ID   INS_APLCA               Reviewed;         156 AA.
AC   Q9NDE7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin B chain';
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=PIN;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 79-93, PROTEOLYTIC
RP   PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=CNS;
RX   PubMed=10479677; DOI=10.1523/jneurosci.19-18-07732.1999;
RA   Floyd P.D., Li L., Rubakhin S.S., Sweedler J.V., Horn C.C., Kupfermann I.,
RA   Alexeeva V.Y., Ellis T.A., Dembrow N.C., Weiss K.R., Vilim F.S.;
RT   "Insulin prohormone processing, distribution, and relation to metabolism in
RT   Aplysia californica.";
RL   J. Neurosci. 19:7732-7741(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 141-156, GAMMA-CARBOXYGLUTAMATION AT GLU-152, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16522341; DOI=10.1016/j.neuint.2006.01.007;
RA   Jakubowski J.A., Hatcher N.G., Xie F., Sweedler J.V.;
RT   "The first gamma-carboxyglutamate-containing neuropeptide.";
RL   Neurochem. Int. 49:223-229(2006).
CC   -!- FUNCTION: Involved in glucose metabolism.
CC   -!- SUBUNIT: Heterodimer of a B chain or a B chain' and an A chain probably
CC       linked by three disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10479677}.
CC   -!- TISSUE SPECIFICITY: Expressed in the central region of the cerebral
CC       ganglia mostly within the F and C clusters.
CC       {ECO:0000269|PubMed:10479677}.
CC   -!- MASS SPECTROMETRY: [Insulin A chain]: Mass=4057.79; Mass_error=0.17;
CC       Method=MALDI; Note=Insulin A chain.;
CC       Evidence={ECO:0000269|PubMed:10479677};
CC   -!- MASS SPECTROMETRY: [Insulin B chain]: Mass=5093.74; Mass_error=0.14;
CC       Method=MALDI; Note=Insulin B chain.;
CC       Evidence={ECO:0000269|PubMed:10479677};
CC   -!- MASS SPECTROMETRY: [Insulin B chain']: Mass=4572; Method=MALDI;
CC       Note=Insulin B chain'.; Evidence={ECO:0000269|PubMed:10479677};
CC   -!- MASS SPECTROMETRY: Mass=9146.53; Mass_error=0.03; Method=MALDI;
CC       Note=Insulin (AI) with the disulfide bonds. The measured ranges are 32-
CC       76, 105-139.; Evidence={ECO:0000269|PubMed:10479677};
CC   -!- MASS SPECTROMETRY: Mass=8625.64; Mass_error=0.02; Method=MALDI;
CC       Note=Insulin (AI') with the disulfide bonds. The measured ranges are
CC       32-72, 105-139.; Evidence={ECO:0000269|PubMed:10479677};
CC   -!- SIMILARITY: Belongs to the insulin family. {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; AF160192; AAF80383.1; -; mRNA.
DR   RefSeq; NP_001191615.1; NM_001204686.1.
DR   AlphaFoldDB; Q9NDE7; -.
DR   GeneID; 100533403; -.
DR   CTD; 47190; -.
DR   OrthoDB; 1644517at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   Pfam; PF00049; Insulin; 1.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..31
FT   CHAIN           32..156
FT                   /note="Insulin"
FT                   /id="PRO_5000056896"
FT   PEPTIDE         32..76
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000307406"
FT   PEPTIDE         32..72
FT                   /note="Insulin B chain'"
FT                   /id="PRO_0000307407"
FT   PROPEP          79..93
FT                   /note="C peptide beta"
FT                   /id="PRO_0000307408"
FT   PROPEP          96..102
FT                   /note="C peptide alpha"
FT                   /id="PRO_0000307409"
FT   PEPTIDE         105..139
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000307410"
FT   PROPEP          141..156
FT                   /note="D peptide"
FT                   /id="PRO_0000307411"
FT   PROPEP          144..156
FT                   /note="D peptide short form"
FT                   /id="PRO_0000307412"
FT   MOD_RES         152
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:16522341"
FT   DISULFID        37..114
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..119
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..128
FT                   /evidence="ECO:0000255"
FT   DISULFID        112..115
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   156 AA;  17627 MW;  901641D2857BD3F3 CRC64;
     MSKFLLQSHS ANACLLTLLL TLASNLDISL ANFEHSCNGY MRPHPRGLCG EDLHVIISNL
     CSSLGGNRRF LAKYMVKRDT ENVNDKLRGI LLNKKEAFSY LTKREASGSI TCECCFNQCR
     IFELAQYCRL PDHFFSRISR TGRSNSGHAQ LEDNFS