INS1_XENLA
ID INS1_XENLA Reviewed; 106 AA.
AC P12706;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=ins-a; Synonyms=ins1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2722842; DOI=10.1016/s0021-9258(18)60549-6;
RA Shuldiner A.R., Phillips S., Roberts C.T. Jr., Leroith D., Roth J.;
RT "Xenopus laevis contains two nonallelic preproinsulin genes. cDNA cloning
RT and evolutionary perspective.";
RL J. Biol. Chem. 264:9428-9432(1989).
RN [2]
RP PROTEIN SEQUENCE OF 24-53 AND 86-106.
RX PubMed=2661211; DOI=10.1210/endo-125-1-469;
RA Shuldiner A.R., Bennett C., Robinson E.A., Roth J.;
RT "Isolation and characterization of two different insulins from an
RT amphibian, Xenopus laevis.";
RL Endocrinology 125:469-477(1989).
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; M24443; AAA49888.1; -; mRNA.
DR PIR; A33847; IPXL1.
DR RefSeq; NP_001079351.1; NM_001085882.1.
DR AlphaFoldDB; P12706; -.
DR SMR; P12706; -.
DR GeneID; 378696; -.
DR KEGG; xla:378696; -.
DR CTD; 378696; -.
DR Xenbase; XB-GENE-6252363; ins.S.
DR OMA; IVEQCCN; -.
DR OrthoDB; 1644517at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 378696; Expressed in pancreas and 6 other tissues.
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 Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2661211"
FT PEPTIDE 24..53
FT /note="Insulin-1 B chain"
FT /id="PRO_0000015929"
FT PROPEP 56..83
FT /note="C peptide"
FT /id="PRO_0000015930"
FT PEPTIDE 86..106
FT /note="Insulin-1 A chain"
FT /id="PRO_0000015931"
FT DISULFID 30..92
FT /note="Interchain (between B and A chains)"
FT DISULFID 42..105
FT /note="Interchain (between B and A chains)"
FT DISULFID 91..96
SQ SEQUENCE 106 AA; 12170 MW; E3552E865CCF025A CRC64;
MALWMQCLPL VLVLFFSTPN TEALVNQHLC GSHLVEALYL VCGDRGFFYY PKVKRDMEQA
LVSGPQDNEL DGMQLQPQEY QKMKRGIVEQ CCHSTCSLFQ LESYCN
