ID   SOVO_SEPOF              Reviewed;          13 AA.
AC   P83567;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   07-OCT-2020, entry version 34.
DE   RecName: Full=SepOvotropin;
OS   Sepia officinalis (Common cuttlefish).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Sepia.
OX   NCBI_TaxID=6610 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   AMIDATION AT TYR-13.
RC   TISSUE=Ovarian follicle;
RX   PubMed=11027583; DOI=10.1006/bbrc.2000.3595;
RA   Zatylny C., Gagnon J., Boucaud-Camou E., Henry J.;
RT   "The SepOvotropin: a new ovarian peptide regulating oocyte transport in
RT   Sepia officinalis.";
RL   Biochem. Biophys. Res. Commun. 276:1013-1018(2000).
CC   -!- FUNCTION: Has myotropic activity targeting the genital tract.
CC       {ECO:0000269|PubMed:11027583}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Follicle, fully grown oocyte and egg.
CC       {ECO:0000269|PubMed:11027583}.
CC   -!- MASS SPECTROMETRY: Mass=1502.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11027583};
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..13
FT                   /note="SepOvotropin"
FT                   /id="PRO_0000044220"
FT   MOD_RES         13
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:11027583"
SQ   SEQUENCE   13 AA;  1503 MW;  483D5C7E34C72727 CRC64;
     PKDSMLLLQV PVY