ID   MPI3_LYMST              Reviewed;         122 AA.
AC   P80090;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Molluscan insulin-related peptide 3;
DE   AltName: Full=MIP III;
DE   Contains:
DE     RecName: Full=Molluscan insulin-related peptide 3 B chain;
DE   Contains:
DE     RecName: Full=Molluscan insulin-related peptide 3 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 [GENOMIC DNA].
RX   PubMed=8240668; DOI=10.1677/jme.0.0110103;
RA   Smit A.B., van Marle A., van Elk R., Bogerd J., van Heerikhuizen H.,
RA   Geraerts W.P.M.;
RT   "Evolutionary conservation of the insulin gene structure in invertebrates:
RT   cloning of the gene encoding molluscan insulin-related peptide III from
RT   Lymnaea stagnalis.";
RL   J. Mol. Endocrinol. 11:103-113(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 30-66 AND 99-122.
RC   TISSUE=Light-green cell;
RX   PubMed=1572366; DOI=10.1111/j.1432-1033.1992.tb16828.x;
RA   Li K.-W., Geraerts W.P.M.;
RT   "Isolation and chemical characterization of a novel insulin-related
RT   neuropeptide from the freshwater snail, Lymnaea stagnalis.";
RL   Eur. J. Biochem. 205:675-678(1992).
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain; disulfide-linked
CC       (doubly).
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}.
CC   -!- CAUTION: PubMed:1572366 reported the formation of pyroglutamic acid by
CC       the N-terminal glutamic acid and of gamma-ethyl glutamate in peptide A.
CC       This is most probably an artifact of isolation. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S69155; AAB28954.1; -; Genomic_DNA.
DR   EMBL; S69104; AAB28954.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; P80090; -.
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   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PIRSF; PIRSF018431; Molluscan_insulin_rel_peptide; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Direct protein sequencing; Disulfide bond; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:1572366"
FT   PEPTIDE         30..66
FT                   /note="Molluscan insulin-related peptide 3 B chain"
FT                   /id="PRO_0000015945"
FT   PROPEP          71..87
FT                   /note="C-beta peptide like"
FT                   /id="PRO_0000015946"
FT   PROPEP          91..96
FT                   /note="C-alpha peptide like"
FT                   /id="PRO_0000015947"
FT   PEPTIDE         99..122
FT                   /note="Molluscan insulin-related peptide 3 A chain"
FT                   /id="PRO_0000015948"
FT   DISULFID        47..109
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        59..122
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        108..113
SQ   SEQUENCE   122 AA;  13669 MW;  17D4CCE479D393B4 CRC64;
     MASVHLTLTK AFMVTVFLTL LLNVSITRGT TQHTCSILSR PHPRGLCGST LANMVQWLCS
     TYTTSSKVKR QAEPDEEDDA MSKIMISKKR ALSYLTKRES RPSIVCECCF NQCTVQELLA
     YC