TKN1_HUMAN
ID TKN1_HUMAN Reviewed; 129 AA.
AC P20366; O60600; O60601; Q00072; Q53GH4; Q549V0; Q549V1; Q549V2; Q6FHM1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Protachykinin-1;
DE AltName: Full=PPT;
DE Contains:
DE RecName: Full=Substance P {ECO:0000303|PubMed:6208535};
DE Contains:
DE RecName: Full=Neurokinin A;
DE Short=NKA;
DE AltName: Full=Neuromedin L;
DE AltName: Full=Substance K;
DE Contains:
DE RecName: Full=Neuropeptide K;
DE Short=NPK;
DE Contains:
DE RecName: Full=Neuropeptide gamma;
DE Contains:
DE RecName: Full=C-terminal-flanking peptide;
DE Flags: Precursor;
GN Name=TAC1; Synonyms=NKA, NKNA, TAC2;
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 BETA), AND AMIDATION AT MET-68 AND
RP MET-107.
RX PubMed=3770210; DOI=10.1016/0014-5793(86)81534-4;
RA Harmar A.J., Armstrong A., Pascall J.C., Chapman K., Rosie R., Curtis A.,
RA Going J., Edwards C.R.W., Fink G.;
RT "cDNA sequence of human beta-preprotachykinin, the common precursor to
RT substance P and neurokinin A.";
RL FEBS Lett. 208:67-72(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC TISSUE=Brain;
RA Tan A., Too H.P.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-122 (ISOFORMS BETA AND GAMMA).
RC TISSUE=Testis;
RX PubMed=1708336; DOI=10.1210/endo-128-5-2441;
RA Chiwakata C., Brackmann B., Hunt N., Davidoff M., Schulze W., Ivell R.;
RT "Tachykinin (substance-P) gene expression in Leydig cells of the human and
RT mouse testis.";
RL Endocrinology 128:2441-2448(1991).
RN [10]
RP PROTEIN SEQUENCE OF 98-107, AND AMIDATION AT MET-107.
RX PubMed=3038549; DOI=10.1111/j.1432-1033.1987.tb13567.x;
RA Theodorsson-Norheim E., Joernvall H., Andersson M., Norheim I., Oeberg K.,
RA Jacobsson G.;
RT "Isolation and characterization of neurokinin A, neurokinin A(3-10) and
RT neurokinin A(4-10) from a neutral water extract of a metastatic ileal
RT carcinoid tumour.";
RL Eur. J. Biochem. 166:693-697(1987).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-122 (ISOFORMS ALPHA; BETA AND DELTA).
RC TISSUE=Blood, and Brain;
RX PubMed=9846828; DOI=10.1016/s0165-5728(98)00170-2;
RA Lai J.P., Douglas S.D., Rappaport E., Wu J.M., Ho W.Z.;
RT "Identification of a delta isoform of preprotachykinin mRNA in human
RT mononuclear phagocytes and lymphocytes.";
RL J. Neuroimmunol. 91:121-128(1998).
RN [12]
RP PROTEIN SEQUENCE OF 111-126.
RC TISSUE=Adrenal medulla;
RX PubMed=2284201; DOI=10.1016/0196-9781(90)90007-r;
RA McGregor G.P., Conlon J.M.;
RT "Characterization of the C-terminal flanking peptide of human beta-
RT preprotachykinin.";
RL Peptides 11:907-910(1990).
RN [13]
RP CLEAVAGE BY ACE AND MME.
RX PubMed=6208535; DOI=10.1016/0196-9781(84)90020-2;
RA Skidgel R.A., Engelbrecht S., Johnson A.R., Erdoes E.G.;
RT "Hydrolysis of substance p and neurotensin by converting enzyme and neutral
RT endopeptidase.";
RL Peptides 5:769-776(1984).
RN [14]
RP CLEAVAGE BY FAP, AND CLEAVAGE SITE.
