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Protein

Insulin

Gene

INS

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

GO - Molecular functioni

  1. identical protein binding Source: IntAct

GO - Biological processi

  1. glucose metabolic process Source: UniProtKB-KW
  2. positive regulation of cell maturation Source: AgBase
  3. positive regulation of gene expression Source: AgBase
  4. positive regulation of phosphatidylinositol 3-kinase signaling Source: AgBase
  5. positive regulation of Rho protein signal transduction Source: AgBase
  6. response to glucose Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin
Cleaved into the following 2 chains:
Gene namesi
Name:INS
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei2118. Bos d Insulin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24243 PublicationsAdd
BLAST
Peptidei25 – 5430Insulin B chain1 PublicationPRO_0000015764Add
BLAST
Propeptidei57 – 8226C peptidePRO_0000015765Add
BLAST
Peptidei85 – 10521Insulin A chain1 PublicationPRO_0000015766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 91Interchain (between B and A chains)1 Publication
Disulfide bondi43 ↔ 104Interchain (between B and A chains)1 Publication
Disulfide bondi90 ↔ 952 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Miscellaneous databases

PMAP-CutDBP01317.

Interactioni

Subunit structurei

Heterodimer of a B chain and an A chain linked by two disulfide bonds.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-3989070,EBI-3989070
IGF1RP080694EBI-3989070,EBI-475981From a different organism.
INSRP062135EBI-3989070,EBI-475899From a different organism.
Sama_0787A1S3N82EBI-3989070,EBI-7016414From a different organism.

Protein-protein interaction databases

DIPiDIP-52901N.
IntActiP01317. 5 interactions.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4311Combined sources
Helixi44 – 463Combined sources
Beta strandi48 – 503Combined sources
Helixi86 – 905Combined sources
Turni91 – 944Combined sources
Helixi97 – 1015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APHX-ray2.00A85-105[»]
B25-54[»]
1BPHX-ray2.00A85-105[»]
B25-54[»]
1CPHX-ray1.90A85-105[»]
B25-54[»]
1DPHX-ray1.90A85-105[»]
B25-54[»]
1HO0NMR-A25-54[»]
1PIDX-ray1.30A/C85-105[»]
B/D25-49[»]
2A3GX-ray2.25A/C85-105[»]
B/D25-54[»]
2BN1X-ray1.40A85-105[»]
B25-54[»]
2BN3X-ray1.40A85-105[»]
B25-54[»]
2INSX-ray2.50A/C85-105[»]
B/D26-54[»]
2ZP6X-ray2.56A/C85-105[»]
B/D25-54[»]
3W14X-ray4.40A/I85-105[»]
B/J25-54[»]
4BS3X-ray2.30A85-105[»]
B25-54[»]
4E7TX-ray1.40A/C85-105[»]
B/D25-54[»]
4E7UX-ray1.30A/C85-105[»]
B/D25-54[»]
4E7VX-ray1.801/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y85-105[»]
2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z25-54[»]
4I5YX-ray1.80A85-105[»]
B25-54[»]
4I5ZX-ray1.80A85-105[»]
B25-54[»]
4IDWX-ray2.70A/C85-105[»]
B/D25-54[»]
4IHNX-ray1.16A85-105[»]
B25-54[»]
4M4FX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4HX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4IX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4JX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4LX-ray1.45A/C85-105[»]
B/D25-54[»]
4M4MX-ray1.50A/C85-105[»]
B/D25-54[»]
ProteinModelPortaliP01317.
SMRiP01317. Positions 25-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01317.

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45999.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01317.

Family and domain databases

Gene3Di1.10.100.10. 1 hit.
InterProiIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01317-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALWTRLRPL LALLALWPPP PARAFVNQHL CGSHLVEALY LVCGERGFFY
60 70 80 90 100
TPKARREVEG PQVGALELAG GPGAGGLEGP PQKRGIVEQC CASVCSLYQL

ENYCN
Length:105
Mass (Da):11,393
Last modified:August 1, 1992 - v2
Checksum:i75307CF78E61C06A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M54979 mRNA. Translation: AAA30722.1.
PIRiA40909. IPBO.
UniGeneiBt.453.

