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 04-NOV-2026, entry version 226. 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), AND FUNCTION. 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; DOI=10.1016/s0026-895x(25)08831-5; 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 SUBCELLULAR LOCATION. RX PubMed=37968728; DOI=10.1186/s13578-023-01165-6; RA Nguyen L.P., Cho M., Nguyen T.U., Park H.K., Nguyen H.T., Mykhailova K., RA Hurh S., Kim H.R., Seong J.Y., Lee C.S., Ham B.J., Hwang J.I.; RT "Neurokinin-2 receptor negatively modulates substance P responses by RT forming complex with Neurokinin-1 receptor."; RL Cell Biosci. 13:212-212(2023). RN [14] 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 [15] RP VARIANT HIS-192, CHARACTERIZATION OF VARIANT HIS-192, AND FUNCTION. 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: Receptor for the tachykinin substance P, also able to bind CC and respond to tachynins neurokinin A/substance K and neurokinin CC B/neuromedin-K (PubMed:1718267, PubMed:15452552). The rank order of CC affinity of this receptor to tachykinins is: substance P > neurokinin CC A/substance K > neurokinin B/neuromedin-K (PubMed:1718267). Substance P CC binding to its receptor triggers G protein-coupled receptor signaling CC via activation of phosphatidylinositol hydrolysis by phospholipase C. CC Substance P binding also triggers signaling via activation of adenylate CC cyclase activity which results in increased intracellular levels of CC cyclic AMP (cAMP) (By similarity). {ECO:0000250|UniProtKB:P14600, CC ECO:0000269|PubMed:15452552, ECO:0000269|PubMed:1718267}. 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 {ECO:0000269|PubMed:37968728}; CC Multi-pass membrane protein {ECO:0000255}. Early endosome CC {ECO:0000250|UniProtKB:P14600}. Note=After signaling cascade CC initiation, substance P binding results in receptor internalization and CC localization to early endosomes, followed by receptor recycling to the CC cell surface. {ECO:0000250|UniProtKB:P14600}. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001058.4. [P25103-1] DR RefSeq; NP_056542.1; NM_015727.3. [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; 6J20; X-ray; 2.70 A; A=2-228, A=237-335. DR PDB; 6J21; X-ray; 3.20 A; A=2-228, A=237-335. 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 PDB; 8U26; EM; 2.50 A; R=1-407. DR AlphaFoldDB; P25103; -. DR BMRB; P25103; -. DR EMDB; EMD-13140; -. DR EMDB; EMD-13141; -. DR EMDB; EMD-24569; -. DR EMDB; EMD-24570; -. DR EMDB; EMD-24572; -. DR EMDB; EMD-41840; -. DR MDposit; P25103; -. DR MDRepo; P25103; -. DR SMR; P25103; -. DR BioGRID; 112732; 73. DR CORUM; P25103; -. DR FunCoup; P25103; 720. DR IntAct; P25103; 69. DR NDEx; IQUERY-CP-TACR1; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000303522; -. DR BindingDB; P25103; -. DR ChEMBL; CHEMBL249; -. DR DrugBank; DB00673; Aprepitant. DR DrugBank; DB05072; AV608. DR DrugBank; DB21149; Befetupitant. DR DrugBank; DB20607; Burapitant. DR DrugBank; DB06634; Casopitant. DR DrugBank; DB05421; CP-122721. DR DrugBank; DB16744; CP-96345. DR DrugBank; DB20991; Dapitant. DR DrugBank; DB18968; Elinzanetant. DR DrugBank; DB12122; Figopitant. DR DrugBank; DB06717; Fosaprepitant. DR DrugBank; DB14019; Fosnetupitant. DR DrugBank; DB01221; Ketamine. DR DrugBank; DB19599; Lanepitant. DR DrugBank; DB09048; Netupitant. DR DrugBank; DB12427; Orvepitant. DR DrugBank; DB04029; Phenylalanylamide. DR DrugBank; DB05466; R673. DR DrugBank; DB09291; Rolapitant. DR