ID   INS_MYXGL               Reviewed;         115 AA.
AC   P01342;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 101.
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   Myxine glutinosa (Atlantic hagfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC   Myxiniformes; Myxinidae; Myxininae; Myxine.
OX   NCBI_TaxID=7769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6265453; DOI=10.1016/s0021-9258(19)69003-4;
RA   Chan S.J., Emdin S.O., Kwok S.C.M., Kramer J.M., Falkmer S., Steiner D.F.;
RT   "Messenger RNA sequence and primary structure of preproinsulin in a
RT   primitive vertebrate, the Atlantic hagfish.";
RL   J. Biol. Chem. 256:7595-7602(1981).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-57 AND 95-115.
RX   PubMed=1097441; DOI=10.1016/s0021-9258(19)41294-5;
RA   Peterson J.D., Steiner D.F., Emdin S.O., Falkmer S.;
RT   "The amino acid sequence of the insulin from a primitive vertebrate, the
RT   atlantic hagfish (Myxine glutinosa).";
RL   J. Biol. Chem. 250:5183-5191(1975).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 AND 6.0 ANGSTROMS).
RX   PubMed=4418746; DOI=10.1038/251239a0;
RA   Peterson J.D., Coulter C.L., Steiner D.F., Emdin S.O., Falkmer S.;
RT   "Structural and crystallographic observations on hagfish insulin.";
RL   Nature 251:239-240(1974).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
RX   PubMed=4427361; DOI=10.1016/0022-2836(74)90557-9;
RA   Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Sabesan M.N.;
RT   "Low resolution crystal structure of hagfish insulin.";
RL   J. Mol. Biol. 87:23-30(1974).
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; V00649; CAA23993.1; -; mRNA.
DR   PIR; A01609; IPHF.
DR   AlphaFoldDB; P01342; -.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:1097441"
FT   PEPTIDE         27..57
FT                   /note="Insulin B chain"
FT                   /evidence="ECO:0000269|PubMed:1097441"
FT                   /id="PRO_0000015852"
FT   PROPEP          60..92
FT                   /note="C peptide"
FT                   /id="PRO_0000015853"
FT   PEPTIDE         95..115
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:1097441"
FT                   /id="PRO_0000015854"
FT   DISULFID        33..101
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        45..114
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        100..105
FT   CONFLICT        109
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   115 AA;  12615 MW;  C6E3352B0C27581A CRC64;
     MALSPFLAAV IPLVLLLSRA PPSADTRTTG HLCGKDLVNA LYIACGVRGF FYDPTKMKRD
     TGALAAFLPL AYAEDNESQD DESIGINEVL KSKRGIVEQC CHKRCSIYDL ENYCN