NK1R_HUMAN
ID NK1R_HUMAN Reviewed; 407 AA.
AC P25103; A8K150;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 206.
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=NK1R, TAC1R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1718267; DOI=10.1016/0006-291x(91)91704-g;
RA Takeda Y., Chou K.B., Takeda J., Sachais B.S., Krause J.E.;
RT "Molecular cloning, structural characterization and functional expression
RT of the human substance P receptor.";
RL Biochem. Biophys. Res. Commun. 179:1232-1240(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=1659396; DOI=10.1016/s0006-291x(05)81181-7;
RA Hopkins B., Powell S.J., Danks P., Briggs I., Graham A.;
RT "Isolation and characterisation of the human lung NK-1 receptor cDNA.";
RL Biochem. Biophys. Res. Commun. 180:1110-1117(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1657150; DOI=10.1021/bi00108a006;
RA Gerard N.P., Garraway L.A., Eddy R.L. Jr., Shows T.B., Iijima H.,
RA Paquet J.L., Gerard C.;
RT "Human substance P receptor (NK-1): organization of the gene, chromosome
RT localization, and functional expression of cDNA clones.";
RL Biochemistry 30:10640-10646(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1312928; DOI=10.1111/j.1432-1033.1992.tb16724.x;
RA Takahashi K., Tanaka A., Hara M., Nakanishi S.;
RT "The primary structure and gene organization of human substance P and
RT neuromedin K receptors.";
RL Eur. J. Biochem. 204:1025-1033(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=1310144;
RA Fong T.M., Anderson S.A., Yu H., Huang R.-R.C., Strader C.D.;
RT "Differential activation of intracellular effector by two isoforms of human
RT neurokinin-1 receptor.";
RL Mol. Pharmacol. 41:24-30(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP LACK OF DETECTION OF ISOFORM 2.
RX PubMed=11864635; DOI=10.1016/s0014-2999(02)01278-5;
RA Page N.M., Bell N.J.;
RT "The human tachykinin NK1 (short form) and tachykinin NK4 receptor: a
RT reappraisal.";
RL Eur. J. Pharmacol. 437:27-30(2002).
RN [12]
RP BINDING TO ANTAGONIST CP-96345.
RX PubMed=8384323; DOI=10.1038/362350a0;
RA Fong T.M., Cascieri M.A., Yu H., Bansai A., Swain C., Strader C.D.;
RT "Amino-aromatic interaction between histidine 197 of the neurokinin-1
RT receptor and CP 96345.";
RL Nature 362:350-353(1993).
RN [13]
RP STRUCTURE BY NMR OF 1-364, AND DISULFIDE BOND.
RX PubMed=20937248; DOI=10.1016/j.bbamem.2010.09.023;
RA Gayen A., Goswami S.K., Mukhopadhyay C.;
RT "NMR evidence of GM1-induced conformational change of Substance P using
RT isotropic bicelles.";
RL Biochim. Biophys. Acta 1808:127-139(2011).
RN [14]
RP VARIANT HIS-192, AND CHARACTERIZATION OF VARIANT HIS-192.
RX PubMed=15452552; DOI=10.1038/sj.tpj.6500276;
RA Randolph G.P., Simon J.S., Arreaza M.G., Qiu P., Lachowicz J.E.,
RA Duffy R.A.;
RT "Identification of single-nucleotide polymorphisms of the human neurokinin
RT 1 receptor gene and pharmacological characterization of a Y192H variant.";
RL Pharmacogenomics J. 4:394-402(2004).
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 -!- INTERACTION:
CC P25103; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-6655287, EBI-9083477;
CC P25103; PRO_0000033530 [P20366]: TAC1; NbExp=2; IntAct=EBI-6655287, EBI-6655360;
CC P25103; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-6655287, EBI-348587;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25103-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25103-3; Sequence=VSP_053824;
CC -!- MISCELLANEOUS: [Isoform 2]: In contrast to Fong et al. data
CC (PubMed:1310144), isoform 2 is not detected by PCR in any of 24 human
CC tissues examined including the placenta (PubMed:11864635).
CC {ECO:0000305|PubMed:11864635, ECO:0000305|PubMed:1310144}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Tachykinin entry;
CC URL="https://en.wikipedia.org/wiki/Tachykinin";
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DR EMBL; S62045; AAB20168.2; -; mRNA.
DR EMBL; M74290; AAA60601.1; -; mRNA.
DR EMBL; M81797; AAA59933.1; -; mRNA.
DR EMBL; M76675; AAA59936.1; -; mRNA.
DR EMBL; X65177; CAA46292.1; -; Genomic_DNA.
DR EMBL; X65178; CAA46292.1; JOINED; Genomic_DNA.
DR EMBL; X65179; CAA46292.1; JOINED; Genomic_DNA.
DR EMBL; X65180; CAA46292.1; JOINED; Genomic_DNA.