RX PubMed=21314817; DOI=10.1111/j.1742-4658.2011.08051.x;
RA Keane F.M., Nadvi N.A., Yao T.W., Gorrell M.D.;
RT "Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are
RT novel substrates of fibroblast activation protein-alpha.";
RL FEBS J. 278:1316-1332(2011).
RN [15]
RP STRUCTURE BY NMR OF 72-107.
RX PubMed=16503654; DOI=10.1021/bi052287o;
RA Dike A., Cowsik S.M.;
RT "Three-dimensional structure of neuropeptide K bound to
RT dodecylphosphocholine micelles.";
RL Biochemistry 45:2994-3004(2006).
CC -!- FUNCTION: Tachykinins are active peptides which excite neurons, evoke
CC behavioral responses, are potent vasodilators and secretagogues, and
CC contract (directly or indirectly) many smooth muscles.
CC -!- INTERACTION:
CC PRO_0000033530; P25103: TACR1; NbExp=2; IntAct=EBI-6655360, EBI-6655287;
CC PRO_0000033534; P21452: TACR2; NbExp=2; IntAct=EBI-6655449, EBI-6655413;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Beta;
CC IsoId=P20366-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=P20366-2; Sequence=VSP_006376, VSP_006377;
CC Name=Gamma;
CC IsoId=P20366-3; Sequence=VSP_006375;
CC Name=Delta;
CC IsoId=P20366-4; Sequence=VSP_006375, VSP_006376, VSP_006377;
CC -!- PTM: [Substance P]: The substance P form is cleaved at Pro-59 by the
CC prolyl endopeptidase FAP (seprase) activity (in vitro)
CC (PubMed:21314817). Substance P is also cleaved and degraded by
CC Angiotensin-converting enzyme (ACE) and neprilysin (MME)
CC (PubMed:6208535). {ECO:0000269|PubMed:21314817,
CC ECO:0000269|PubMed:6208535}.
CC -!- SIMILARITY: Belongs to the tachykinin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Neurokinin-1 entry;
CC URL="https://en.wikipedia.org/wiki/Neurokinin_1";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TAC1ID44483ch7q21.html";
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DR EMBL; X54469; CAA38351.1; -; mRNA.
DR EMBL; U37529; AAA79195.1; -; mRNA.
DR EMBL; CR407602; CAG28529.1; -; mRNA.
DR EMBL; CR541730; CAG46531.1; -; mRNA.
DR EMBL; AK222957; BAD96677.1; -; mRNA.
DR EMBL; AC004140; AAQ96888.1; -; Genomic_DNA.
DR EMBL; AC004140; AAQ96889.1; -; Genomic_DNA.
DR EMBL; AC004140; AAQ96890.1; -; Genomic_DNA.
DR EMBL; AC004140; AAQ96891.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24116.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24117.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24118.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24119.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76734.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76735.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76736.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76737.1; -; Genomic_DNA.
DR EMBL; BC018047; AAH18047.1; -; mRNA.
DR EMBL; M68906; AAA60159.1; -; mRNA.
DR EMBL; M68907; AAA60160.1; -; mRNA.
DR EMBL; AF050655; AAC15701.1; -; mRNA.
DR EMBL; AF050656; AAC15702.1; -; mRNA.
DR EMBL; AF050658; AAC15704.1; -; mRNA.
DR CCDS; CCDS5649.1; -. [P20366-1]
DR CCDS; CCDS5650.1; -. [P20366-2]
DR CCDS; CCDS5651.1; -. [P20366-3]
DR PIR; A24805; SPHUB.
DR RefSeq; NP_003173.1; NM_003182.2. [P20366-1]
DR RefSeq; NP_054702.1; NM_013996.2. [P20366-2]
DR RefSeq; NP_054703.1; NM_013997.2. [P20366-3]
DR RefSeq; NP_054704.1; NM_013998.2. [P20366-4]
DR PDB; 2B19; NMR; -; A=72-107.
DR PDB; 2KS9; NMR; -; B=58-68.
