NK1R_CAVPO
ID NK1R_CAVPO Reviewed; 407 AA.
AC P30547;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Substance-P receptor;
DE Short=SPR;
DE AltName: Full=NK-1 receptor;
DE Short=NK-1R;
DE AltName: Full=Tachykinin receptor 1;
GN Name=TACR1; Synonyms=TAC1R;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RX PubMed=1374648; DOI=10.1016/0167-4781(92)90105-9;
RA Gorbulev V., Akhundova A., Luzius H., Fahrenholz F.;
RT "Molecular cloning of substance P receptor cDNA from guinea-pig uterus.";
RL Biochim. Biophys. Acta 1131:99-102(1992).
CC -!- FUNCTION: This is a receptor for the tachykinin neuropeptide substance
CC P. It is probably 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 P > substance K
CC > neuromedin-K.
CC -!- SUBUNIT: Interacts with ARRB1. {ECO:0000250}.
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; X64323; CAA45608.1; -; mRNA.
DR PIR; S23510; S23510.
DR RefSeq; NP_001166332.1; NM_001172861.1.
DR RefSeq; XP_013006930.1; XM_013151476.1.
DR AlphaFoldDB; P30547; -.
DR SMR; P30547; -.
DR STRING; 10141.ENSCPOP00000001340; -.
DR BindingDB; P30547; -.
DR ChEMBL; CHEMBL3942; -.
DR PRIDE; P30547; -.
DR Ensembl; ENSCPOT00000046226; ENSCPOP00000030949; ENSCPOG00000036008.
DR GeneID; 100135626; -.
DR KEGG; cpoc:100135626; -.
DR CTD; 6869; -.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000153745; -.
DR InParanoid; P30547; -.
DR OMA; SYAVHNE; -.
DR OrthoDB; 715197at2759; -.
DR TreeFam; TF315303; -.
DR PRO; PR:P30547; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000036008; Expressed in thyroid gland and 5 other tissues.
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:0061827; C:sperm head; IEA:Ensembl.
DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR GO; GO:0016496; F:substance P receptor activity; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0070472; P:regulation of uterine smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001681; Neurokn_rcpt.
DR InterPro; IPR000046; NK1_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01024; NEUROKININ1R.
DR PRINTS; PR00244; NEUROKININR.
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..407
FT /note="Substance-P receptor"
FT /id="PRO_0000069884"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 363..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 407 AA; 46257 MW; F8C5D31C4BB45E6B CRC64;
MDNVLPVDSD LFPNISTNTS EPNQFVQPAW QIVLWAAAYT VIVVTSVVGN VVVMWIILAH
KRMRTVTNYF LVNLAFAEAS MAAFNTVVNF TYAVHNEWYY GLFYCKFHNF FPIAAVFASI
YSMTAVAFDR YMAIIHPLQP RLSATATKVV ICVIWVLALL LAFPQGYYST TETMPGRVVC
MIEWPSHPDK IYEKVYHICV TVLIYFLPLL VIGYAYTVVG ITLWASEIPG DSSDRYHEQV
SAKRKVVKMM IVVVCTFAIC WLPFHIFFLL PYINPDLYLK KFIQQVYLAI MWLAMSSTMY
NPIIYCCLND RFRLGFKHAF RCCPFISAAD YEGLEMKSTR YFQTQGSVYK VSRLETTIST
VVGAHEEDPE EGPKATPSSL DLTSNGSSRS NSKTVTESSS FYSNMLS