DR EMBL; X65181; CAA46292.1; JOINED; Genomic_DNA.
DR EMBL; M84425; AAA36641.1; -; mRNA.
DR EMBL; M84426; AAA36644.1; -; mRNA.
DR EMBL; AY462098; AAR23925.1; -; mRNA.
DR EMBL; AK289765; BAF82454.1; -; mRNA.
DR EMBL; CH471053; EAW99596.1; -; Genomic_DNA.
DR EMBL; BC074911; AAH74911.1; -; mRNA.
DR EMBL; BC074912; AAH74912.1; -; mRNA.
DR EMBL; AC007400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1958.1; -. [P25103-1]
DR CCDS; CCDS46345.1; -. [P25103-3]
DR PIR; A41134; JQ1274.
DR RefSeq; NP_001049.1; NM_001058.3. [P25103-1]
DR RefSeq; NP_056542.1; NM_015727.2. [P25103-3]
DR PDB; 2KS9; NMR; -; A=1-364.
DR PDB; 2KSA; NMR; -; A=1-364.
DR PDB; 2KSB; NMR; -; A=1-364.
DR PDB; 6E59; X-ray; 3.40 A; A=1-227, A=238-346.
DR PDB; 6HLL; X-ray; 3.27 A; A=1-226, A=238-335.
DR PDB; 6HLO; X-ray; 2.40 A; A=1-226, A=238-335.
DR PDB; 6HLP; X-ray; 2.20 A; A=1-226, A=238-335.
DR PDB; 7P00; EM; 2.71 A; R=1-335.
DR PDB; 7P02; EM; 2.87 A; R=1-335.
DR PDB; 7RMG; EM; 3.00 A; R=1-407.
DR PDB; 7RMH; EM; 3.10 A; R=1-407.
DR PDB; 7RMI; EM; 3.20 A; R=1-407.
DR PDBsum; 2KS9; -.
DR PDBsum; 2KSA; -.
DR PDBsum; 2KSB; -.
DR PDBsum; 6E59; -.
DR PDBsum; 6HLL; -.
DR PDBsum; 6HLO; -.
DR PDBsum; 6HLP; -.
DR PDBsum; 7P00; -.
DR PDBsum; 7P02; -.
DR PDBsum; 7RMG; -.
DR PDBsum; 7RMH; -.
DR PDBsum; 7RMI; -.
DR AlphaFoldDB; P25103; -.
DR BMRB; P25103; -.
DR SMR; P25103; -.
DR BioGRID; 112732; 72.
DR IntAct; P25103; 46.
DR STRING; 9606.ENSP00000303522; -.
DR BindingDB; P25103; -.
DR ChEMBL; CHEMBL249; -.
DR DrugBank; DB00673; Aprepitant.
DR DrugBank; DB05072; AV608.
DR DrugBank; DB06634; Casopitant.
DR DrugBank; DB05421; CP-122721.
DR DrugBank; DB14019; Fosnetupitant.
DR DrugBank; DB05418; GW 597599.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB09048; Netupitant.
DR DrugBank; DB05466; R673.
DR DrugBank; DB09291; Rolapitant.
DR DrugBank; DB05790; SR 140333.
DR DrugBank; DB00193; Tramadol.
DR DrugBank; DB04894; Vapreotide.
DR DrugBank; DB11949; Vestipitant.
DR DrugBank; DB12436; Vofopitant.
DR DrugCentral; P25103; -.
DR GuidetoPHARMACOLOGY; 360; -.
DR GlyGen; P25103; 2 sites.
DR iPTMnet; P25103; -.
DR PhosphoSitePlus; P25103; -.
DR BioMuta; TACR1; -.
DR DMDM; 128359; -.
DR MassIVE; P25103; -.
DR PaxDb; P25103; -.
DR PeptideAtlas; P25103; -.
DR PRIDE; P25103; -.
DR ProteomicsDB; 54260; -. [P25103-1]
DR ABCD; P25103; 1 sequenced antibody.
DR Antibodypedia; 16803; 569 antibodies from 41 providers.
DR DNASU; 6869; -.
DR Ensembl; ENST00000305249.10; ENSP00000303522.4; ENSG00000115353.11. [P25103-1]
DR Ensembl; ENST00000409848.3; ENSP00000386448.3; ENSG00000115353.11. [P25103-3]
DR GeneID; 6869; -.
DR KEGG; hsa:6869; -.
DR MANE-Select; ENST00000305249.10; ENSP00000303522.4; NM_001058.4; NP_001049.1.
DR UCSC; uc002sng.3; human. [P25103-1]
DR CTD; 6869; -.
DR DisGeNET; 6869; -.
DR GeneCards; TACR1; -.
DR HGNC; HGNC:11526; TACR1.
DR HPA; ENSG00000115353; Low tissue specificity.
DR MIM; 162323; gene.
