INS1_RAT
ID INS1_RAT Reviewed; 110 AA.
AC P01322;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Insulin-1;
DE Contains:
DE RecName: Full=Insulin-1 B chain;
DE Contains:
DE RecName: Full=Insulin-1 A chain;
DE Flags: Precursor;
GN Name=Ins1; Synonyms=Ins-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=498283; DOI=10.1016/0092-8674(79)90070-9;
RA Cordell B., Bell G.I., Tischer E., Denoto F.M., Ullrich A., Pictet R.L.,
RA Rutter W.J., Goodman H.M.;
RT "Isolation and characterization of a cloned rat insulin gene.";
RL Cell 18:533-543(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=498284; DOI=10.1016/0092-8674(79)90071-0;
RA Lomedico P., Rosenthal N., Efstratiadis A., Gilbert W., Kolodner R.,
RA Tizard R.;
RT "The structure and evolution of the two nonallelic rat preproinsulin
RT genes.";
RL Cell 18:545-558(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6249167; DOI=10.1111/j.1749-6632.1980.tb47271.x;
RA Lomedico P.T., Rosenthal N., Kolodner R., Efstratiadis A., Gilbert W.;
RT "The structure of rat preproinsulin genes.";
RL Ann. N. Y. Acad. Sci. 343:425-432(1980).
RN [4]
RP PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX PubMed=4311938; DOI=10.1016/b978-0-12-571125-8.50008-9;
RA Steiner D.F., Clark J.L., Nolan C., Rubenstein A.H., Margoliash E.,
RA Aten B., Oyer P.E.;
RT "Proinsulin and the biosynthesis of insulin.";
RL Recent Prog. Horm. Res. 25:207-282(1969).
RN [5]
RP PROTEIN SEQUENCE OF 57-87.
RX PubMed=4640931; DOI=10.1016/s0021-9258(20)81791-8;
RA Tager H.S., Steiner D.F.;
RT "Primary structures of the proinsulin connecting peptides of the rat and
RT the horse.";
RL J. Biol. Chem. 247:7936-7940(1972).
RN [6]
RP PROTEIN SEQUENCE OF 57-87, AND SEQUENCE REVISION.
RX PubMed=4554104; DOI=10.1111/j.1432-1033.1972.tb01680.x;
RA Markussen J., Sundby F.;
RT "Rat-proinsulin C-peptides. Amino-acid sequences.";
RL Eur. J. Biochem. 25:153-162(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; V01242; CAA24559.1; -; Genomic_DNA.
DR EMBL; J00747; AAA41442.1; -; Genomic_DNA.
DR EMBL; M25584; AAA41439.1; -; Genomic_DNA.
DR PIR; A90788; IPRT1.
DR RefSeq; NP_062002.1; NM_019129.3.
DR AlphaFoldDB; P01322; -.
DR SMR; P01322; -.
DR STRING; 10116.ENSRNOP00000016052; -.
DR PaxDb; P01322; -.
DR PRIDE; P01322; -.
DR Ensembl; ENSRNOT00000016052; ENSRNOP00000016052; ENSRNOG00000012052.
DR GeneID; 24505; -.
DR KEGG; rno:24505; -.
DR UCSC; RGD:2915; rat.
DR CTD; 16333; -.
DR RGD; 2915; Ins1.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR GeneTree; ENSGT00390000015440; -.
DR HOGENOM; CLU_140421_1_0_1; -.
DR InParanoid; P01322; -.
DR OMA; IVEQCCN; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P01322; -.
DR TreeFam; TF332820; -.
DR PRO; PR:P01322; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012052; Expressed in pancreas and 6 other tissues.
DR Genevisible; P01322; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; IDA:RGD.
DR GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050714; P:positive regulation of protein secretion; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
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 Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:4311938"
FT PEPTIDE 25..54
FT /note="Insulin-1 B chain"
FT /evidence="ECO:0000269|PubMed:498284"
FT /id="PRO_0000015895"
FT PROPEP 57..87
FT /note="C peptide"
FT /id="PRO_0000015896"
FT PEPTIDE 90..110
FT /note="Insulin-1 A chain"
FT /evidence="ECO:0000269|PubMed:498284"
FT /id="PRO_0000015897"
FT DISULFID 31..96
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 43..109
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 95..100
FT /evidence="ECO:0000250|UniProtKB:P01308"
SQ SEQUENCE 110 AA; 12421 MW; 51D606DA54AE3533 CRC64;
MALWMRFLPL LALLVLWEPK PAQAFVKQHL CGPHLVEALY LVCGERGFFY TPKSRREVED
PQVPQLELGG GPEAGDLQTL ALEVARQKRG IVDQCCTSIC SLYQLENYCN
