ID   INS_SHEEP               Reviewed;         105 AA.
AC   P01318;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 102.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8011164; DOI=10.1089/dna.1994.13.377;
RA   Ohlsen S.M., Lugenbeel K.A., Wong E.A.;
RT   "Characterization of the linked ovine insulin and insulin-like growth
RT   factor-II genes.";
RL   DNA Cell Biol. 13:377-388(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 85-105.
RX   PubMed=13249948; DOI=10.1042/bj0600556;
RA   Brown H., Sanger F., Kitai R.;
RT   "The structure of pig and sheep insulins.";
RL   Biochem. J. 60:556-565(1955).
RN   [3]
RP   PROTEIN SEQUENCE OF 57-82.
RX   PubMed=4626369; DOI=10.1016/s0021-9258(19)44991-0;
RA   Peterson J.D., Nehrlich S., Oyer P.E., Steiner D.F.;
RT   "Determination of the amino acid sequence of the monkey, sheep, and dog
RT   proinsulin C-peptides by a semi-micro Edman degradation procedure.";
RL   J. Biol. Chem. 247:4866-4871(1972).
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. {ECO:0000250|UniProtKB:P01308}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; U00659; AAB60625.1; -; Genomic_DNA.
DR   PIR; S16430; INSH.
DR   PDB; 6CE7; EM; 7.40 A; O=25-54.
DR   PDB; 6CE9; EM; 4.30 A; L/O=25-54.
DR   PDB; 6CEB; EM; 4.70 A; L/O=25-54.
DR   PDBsum; 6CE7; -.
DR   PDBsum; 6CE9; -.
DR   PDBsum; 6CEB; -.
DR   AlphaFoldDB; P01318; -.
DR   BMRB; P01318; -.
DR   SMR; P01318; -.
DR   IntAct; P01318; 1.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:AgBase.
DR   GO; GO:1904927; P:cellular response to palmitoleic acid; IDA:AgBase.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:1903576; P:response to L-arginine; ISS:AgBase.
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   3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:13249948"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015909"
FT   PROPEP          57..82
FT                   /note="C peptide"
FT                   /id="PRO_0000015910"
FT   PEPTIDE         85..105
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015911"
FT   DISULFID        31..91
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
FT   DISULFID        43..104
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
FT   DISULFID        90..95
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
SQ   SEQUENCE   105 AA;  11235 MW;  8B27C7FB9922BC7A CRC64;
     MALWTRLVPL LALLALWAPA PAHAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG
     PQVGALELAG GPGAGGLEGP PQKRGIVEQC CAGVCSLYQL ENYCN