ID   SCHS_LYMST              Reviewed;          79 AA.
AC   P24471;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Schistosomin;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=CNS;
RX   PubMed=1953679; DOI=10.1042/bj2790837;
RA   Hordijk P.L., Schallig H.D.F.H., Ebberink R.H.M., de Jong-Brink M.,
RA   Joosse J.;
RT   "Primary structure and origin of schistosomin, an anti-gonadotropic
RT   neuropeptide of the pond snail Lymnaea stagnalis.";
RL   Biochem. J. 279:837-842(1991).
CC   -!- FUNCTION: Anti-gonadotropic neuropeptide. It also decreases the binding
CC       capacity of calfluxin to membrane-bound receptors of the albumen gland.
CC       This leads to inhibition of the reproductive activities of the infected
CC       snail.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Growth-controlling neurosecretory light green
CC       cells, in the cerebral ganglia of the CNS.
CC   -!- INDUCTION: Its release and/or synthesis is stimulated during parasitic
CC       infection.
CC   -!- PTM: Contains four disulfide bonds. {ECO:0000305}.
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DR   PIR; S19274; S19274.
DR   AlphaFoldDB; P24471; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   CHAIN           1..79
FT                   /note="Schistosomin"
FT                   /id="PRO_0000097625"
SQ   SEQUENCE   79 AA;  8745 MW;  441ACA5A7F9BEF87 CRC64;
     DNYWCPQSGE AFECFESDPN AKFCLNSGKT SVVICSKCRK KYEFCRNGLK VSKRPDYDCG
     AGWESTPCTG DNSAVPAVF