Cross-referencesi

Web resourcesi

Protein Spotlight

Protein of the 20th century - Issue 9 of April 2001

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M54979 mRNA. Translation: AAA30722.1.
PIRiA40909. IPBO.
UniGeneiBt.453.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1APHX-ray2.00A85-105[»]
B25-54[»]
1BPHX-ray2.00A85-105[»]
B25-54[»]
1CPHX-ray1.90A85-105[»]
B25-54[»]
1DPHX-ray1.90A85-105[»]
B25-54[»]
1HO0NMR-A25-54[»]
1PIDX-ray1.30A/C85-105[»]
B/D25-49[»]
2A3GX-ray2.25A/C85-105[»]
B/D25-54[»]
2BN1X-ray1.40A85-105[»]
B25-54[»]
2BN3X-ray1.40A85-105[»]
B25-54[»]
2INSX-ray2.50A/C85-105[»]
B/D26-54[»]
2ZP6X-ray2.56A/C85-105[»]
B/D25-54[»]
3W14X-ray4.40A/I85-105[»]
B/J25-54[»]
4BS3X-ray2.30A85-105[»]
B25-54[»]
4E7TX-ray1.40A/C85-105[»]
B/D25-54[»]
4E7UX-ray1.30A/C85-105[»]
B/D25-54[»]
4E7VX-ray1.801/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y85-105[»]
2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z25-54[»]
4I5YX-ray1.80A85-105[»]
B25-54[»]
4I5ZX-ray1.80A85-105[»]
B25-54[»]
4IDWX-ray2.70A/C85-105[»]
B/D25-54[»]
4IHNX-ray1.16A85-105[»]
B25-54[»]
4M4FX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4HX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4IX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4JX-ray1.90A/C85-105[»]
B/D25-54[»]
4M4LX-ray1.45A/C85-105[»]
B/D25-54[»]
4M4MX-ray1.50A/C85-105[»]
B/D25-54[»]
ProteinModelPortaliP01317.
SMRiP01317. Positions 25-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-52901N.
IntActiP01317. 5 interactions.

Protein family/group databases

Allergomei2118. Bos d Insulin.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG45999.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01317.

Miscellaneous databases

EvolutionaryTraceiP01317.
NextBioi20804979.
PMAP-CutDBP01317.

Family and domain databases

Gene3Di1.10.100.10. 1 hit.
InterProiIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and nucleotide sequence analysis of complementary deoxyribonucleic acid for bovine preproinsulin."
    D'Agostino J., Younes M.A., White J.W., Besch P.K., Field J.B., Frazier M.L.
    Mol. Endocrinol. 1:327-331(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The structure of bovine proinsulin."
    Nolan C., Margoliash E., Peterson J.D., Steiner D.F.
    J. Biol. Chem. 246:2780-2795(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-105.
  3. "The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates."
    Sanger F., Tuppy H.
    Biochem. J. 49:481-490(1951) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-54.
  4. "Isolation and characterization of proinsulin C-peptide from bovine pancreas."
    Steiner D.F., Cho S., Oyer P.E., Terris S., Peterson J.D., Rubenstein A.H.
    J. Biol. Chem. 246:1365-1374(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-82.
  5. "Bovine proinsulin: amino acid sequence of the C-peptide isolated from pancreas."
    Salokangas A., Smyth D.G., Markussen J., Sundby F.
    Eur. J. Biochem. 20:183-189(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-82.
  6. "The amino-acid sequence in the glycyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates."
    Sanger F., Thompson E.O.P.
    Biochem. J. 53:366-374(1953) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 85-105.
  7. "The disulphide bonds of insulin."
    Ryle A.P., Sanger F., Smith L.F., Kitai R.
    Biochem. J. 60:541-556(1955) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-54 AND 85-105, DISULFIDE BONDS.
  8. "The structure of des-Phe b1 bovine insulin."
    Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G., Reynolds C.D.
    Acta Crystallogr. B 38:3028-3032(1982)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-54.
  9. "A model of insulin fibrils derived from the X-ray crystal structure of a monomeric insulin (despentapeptide insulin)."
    Brange J., Dodson G.G., Edwards D.J., Holden P.H., Whittingham J.L.
    Proteins 27:507-516(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-49.

Entry informationi

Entry nameiINS_BOVIN
AccessioniPrimary (citable) accession number: P01317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1992
Last modified: February 4, 2015
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.