INS_FELCA
ID INS_FELCA Reviewed; 110 AA.
AC P06306; Q8WNW6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Okamoto S., Morimatsu M.;
RT "Cat insulin.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX PubMed=3518635; DOI=10.1016/0003-9861(86)90528-x;
RA Hallden G., Gafvelin G., Mutt V., Joernvall H.;
RT "Characterization of cat insulin.";
RL Arch. Biochem. Biophys. 247:20-27(1986).
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; AB043535; BAB84110.1; -; mRNA.
DR PIR; A01588; INCT.
DR RefSeq; NP_001009272.1; NM_001009272.1.
DR RefSeq; XP_019666739.1; XM_019811180.1.
DR AlphaFoldDB; P06306; -.
DR SMR; P06306; -.
DR STRING; 9685.ENSFCAP00000020961; -.
DR GeneID; 493804; -.
DR KEGG; fca:493804; -.
DR CTD; 3630; -.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR HOGENOM; CLU_140421_1_0_1; -.
DR InParanoid; P06306; -.
DR OMA; IVEQCCN; -.
DR OrthoDB; 1644517at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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 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:3518635"
FT PEPTIDE 25..54
FT /note="Insulin B chain"
FT /id="PRO_0000015809"
FT PROPEP 57..87
FT /note="C peptide"
FT /id="PRO_0000227016"
FT PEPTIDE 90..110
FT /note="Insulin A chain"
FT /id="PRO_0000015810"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 12069 MW; 95FB6E170C7BECA4 CRC64;
MAPWTRLLPL LALLSLWIPA PTRAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREAED
LQGKDAELGE APGAGGLQPS ALEAPLQKRG IVEQCCASVC SLYQLEHYCN