DrugBank; DB16742; RP-67580. DR DrugBank; DB05875; Sar9, Met (O2)11-Substance P. DR DrugBank; DB01037; Selegiline. DR DrugBank; DB12973; Serlopitant. DR DrugBank; DB05790; SR 140333. DR DrugBank; DB19198; Substance P. DR DrugBank; DB12580; Tradipitant. DR DrugBank; DB00193; Tramadol. DR DrugBank; DB04894; Vapreotide. DR DrugBank; DB11949; Vestipitant. DR DrugBank; DB12436; Vofopitant. DR DrugCentral; P25103; -. DR GuidetoPHARMACOLOGY; 360; -. DR GlyCosmos; P25103; 3 sites, No reported glycans. DR GlyGen; P25103; 3 sites. DR iPTMnet; P25103; -. DR PhosphoSitePlus; P25103; -. DR BioMuta; TACR1; -. DR DMDM; 128359; -. DR MassIVE; P25103; -. DR PaxDb; 9606-ENSP00000303522; -. DR PeptideAtlas; P25103; -. DR ProteomicsDB; 54260; -. [P25103-1] DR ABCD; P25103; 1 sequenced antibody. DR Antibodypedia; 16803; 645 antibodies from 44 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 AGR; HGNC:11526; -. DR ClinPGx; PA36302; -. DR CTD; 6869; -. DR DisGeNET; 6869; -. DR GeneCards; TACR1; -. DR HGNC; HGNC:11526; TACR1. DR HPA; ENSG00000115353; Tissue enhanced (adipose). DR MalaCards; TACR1; -. DR MIM; 162323; gene. DR OpenTargets; ENSG00000115353; -. DR VEuPathDB; HostDB:ENSG00000115353; -. DR eggNOG; KOG4219; Eukaryota. DR GeneTree; ENSGT00940000153745; -. DR HOGENOM; CLU_009579_6_1_1; -. DR InParanoid; P25103; -. DR OMA; AAHGKYA; -. DR OrthoDB; 5981855at2759; -. DR PAN-GO; P25103; 4 GO annotations based on evolutionary models. DR PhylomeDB; P25103; -. 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 Agora; ENSG00000115353; -. DR BioGRID-ORCS; 6869; 13 hits in 1156 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 male germ line stem cell (sensu Vertebrata) in testis and 127 other cell types or tissues. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0004995; F:tachykinin receptor activity; TAS:ProtInc. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProt. 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:0007209; P:phospholipase C-activating tachykinin receptor signaling pathway; IDA:UniProt. 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: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: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: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 CDD; cd16002; 7tmA_NK1R; 1. DR FunFam; 1.20.1070.10:FF:000078; Neuromedin-K receptor; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR001681; Neurokn_rcpt. DR InterPro; IPR000046; NK1_rcpt. DR PANTHER; PTHR46925; G-PROTEIN COUPLED RECEPTOR TKR-1-RELATED; 1. DR PANTHER; PTHR46925:SF4; SUBSTANCE-P RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01024; NEUROKININ1R. DR PRINTS; PR00244; NEUROKININR. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. 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 Endosome; G protein-coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Proteomics identification; Receptor; Reference proteome; KW Transducer; Transmembrane; 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 376..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 140..143 FT /evidence="ECO:0007829|PDB:8U26" FT HELIX 144..168 FT /evidence="ECO:0007829|PDB:6HLP" FT STRAND 169..182 FT /evidence="ECO:0007829|PDB:6HLP" FT HELIX 191..201 FT /evidence="ECO:0007829|PDB:6HLP" FT HELIX 202..206 FT /evidence="ECO:0007829|PDB:6HLP" FT HELIX 207..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 HELIX 275..279 FT /evidence="ECO:0007829|PDB:8U26" 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 //