ID   TKN1_TORMA              Reviewed;          16 AA.
AC   Q7LZ48;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Des[Ser(1)Pro(2)] scyliorhinin-2;
DE   AltName: Full=Des[Ser(1)Pro(2)] scyliorhinin II;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT MET-16.
RC   TISSUE=Intestine;
RX   PubMed=2847952; DOI=10.1016/0016-6480(88)90266-3;
RA   Conlon J.M., Thim L.;
RT   "Isolation of the tachykinin, des[Ser1Pro2]scyliorhinin II from the
RT   intestine of the ray, Torpedo marmorata.";
RL   Gen. Comp. Endocrinol. 71:383-388(1988).
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   -!- SIMILARITY: Belongs to the tachykinin family. {ECO:0000305}.
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DR   PIR; A60839; A60839.
DR   AlphaFoldDB; Q7LZ48; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013055; Tachy_Neuro_lke_CS.
DR   PROSITE; PS00267; TACHYKININ; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Neuropeptide; Secreted.
FT   PEPTIDE         1..16
FT                   /note="Des[Ser(1)Pro(2)] scyliorhinin-2"
FT                   /id="PRO_0000044412"
FT   MOD_RES         16
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|PubMed:2847952"
SQ   SEQUENCE   16 AA;  1670 MW;  97C839201E2F3907 CRC64;
     SNSKCPDGPD CFVGLM