ID   MPI5_LYMST              Reviewed;         138 AA.
AC   P31241;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Molluscan insulin-related peptide 5;
DE   AltName: Full=MIP V;
DE   Contains:
DE     RecName: Full=Molluscan insulin-related peptide 5 B chain;
DE   Contains:
DE     RecName: Full=Molluscan insulin-related peptide 5 A chain;
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 [MRNA].
RC   TISSUE=CNS;
RX   PubMed=1323019; DOI=10.1016/0169-328x(92)90003-t;
RA   Smit A.B., Thijsen S.F.T., Geraerts W.P.M., Meester I., Heerikhuizen H.,
RA   Joosse J.;
RT   "Characterization of a cDNA clone encoding molluscan insulin-related
RT   peptide V of Lymnaea stagnalis.";
RL   Brain Res. Mol. Brain Res. 14:7-12(1992).
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC       Note=Secretory granules.
CC   -!- TISSUE SPECIFICITY: Expressed in the cerebral light-green cells which
CC       are giant neuroendocrines cells involved in the control of growth.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; X59302; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A43957; A43957.
DR   AlphaFoldDB; P31241; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR016724; Insulin-rel_pep.
DR   InterPro; IPR022353; Insulin_CS.
DR   Pfam; PF00049; Insulin; 1.
DR   PIRSF; PIRSF018431; Molluscan_insulin_rel_peptide; 1.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle; Disulfide bond;
KW   Pyrrolidone carboxylic acid; Signal.
FT   SIGNAL          1..31
FT   PEPTIDE         32..69
FT                   /note="Molluscan insulin-related peptide 5 B chain"
FT                   /id="PRO_0000015949"
FT   PROPEP          72..84
FT                   /note="C-beta peptide like"
FT                   /id="PRO_0000015950"
FT   PROPEP          87..111
FT                   /note="C-alpha peptide like"
FT                   /id="PRO_0000015951"
FT   PEPTIDE         114..138
FT                   /note="Molluscan insulin-related peptide 5 A chain"
FT                   /id="PRO_0000015952"
FT   MOD_RES         32
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         114
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..124
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..137
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..128
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15540 MW;  9EF1921B84A9D6CA CRC64;
     MAGVRLVFTK AFMVTVLLTL LLNIGVKPAE GQFSACSFSS RPHPRGICGS DLADLRAFIC
     SRRNQPAMVK RDAETGWLLP ETMVKRNAQT DLDDPLRNIK LSSESALTYL TKRQRTTNLV
     CECCYNVCTV DVFYEYCY