ID   OVUH_LYMST              Reviewed;         259 AA.
AC   P06308; P20055;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Ovulation prohormone;
DE   Contains:
DE     RecName: Full=Beta-3-CDCP;
DE   Contains:
DE     RecName: Full=Beta-2-CDCP;
DE   Contains:
DE     RecName: Full=Beta-1-CDCP;
DE   Contains:
DE     RecName: Full=Calfluxin;
DE   Contains:
DE     RecName: Full=Alpha-CDCP;
DE   Contains:
DE     RecName: Full=Ovulation hormone;
DE     AltName: Full=Cerebral neurosecretory caudodorsal cell hormone;
DE              Short=CDCH;
DE   Contains:
DE     RecName: Full=X-CDCP;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE.
RX   PubMed=3183719; DOI=10.1523/jneurosci.08-11-04184.1988;
RA   Vreugdenhil E., Jackson J.F., Bouwmeester T., Smit A.B., van Minnen J.,
RA   van Heerikhuizen H., Klootwijk J., Joosse J.;
RT   "Isolation, characterization, and evolutionary aspects of a cDNA clone
RT   encoding multiple neuropeptides involved in the stereotyped egg-laying
RT   behavior of the freshwater snail Lymnaea stagnalis.";
RL   J. Neurosci. 8:4184-4191(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 198-233, AND AMIDATION AT LEU-233.
RX   PubMed=16578788; DOI=10.1073/pnas.82.22.7767;
RA   Ebberink R.H.M., van Loenhout H., Geraerts W.P.M., Joosse J.;
RT   "Purification and amino acid sequence of the ovulation neurohormone of
RT   Lymnaea stagnalis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7767-7771(1985).
CC   -!- FUNCTION: CDCH induces ovulation and egg-mass production; it may also
CC       stimulate synthesis of secretory products in the female accessory sex
CC       glands and affect neurons in the neuronal circuits controlling
CC       locomotion and feeding.
CC   -!- FUNCTION: Calfluxin is involved in the influx of calcium into
CC       mitochondria of the albumen gland.
CC   -!- FUNCTION: CDCA (or alpha-CDCP) triggers the electrical activity of the
CC       caudodorsal cells (CDCS).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the molluscan ELH family. {ECO:0000305}.
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DR   PIR; A34946; ONGAOL.
DR   AlphaFoldDB; P06308; -.
DR   PRIDE; P06308; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR003424; ELH.
DR   Pfam; PF02323; ELH; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Hormone; Neuropeptide; Repeat; Secreted; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..102
FT                   /id="PRO_0000001914"
FT   PEPTIDE         105..109
FT                   /note="Beta-3-CDCP"
FT                   /id="PRO_0000001915"
FT   PEPTIDE         112..116
FT                   /note="Beta-2-CDCP"
FT                   /id="PRO_0000001916"
FT   PEPTIDE         119..123
FT                   /note="Beta-1-CDCP"
FT                   /id="PRO_0000001917"
FT   PEPTIDE         126..139
FT                   /note="Calfluxin"
FT                   /id="PRO_0000001918"
FT   PEPTIDE         144..152
FT                   /note="Alpha-CDCP"
FT                   /id="PRO_0000001919"
FT   PEPTIDE         156..178
FT                   /note="X-CDCP"
FT                   /id="PRO_0000001920"
FT   PROPEP          181..195
FT                   /id="PRO_0000001921"
FT   PEPTIDE         198..233
FT                   /note="Ovulation hormone"
FT                   /id="PRO_0000001922"
FT   PROPEP          237..259
FT                   /id="PRO_0000001923"
FT   REPEAT          119..123
FT   REPEAT          146..150
FT   REGION          42..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..150
FT                   /note="2 X 5 AA repeats of R-L-R-F-H"
FT   REGION          149..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         233
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:16578788"
FT   CONFLICT        217
FT                   /note="K -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   259 AA;  29613 MW;  6EF26D5A29ADC4FE CRC64;
     MKMSGLLSKP DYGVVGIVFT VVFCCWCSSS TTHALSIAEP GRDRYDKRSP TGHGVEVVES
     GEDYGSNRPQ PVYGDEDEED SADVYVGSDE SSSGEKTRLT AAKRRLRFNK RRLRASKRRL
     RFHKRRVDSA DESNDDGFDR KAREPRLRFH DVRKRSATAE EGSENAEIEE SHLGNSRSRR
     SAGSAPSSAN EVQRSKRLSI TNDLRAIADS YLYDQHKLRE RQEENLRRRF LELGKRGSAF
     FDHIPIIFGE PQYDYQPFK