TKN1_RABIT
ID TKN1_RABIT Reviewed; 115 AA.
AC P41540;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 gamma;
DE Contains:
DE RecName: Full=C-terminal-flanking peptide;
DE Flags: Precursor;
GN Name=TAC1; Synonyms=NKA, NKNA, TAC2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8363593; DOI=10.1006/bbrc.1993.2019;
RA Maegert H.-J., Heitland A., Rose M., Forssmann W.-G.;
RT "Nucleotide sequence of the rabbit gamma-preprotachykinin I cDNA.";
RL Biochem. Biophys. Res. Commun. 195:128-131(1993).
RN [2]
RP PROTEIN SEQUENCE OF 72-92, AND AMIDATION AT MET-92.
RA Kage R., McGregor G.P., Thim L., Conlon J.M.;
RT "Gamma-neuropeptide K: a peptide isolated from rabbit gut that is derived
RT from gamma-preprotachykinin.";
RL Regul. Pept. 18:346-346(1987).
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=P41540-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=P41540-2; Sequence=Not described;
CC Name=Gamma;
CC IsoId=P41540-4; Sequence=Not described;
CC Name=Delta;
CC IsoId=P41540-3; 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; X62994; CAA44728.1; -; mRNA.
DR PIR; JN0709; SPRBG.
DR RefSeq; NP_001095168.1; NM_001101698.1. [P41540-1]
DR PDB; 2MCE; NMR; -; A=72-92.
DR PDBsum; 2MCE; -.
DR AlphaFoldDB; P41540; -.
DR BMRB; P41540; -.
DR SMR; P41540; -.
DR GeneID; 100009275; -.
DR KEGG; ocu:100009275; -.
DR CTD; 6863; -.
DR InParanoid; P41540; -.
DR Proteomes; UP000001811; 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 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_0000033557"
FT PEPTIDE 58..68
FT /note="Substance P"
FT /id="PRO_0000033558"
FT PEPTIDE 72..92
FT /note="Neuropeptide gamma"
FT /id="PRO_0000033559"
FT PEPTIDE 83..92
FT /note="Neurokinin A"
FT /id="PRO_0000033560"
FT PEPTIDE 96..111
FT /note="C-terminal-flanking peptide"
FT /id="PRO_0000033561"
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 92
FT /note="Methionine amide"
FT /evidence="ECO:0000269|Ref.2"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2MCE"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2MCE"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:2MCE"
SQ SEQUENCE 115 AA; 13370 MW; 5EC76F7C9B10E1C6 CRC64;
MKILVALAVL ALVSTQLFAE DIRANDDLNY WSDWSDSDQI KEELPEPFEH LLQRIARRPK
PQQFFGLMGK RDAGHGQISH KRHKTDSFVG LMGKRALNSV AYERSAMQNY ERRRK