DR PDB; 2KSA; NMR; -; B=58-68.
DR PDB; 2KSB; NMR; -; B=58-68.
DR PDB; 4HOM; X-ray; 1.90 A; B=58-68.
DR PDB; 7P02; EM; 2.87 A; P=58-68.
DR PDB; 7RMG; EM; 3.00 A; S=58-68.
DR PDB; 7RMH; EM; 3.10 A; S=58-68.
DR PDB; 7VDM; EM; 2.98 A; L=58-68.
DR PDBsum; 2B19; -.
DR PDBsum; 2KS9; -.
DR PDBsum; 2KSA; -.
DR PDBsum; 2KSB; -.
DR PDBsum; 4HOM; -.
DR PDBsum; 7P02; -.
DR PDBsum; 7RMG; -.
DR PDBsum; 7RMH; -.
DR PDBsum; 7VDM; -.
DR AlphaFoldDB; P20366; -.
DR SMR; P20366; -.
DR BioGRID; 112727; 7.
DR IntAct; P20366; 10.
DR MINT; P20366; -.
DR STRING; 9606.ENSP00000321106; -.
DR BindingDB; P20366; -.
DR PhosphoSitePlus; P20366; -.
DR BioMuta; TAC1; -.
DR DMDM; 135886; -.
DR MassIVE; P20366; -.
DR PaxDb; P20366; -.
DR PeptideAtlas; P20366; -.
DR PRIDE; P20366; -.
DR ProteomicsDB; 53754; -. [P20366-1]
DR ProteomicsDB; 53755; -. [P20366-2]
DR ProteomicsDB; 53756; -. [P20366-3]
DR ProteomicsDB; 53757; -. [P20366-4]
DR Antibodypedia; 2784; 626 antibodies from 39 providers.
DR DNASU; 6863; -.
DR Ensembl; ENST00000319273.10; ENSP00000321106.5; ENSG00000006128.12. [P20366-1]
DR Ensembl; ENST00000346867.4; ENSP00000289574.4; ENSG00000006128.12. [P20366-3]
DR Ensembl; ENST00000350485.8; ENSP00000289576.4; ENSG00000006128.12. [P20366-2]
DR GeneID; 6863; -.
DR KEGG; hsa:6863; -.
DR MANE-Select; ENST00000319273.10; ENSP00000321106.5; NM_003182.3; NP_003173.1.
DR UCSC; uc003uop.5; human. [P20366-1]
DR CTD; 6863; -.
DR DisGeNET; 6863; -.
DR GeneCards; TAC1; -.
DR HGNC; HGNC:11517; TAC1.
DR HPA; ENSG00000006128; Group enriched (brain, lymphoid tissue).
DR MIM; 162320; gene.
DR neXtProt; NX_P20366; -.
DR OpenTargets; ENSG00000006128; -.
DR PharmGKB; PA36297; -.
DR VEuPathDB; HostDB:ENSG00000006128; -.
DR eggNOG; ENOG502S1KJ; Eukaryota.
DR GeneTree; ENSGT00390000002457; -.
DR HOGENOM; CLU_149426_0_0_1; -.
DR InParanoid; P20366; -.
DR OMA; NQIQDDW; -.
DR OrthoDB; 1504814at2759; -.
DR PhylomeDB; P20366; -.
DR TreeFam; TF333405; -.
DR PathwayCommons; P20366; -.
DR Reactome; R-HSA-380095; Tachykinin receptors bind tachykinins.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P20366; -.
DR SIGNOR; P20366; -.
DR BioGRID-ORCS; 6863; 10 hits in 1061 CRISPR screens.
DR EvolutionaryTrace; P20366; -.
DR GeneWiki; TAC1; -.
DR GenomeRNAi; 6863; -.
DR Pharos; P20366; Tbio.
DR PRO; PR:P20366; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P20366; protein.
DR Bgee; ENSG00000006128; Expressed in dorsal root ganglion and 141 other tissues.
