ID   TKNA_HORSE              Reviewed;          11 AA.
AC   P67933; P01290;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Substance P;
GN   Name=TAC1; Synonyms=NKA, NKNA, TAC2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT MET-11.
RA   Studer R.O., Trzeciak A., Lergier W.;
RT   "Isolation and amino-acid sequence of substance P from horse intestine.";
RL   Helv. Chim. Acta 56:860-866(1973).
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   -!- PTM: [Substance P]: The substance P form is cleaved at Pro-2 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   PIR; A01558; SPHO.
DR   Proteomes; UP000002281; 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   Pfam; PF02202; Tachykinin; 1.
DR   PROSITE; PS00267; TACHYKININ; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Neuropeptide; Neurotransmitter;
KW   Reference proteome; Secreted.
FT   PEPTIDE         1..11
FT                   /note="Substance P"
FT                   /id="PRO_0000044420"
FT   SITE            2..3
FT                   /note="Cleavage; by FAP"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            6..7
FT                   /note="Cleavage; by MME"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            7..8
FT                   /note="Cleavage; by MME"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            8..9
FT                   /note="Cleavage; by ACE"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   SITE            9..10
FT                   /note="Cleavage; by ACE and MME"
FT                   /evidence="ECO:0000250|UniProtKB:P20366"
FT   MOD_RES         11
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   11 AA;  1349 MW;  3E757FE3C9D6C6C7 CRC64;
     RPKPQQFFGL M