TKNA_CAVPO
ID TKNA_CAVPO Reviewed; 11 AA.
AC P67932; P01290;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Substance P;
GN Name=TAC1; Synonyms=NKA, NKNA, TAC2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE, AND AMIDATION AT MET-11.
RC TISSUE=Small intestine;
RX PubMed=2478925; DOI=10.1016/0143-4179(89)90066-8;
RA Murphy R.;
RT "Primary amino acid sequence of guinea-pig substance P.";
RL Neuropeptides 14:105-110(1989).
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; A60654; A60654.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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_0000044419"
FT SITE 2..3
FT /note="Cleavage; b2y 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|PubMed:2478925"
SQ SEQUENCE 11 AA; 1349 MW; 3E757FE3C9D6C6C7 CRC64;
RPKPQQFFGL M