHQ AELHIRDVRG HDASIYVCRV EVLGLGVGTG
NGTRLVVEKE HPQLGAGTVL LLRAGFYAVS FLSVAVGSTV YYQGKCLTWK GPRRQLPAVV
PAPLPPPCGS SAQLLPPVPG G
