MPI2_LYMST
ID MPI2_LYMST Reviewed; 137 AA.
AC P25289;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Molluscan insulin-related peptide 2;
DE AltName: Full=MIP II;
DE Contains:
DE RecName: Full=Molluscan insulin-related peptide 2 B chain;
DE Contains:
DE RecName: Full=Molluscan insulin-related peptide 2 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=1868853; DOI=10.1111/j.1432-1033.1991.tb16173.x;
RA Smit A.B., Geraerts W.P.M., Meester I., van Heerikhuizen H., Joosse J.;
RT "Characterization of a cDNA clone encoding molluscan insulin-related
RT peptide II of Lymnaea stagnalis.";
RL Eur. J. Biochem. 199:699-703(1991).
RN [2]
RP PROTEIN SEQUENCE OF 32-66 AND 113-137, AND PYROGLUTAMATE FORMATION AT
RP GLN-32 AND GLN-113.
RC TISSUE=Light-green cell;
RX PubMed=1350761; DOI=10.1210/endo.130.6.1350761;
RA Li K.-W., Geraerts W.P.M., Joosse J.;
RT "Purification and sequencing of molluscan insulin-related peptide II from
RT the neuroendocrine light green cells in Lymnaea stagnalis.";
RL Endocrinology 130:3427-3432(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; CAA41989.1; -; mRNA.
DR PIR; S17195; S17195.
DR AlphaFoldDB; P25289; -.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Pyrrolidone carboxylic acid;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:1350761"
FT PEPTIDE 32..68
FT /note="Molluscan insulin-related peptide 2 B chain"
FT /id="PRO_0000015941"
FT PROPEP 71..83
FT /note="C-beta peptide like"
FT /id="PRO_0000015942"
FT PROPEP 86..110
FT /note="C-alpha peptide like"
FT /id="PRO_0000015943"
FT PEPTIDE 113..137
FT /note="Molluscan insulin-related peptide 2 A chain"
FT /id="PRO_0000015944"
FT MOD_RES 32
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1350761"
FT MOD_RES 113
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1350761"
FT DISULFID 47..123
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 59..136
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 122..127
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 15257 MW; B9E56409D1EECB41 CRC64;
MVGVRLVFTN AFVVTVLLTL LLDVVVKPAE GQSSCSLSSR PHPRGICGSN LAGFRAFICS
NQNSPSMVKR DAETGWLLPE TMVKRNAETD LDDPLRNIKL SSESALTYLT KRQRTTNLVC
ECCFNYCTPD VVRKYCY
