NK2R_BOVIN
ID NK2R_BOVIN Reviewed; 384 AA.
AC P05363;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Substance-K receptor;
DE Short=SKR;
DE AltName: Full=NK-2 receptor;
DE Short=NK-2R;
DE AltName: Full=Neurokinin A receptor;
DE AltName: Full=Tachykinin receptor 2;
GN Name=TACR2; Synonyms=TAC2R;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2823146; DOI=10.1038/329836a0;
RA Masu Y., Nakayama K., Tamaki H., Harada Y., Kuno M., Nakanishi S.;
RT "cDNA cloning of bovine substance-K receptor through oocyte expression
RT system.";
RL Nature 329:836-838(1987).
CC -!- FUNCTION: This is a receptor for the tachykinin neuropeptide substance
CC K (neurokinin A). It is associated with G proteins that activate a
CC phosphatidylinositol-calcium second messenger system. The rank order of
CC affinity of this receptor to tachykinins is: substance K > neuromedin-K
CC > substance P.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X06295; CAA29621.1; -; mRNA.
DR PIR; S00516; S00516.
DR RefSeq; NP_776894.1; NM_174469.2.
DR AlphaFoldDB; P05363; -.
DR SMR; P05363; -.
DR STRING; 9913.ENSBTAP00000028870; -.
DR BindingDB; P05363; -.
DR ChEMBL; CHEMBL4815; -.
DR PaxDb; P05363; -.
DR Ensembl; ENSBTAT00000028870; ENSBTAP00000028870; ENSBTAG00000021664.
DR GeneID; 282088; -.
DR KEGG; bta:282088; -.
DR CTD; 6865; -.
DR VEuPathDB; HostDB:ENSBTAG00000021664; -.
DR VGNC; VGNC:35561; TACR2.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000155512; -.
DR InParanoid; P05363; -.
DR OMA; RRVNRCH; -.
DR OrthoDB; 715197at2759; -.
DR TreeFam; TF315303; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000021664; Expressed in omasum and 68 other tissues.
DR ExpressionAtlas; P05363; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0061827; C:sperm head; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IBA:GO_Central.
DR GO; GO:0016497; F:substance K receptor activity; IBA:GO_Central.
DR GO; GO:0004995; F:tachykinin receptor activity; IBA:GO_Central.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IBA:GO_Central.
DR GO; GO:0070472; P:regulation of uterine smooth muscle contraction; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001681; Neurokn_rcpt.
DR InterPro; IPR000913; NK2_rcpt.
DR PANTHER; PTHR46925:SF3; PTHR46925:SF3; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01025; NEUROKININ2R.
DR PRINTS; PR00244; NEUROKININR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Substance-K receptor"
FT /id="PRO_0000069890"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 324
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 384 AA; 43069 MW; 1EC676BBD7FF1672 CRC64;
MGACVVMTDI NISSGLDSNA TGITAFSMPG WQLALWTAAY LALVLVAVMG NATVIWIILA
HQRMRTVTNY FIVNLALADL CMAAFNAAFN FVYASHNIWY FGRAFCYFQN LFPITAMFVS
IYSMTAIAAD RYMAIVHPFQ PRLSAPGTRA VIAGIWLVAL ALAFPQCFYS TITTDEGATK
CVVAWPEDSG GKMLLLYHLI VIALIYFLPL VVMFVAYSVI GLTLWRRSVP GHQAHGANLR
HLQAKKKFVK TMVLVVVTFA ICWLPYHLYF ILGTFQEDIY CHKFIQQVYL ALFWLAMSST
MYNPIIYCCL NHRFRSGFRL AFRCCPWVTP TEEDKMELTY TPSLSTRVNR CHTKEIFFMS
GDVAPSEAVN GQAESPQAGV STEP
