ID   TKN1_MESAU              Reviewed;         130 AA.
AC   Q60541; P49110;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Protachykinin-1;
DE   AltName: Full=PPT;
DE   Contains:
DE     RecName: Full=Substance P;
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   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA).
RC   STRAIN=Aura; TISSUE=Brain;
RA   Heitland A., Kruhoffer M., Juergen Maegert H.J., Forssmann W.-G.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Beta;
CC         IsoId=Q60541-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=Q60541-3; Sequence=Not described;
CC       Name=Gamma;
CC         IsoId=Q60541-2; Sequence=VSP_006378;
CC       Name=Delta;
CC         IsoId=Q60541-4; Sequence=Not described;
CC   -!- PTM: [Substance P]: The substance P form is cleaved at Pro-59 by the
CC       prolyl endopeptidase FAP (seprase) activity (in vitro). Substance P is
CC       also cleaved and degraded by Angiotensin-converting enzyme (ACE) and
CC       neprilysin (MME). {ECO:0000250|UniProtKB:P20366}.
CC   -!- SIMILARITY: Belongs to the tachykinin family. {ECO:0000305}.
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DR   EMBL; X80662; CAA56691.1; -; mRNA.
DR   EMBL; X80663; CAA56692.1; -; mRNA.
DR   PIR; S47038; S47038.
DR   PIR; S47039; S47039.
DR   AlphaFoldDB; Q60541; -.
DR   STRING; 10036.XP_005082986.1; -.
DR   eggNOG; ENOG502S1KJ; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0007217; P:tachykinin receptor signaling pathway; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Alternative splicing; Amidation; Cleavage on pair of basic residues;
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_0000033536"
FT   PEPTIDE         58..68
FT                   /note="Substance P"
FT                   /id="PRO_0000033537"
FT   PEPTIDE         72..107
FT                   /note="Neuropeptide K"
FT                   /id="PRO_0000033538"
FT   PEPTIDE         72..73
FT                   /note="Neuropeptide gamma, 1st part"
FT                   /id="PRO_0000033539"
FT   PEPTIDE         89..107
FT                   /note="Neuropeptide gamma, 2nd part"
FT                   /id="PRO_0000033540"
FT   PEPTIDE         98..107
FT                   /note="Neurokinin A"
FT                   /id="PRO_0000033541"
FT   PEPTIDE         111..126
FT                   /note="C-terminal-flanking peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033542"
FT   SITE            59..60
FT                   /note="Cleavage; by FAP"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            63..64
FT                   /note="Cleavage; by MME"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            64..65
FT                   /note="Cleavage; by MME"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            65..66
FT                   /note="Cleavage; by ACE"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            66..67
FT                   /note="Cleavage; by ACE and MME"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   MOD_RES         68
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   MOD_RES         107
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   VAR_SEQ         74..88
FT                   /note="Missing (in isoform Gamma)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_006378"
SQ   SEQUENCE   130 AA;  14907 MW;  CC92E9371A646F2E CRC64;
     MKILVAVAVF FLVSTQLSAE EIGANDDLNY WSDWSDSDQI KEALPEPFEH ILQRIARRPK
     PQQFFGLMGK RDADSSIEKQ VALLKALYGH GQISHKRHKT DSFVGLMGKR ALNSVAFERS
     AMQNYERRRK