ID   MPI7_LYMST              Reviewed;         180 AA.
AC   P91797;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Molluscan insulin-related peptide 7;
DE   AltName: Full=MIP VII;
DE   Contains:
DE     RecName: Full=Molluscan insulin-related peptide 7 B chain;
DE   Contains:
DE     RecName: Full=Molluscan insulin-related peptide 7 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=8848162; DOI=10.1016/0306-4522(95)00378-9;
RA   Smit A.B., Spijker S., van Minnen J., Burke J.F., de Winter F., Elk R.,
RA   Geraerts W.P.M.;
RT   "Expression and characterization of molluscan insulin-related peptide VII
RT   from the mollusc Lymnaea stagnalis.";
RL   Neuroscience 70:589-596(1996).
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   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; S82894; AAB46831.1; -; mRNA.
DR   AlphaFoldDB; P91797; -.
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..25
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         26..67
FT                   /note="Molluscan insulin-related peptide 7 B chain"
FT                   /id="PRO_0000015953"
FT   PROPEP          71..152
FT                   /note="C peptide like"
FT                   /id="PRO_0000015954"
FT   PEPTIDE         155..180
FT                   /note="Molluscan insulin-related peptide 7 A chain"
FT                   /id="PRO_0000015955"
FT   MOD_RES         26
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..167
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..180
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..171
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  20214 MW;  89BF903FA38F0DAA CRC64;
     MNASVESCLT FTFVLVALCV GLTIGQQVNT CTMFSRQHPR GLCGNRLARA HANLCFLLRN
     TYPDIFPRKR SVDNTFEKVY SIPLSVLAEL DLSDDDWGAY VSKKDIPYRS ETNGLSGANF
     ESSAFDKQLE LPAMKSTTSQ LFRILKLRGS RLKREVMAEP SLVCDCCYNE CSVRKLATYC