ID   INS_PANBU               Reviewed;         110 AA.
AC   Q98TA8;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=ins;
OS   Pantodon buchholzi (Freshwater butterflyfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Pantodontidae; Pantodon.
OX   NCBI_TaxID=8276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11306171; DOI=10.1016/s0303-7207(00)00449-4;
RA   Al-Mahrouki A.A., Irwin D.M., Graham L.C., Youson J.H.;
RT   "Molecular cloning of preproinsulin cDNAs from several osteoglossomorphs
RT   and a cyprinid.";
RL   Mol. Cell. Endocrinol. 174:51-58(2001).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It increases
CC       cell permeability to monosaccharides, amino acids and fatty acids. It
CC       accelerates glycolysis, the pentose phosphate cycle, and glycogen
CC       synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AF199588; AAK28712.1; -; mRNA.
DR   AlphaFoldDB; Q98TA8; -.
DR   SMR; Q98TA8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04367; IlGF_insulin_like; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR11454; PTHR11454; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..53
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000042212"
FT   PROPEP          56..87
FT                   /note="C peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000042213"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000042214"
FT   DISULFID        30..96
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..109
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   110 AA;  12324 MW;  BDECCD659D872E06 CRC64;
     MALWLQAFTL LVLLVLSSPG AQSASSQHLC GSHLVDALYM VCGEKGFFYQ PKTKRDVDPL
     LGFLSPKSAQ ENEADEYPYK DQGDLKVKRG IVEQCCHHPC NIFDLQNYCN