DR Genevisible; P20366; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0031836; F:neuromedin K receptor binding; IPI:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; IDA:UniProtKB.
DR GO; GO:0031837; F:substance K receptor binding; IPI:UniProtKB.
DR GO; GO:0031835; F:substance P receptor binding; IPI:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019732; P:antifungal humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0009582; P:detection of abiotic stimulus; TAS:ProtInc.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0007320; P:insemination; TAS:ProtInc.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IDA:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR GO; GO:0001878; P:response to yeast; IDA:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0007217; P:tachykinin receptor signaling pathway; IDA:UniProtKB.
DR InterPro; IPR013055; Tachy_Neuro_lke_CS.
DR InterPro; IPR008215; Tachykinin_dom.
DR InterPro; IPR008216; Tachykinin_fam.
DR Pfam; PF02202; Tachykinin; 1.
DR PRINTS; PR01829; PROTACHYKNIN.
DR SMART; SM00203; TK; 2.
DR PROSITE; PS00267; TACHYKININ; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amidation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Neurotransmitter; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..56
FT /evidence="ECO:0000255"
FT /id="PRO_0000033529"
FT PEPTIDE 58..68
FT /note="Substance P"
FT /id="PRO_0000033530"
FT PEPTIDE 72..107
FT /note="Neuropeptide K"
FT /id="PRO_0000033531"
FT PEPTIDE 72..73
FT /note="Neuropeptide gamma, 1st part"
FT /id="PRO_0000033532"
FT PEPTIDE 89..107
FT /note="Neuropeptide gamma, 2nd part"
FT /id="PRO_0000033533"
FT PEPTIDE 98..107
FT /note="Neurokinin A"
FT /id="PRO_0000033534"
FT PEPTIDE 111..126
FT /note="C-terminal-flanking peptide"
FT /id="PRO_0000033535"
FT SITE 59..60
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000269|PubMed:21314817"
FT SITE 63..64
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000269|PubMed:6208535"
FT SITE 64..65
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000269|PubMed:6208535"
FT SITE 65..66
FT /note="Cleavage; by ACE"
FT /evidence="ECO:0000269|PubMed:6208535"
FT SITE 66..67
FT /note="Cleavage; by ACE and MME"
FT /evidence="ECO:0000269|PubMed:6208535"
FT MOD_RES 68
FT /note="Methionine amide"
FT /evidence="ECO:0000269|PubMed:3770210"
FT MOD_RES 107
FT /note="Methionine amide"
FT /evidence="ECO:0000269|PubMed:3038549,
FT ECO:0000269|PubMed:3770210"
FT VAR_SEQ 74..88
FT /note="Missing (in isoform Gamma and isoform Delta)"
FT /evidence="ECO:0000303|PubMed:1708336,
FT ECO:0000303|PubMed:9846828"
FT /id="VSP_006375"
FT VAR_SEQ 97..114
FT /note="Missing (in isoform Alpha and isoform Delta)"
FT /evidence="ECO:0000303|PubMed:9846828"
FT /id="VSP_006376"
FT VAR_SEQ 115
FT /note="V -> M (in isoform Alpha and isoform Delta)"
FT /evidence="ECO:0000303|PubMed:9846828"
FT /id="VSP_006377"
FT CONFLICT 32
FT /note="S -> P (in Ref. 4; BAD96677)"
FT /evidence="ECO:0000305"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:2KSB"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2KS9"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2B19"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2B19"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2B19"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2B19"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2B19"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:2B19"
SQ SEQUENCE 129 AA; 15003 MW; 51412C1692368DE4 CRC64;
MKILVALAVF FLVSTQLFAE EIGANDDLNY WSDWYDSDQI KEELPEPFEH LLQRIARRPK
PQQFFGLMGK RDADSSIEKQ VALLKALYGH GQISHKRHKT DSFVGLMGKR ALNSVAYERS
AMQNYERRR