DR neXtProt; NX_P25103; -.
DR OpenTargets; ENSG00000115353; -.
DR PharmGKB; PA36302; -.
DR VEuPathDB; HostDB:ENSG00000115353; -.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000153745; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; P25103; -.
DR OMA; SYAVHNE; -.
DR OrthoDB; 715197at2759; -.
DR PhylomeDB; P25103; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; P25103; -.
DR Reactome; R-HSA-380095; Tachykinin receptors bind tachykinins.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P25103; -.
DR SIGNOR; P25103; -.
DR BioGRID-ORCS; 6869; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; TACR1; human.
DR EvolutionaryTrace; P25103; -.
DR GeneWiki; Tachykinin_receptor_1; -.
DR GenomeRNAi; 6869; -.
DR Pharos; P25103; Tclin.
DR PRO; PR:P25103; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P25103; protein.
DR Bgee; ENSG00000115353; Expressed in endocervix and 126 other tissues.
DR Genevisible; P25103; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0061827; C:sperm head; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB.
DR GO; GO:0016496; F:substance P receptor activity; IMP:UniProtKB.
DR GO; GO:0004995; F:tachykinin receptor activity; IBA:GO_Central.
DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
DR GO; GO:0002118; P:aggressive behavior; IEA:Ensembl.
DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
DR GO; GO:0009582; P:detection of abiotic stimulus; TAS:ProtInc.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0035106; P:operant conditioning; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0045760; P:positive regulation of action potential; IEA:Ensembl.
DR GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IEA:Ensembl.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IEA:Ensembl.
DR GO; GO:0045778; P:positive regulation of ossification; IEA:Ensembl.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0046878; P:positive regulation of saliva secretion; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IEA:Ensembl.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0010193; P:response to ozone; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; IEA:Ensembl.
DR GO; GO:0042713; P:sperm ejaculation; IEA:Ensembl.
DR GO; GO:0007217; P:tachykinin receptor signaling pathway; IDA:BHF-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..407
FT /note="Substance-P receptor"
FT /id="PRO_0000069885"
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 364..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 BINDING 197
FT /ligand="CP-96345"
FT /ligand_id="ChEBI:CHEBI:187905"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:8384323"
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,
FT ECO:0000269|PubMed:20937248"
FT VAR_SEQ 312..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1310144"
FT /id="VSP_053824"
FT VARIANT 192
FT /note="Y -> H (display properties similar to those of the
FT wild-type receptor; dbSNP:rs200685841)"
FT /evidence="ECO:0000269|PubMed:15452552"
FT /id="VAR_026826"
FT CONFLICT 116
FT /note="V -> C (in Ref. 3; AAA59936)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="V -> I (in Ref. 3; AAA59936)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2KS9"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2KS9"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2KS9"
FT HELIX 29..58
FT /evidence="ECO:0007829|PDB:6HLP"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6HLP"
FT HELIX 66..94
FT /evidence="ECO:0007829|PDB:6HLP"
FT HELIX 102..135
FT /evidence="ECO:0007829|PDB:6HLP"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:7P02"
FT HELIX 144..168
FT /evidence="ECO:0007829|PDB:6HLP"
FT STRAND 169..182
FT /evidence="ECO:0007829|PDB:6HLP"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:6HLP"
FT HELIX 206..225
FT /evidence="ECO:0007829|PDB:6HLP"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2KS9"
FT HELIX 238..273
FT /evidence="ECO:0007829|PDB:6HLP"
FT TURN 275..279
FT /evidence="ECO:0007829|PDB:7P00"
FT HELIX 283..308
FT /evidence="ECO:0007829|PDB:6HLP"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:6HLP"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6HLP"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6HLP"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:2KS9"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2KS9"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:2KS9"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2KS9"
SQ SEQUENCE 407 AA; 46251 MW; 2AFFD3F61B1A3041 CRC64;
MDNVLPVDSD LSPNISTNTS EPNQFVQPAW QIVLWAAAYT VIVVTSVVGN VVVMWIILAH
KRMRTVTNYF LVNLAFAEAS MAAFNTVVNF TYAVHNEWYY GLFYCKFHNF FPIAAVFASI
YSMTAVAFDR YMAIIHPLQP RLSATATKVV ICVIWVLALL LAFPQGYYST TETMPSRVVC
MIEWPEHPNK IYEKVYHICV TVLIYFLPLL VIGYAYTVVG ITLWASEIPG DSSDRYHEQV
SAKRKVVKMM IVVVCTFAIC WLPFHIFFLL PYINPDLYLK KFIQQVYLAI MWLAMSSTMY
NPIIYCCLND RFRLGFKHAF RCCPFISAGD YEGLEMKSTR YLQTQGSVYK VSRLETTIST
VVGAHEEEPE DGPKATPSSL DLTSNCSSRS DSKTMTESFS FSSNVLS
