SAPP_SEPOF
ID SAPP_SEPOF Reviewed; 6 AA.
AC P83569;
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=Sperm-attracting peptide SepSAP;
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, DEVELOPMENTAL STAGE, MASS SPECTROMETRY, AND
RP AMIDATION AT VAL-6.
RC TISSUE=Egg;
RX PubMed=12207899; DOI=10.1016/s0006-291x(02)02036-3;
RA Zatylny C., Marvin L., Gagnon J., Henry J.;
RT "Fertilization in Sepia officinalis: the first mollusk sperm-attracting
RT peptide.";
RL Biochem. Biophys. Res. Commun. 296:1186-1193(2002).
CC -!- FUNCTION: Attracts sperm increasing the chances of gamete collision.
CC {ECO:0000269|PubMed:12207899}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: First appears in the ovarian follicles furing
CC vitellogenesis. Accumulates in the oocytes before being secreted during
CC fertilization. Expression continues in the embedded oocyte. Accumulates
CC in the egg capsule after fertilization. {ECO:0000269|PubMed:12207899}.
CC -!- MASS SPECTROMETRY: Mass=596.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12207899};
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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..6
FT /note="Sperm-attracting peptide SepSAP"
FT /id="PRO_0000044216"
FT MOD_RES 6
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:12207899"
SQ SEQUENCE 6 AA; 597 MW; 72C8676AA0470000 CRC64;
PIDPGV