NK1R_CANLF
ID NK1R_CANLF Reviewed; 407 AA.
AC Q5DUB3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Engberg S., Drmota T.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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; AJ884915; CAI58656.1; -; mRNA.
DR RefSeq; NP_001012637.1; NM_001012619.1.
DR AlphaFoldDB; Q5DUB3; -.
DR BMRB; Q5DUB3; -.
DR SMR; Q5DUB3; -.
DR STRING; 9615.ENSCAFP00000012041; -.
DR PaxDb; Q5DUB3; -.
DR Ensembl; ENSCAFT00030032971; ENSCAFP00030028765; ENSCAFG00030017843.
DR Ensembl; ENSCAFT00040012681; ENSCAFP00040010993; ENSCAFG00040006803.
DR Ensembl; ENSCAFT00845029508; ENSCAFP00845023180; ENSCAFG00845016647.
DR GeneID; 403815; -.
DR KEGG; cfa:403815; -.
DR CTD; 6869; -.
DR VEuPathDB; HostDB:ENSCAFG00845016647; -.
DR VGNC; VGNC:47066; TACR1.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000153745; -.
DR InParanoid; Q5DUB3; -.
DR OrthoDB; 715197at2759; -.
DR Proteomes; UP000002254; Chromosome 17.
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_0000069883"
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 365..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..394
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; 46464 MW; 18C8F4EA4FBF4F14 CRC64;
MDNVLQVDSD LFPNISTNTS EPNQFVQPAW QIVLWAAAYT VIVVTSVVGN VVVMWIILAH
KRMRTVTNYF LVNLAFAEAS MAAFNTVVNF TYAVHNEWYY GLFYCKFHNF FPIAAVFASI
YSMTAVAFDR YMAIIHPLQP RLSATATKVV ICVIWVLALL LAFPQGYYST TETMPNRVVC
MIEWPEHPNK IYEKVYHICV TVLIYFLPLL VIGYAYTVVG ITLWASEIPG DSSDRYHEQV
SAKRKVVKMM IVVVCTFAIC WLPFHIFFLL PYINPDLYLE KFIQQVYLAI MWLAMSSTMY
NPIIYCCLND RFRLGFKHAF RCCPFISAGD YEGLEMKSTR YLQTQGSVYK VSRLETTVST
VVGAHEEELE DGPKTTPSSL DLTSNGSSRS DSKTMTESFS FYSNMLS
