NK1R_MERUN
ID NK1R_MERUN Reviewed; 407 AA.
AC Q5DUB1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 60.
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 Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Meriones.
OX NCBI_TaxID=10047;
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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AJ884917; CAI58658.1; -; mRNA.
DR AlphaFoldDB; Q5DUB1; -.
DR SMR; Q5DUB1; -.
DR ChEMBL; CHEMBL1764942; -.
DR DrugCentral; Q5DUB1; -.
DR Ensembl; ENSMUGT00000029267; ENSMUGP00000025517; ENSMUGG00000021264.
DR OrthoDB; 715197at2759; -.
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; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..407
FT /note="Substance-P receptor"
FT /id="PRO_0000069886"
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..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 CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
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; 46178 MW; 14B2ED9632325023 CRC64;
MDNVLPGDSD LFPNISTNSS ESNQFVQPAW QIVLWAAAYT VIVVTSVVGN VVVMWIILAH
KRMRTVTNYF LVNLAFAEAS MAAFNTVVNF TYAVHNEWYY GLFYCKFHNF FPIAAVFASI
YSMTAVAFDR YMAIIHPLQP RLSATATKVV IFVIWVLALL LAFPQGYYST TETMPGRVVC
MIEWPEHPNR TYEKAYHICV TVLIYFLPLL VIGYAYTVVG ITLWASEIPG DSSDRYHEQV
SAKRKVVKMM IVVVCTFAIC WLPFHVFFLL PYINPDLYVK KFIQQVYLAI MWLAMSSTMY
NPIIYCCLND RFRLGFKHAF RCCPFISAGD YEGLEMKSTR YLQTQGSVYK VSRLETTIST
VVGAHEDEAE EGPKATPSSL DLTSNGSSRS NSKTMTESSS FYSNMLA
