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Protein

Insulin

Gene

INS

Organism
Sus scrofa (Pig)
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 migration Source: BHF-UCL
  3. positive regulation of DNA replication Source: BHF-UCL
  4. positive regulation of insulin receptor signaling pathway Source: BHF-UCL
  5. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  6. positive regulation of protein autophosphorylation Source: BHF-UCL
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei2122. Sus s Insulin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Peptidei25 – 5430Insulin B chainPRO_0000015879Add
BLAST
Propeptidei57 – 8529C peptidePRO_0000015880Add
BLAST
Peptidei88 – 10821Insulin A chainPRO_0000015881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 94Interchain (between B and A chains)
Disulfide bondi43 ↔ 107Interchain (between B and A chains)
Disulfide bondi93 ↔ 98

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-8437944,EBI-8437944

Protein-protein interaction databases

IntActiP01315. 1 interaction.
MINTiMINT-1505666.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4311Combined sources
Helixi44 – 463Combined sources
Beta strandi48 – 503Combined sources
Helixi89 – 957Combined sources
Helixi100 – 1034Combined sources
Helixi104 – 1063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B17X-ray1.70A88-108[»]
B25-54[»]
1B18X-ray1.80A88-108[»]
B25-54[»]
1B19X-ray1.80A88-108[»]
B25-54[»]
1B2AX-ray1.70A88-108[»]
B25-54[»]
1B2BX-ray1.80A88-108[»]
B25-54[»]
1B2CX-ray1.80A88-108[»]
B25-54[»]
1B2DX-ray1.70A88-108[»]
B25-54[»]
1B2EX-ray1.90A88-108[»]
B25-54[»]
1B2FX-ray1.90A88-108[»]
B25-54[»]
1B2GX-ray1.80A88-108[»]
B25-54[»]
1DEIX-ray1.60A/C88-108[»]
B/D25-47[»]
1IZAX-ray2.50A/C88-108[»]
B/D25-53[»]
1IZBX-ray2.00A/C88-108[»]
B/D25-53[»]
1M5AX-ray1.20A/C88-108[»]
B/D25-54[»]
1MPJX-ray2.30A/C88-108[»]
B/D25-54[»]
1SDBX-ray1.65A88-108[»]
B27-49[»]
1WAVX-ray2.50A/C/E/G/I/K88-108[»]
B/D/F/H/J/L25-54[»]
1ZEIX-ray1.90A/B/C/D/E/F25-54[»]
A/B/C/D/E/F88-108[»]
1ZNIX-ray1.50A/C88-108[»]
B/D25-54[»]
2EFAneutron diffraction2.70A88-108[»]
B25-54[»]
2G4MX-ray1.80A88-108[»]
B25-54[»]
2TCIX-ray1.80A/C88-108[»]
B/D25-54[»]
2ZPPneutron diffraction2.50A88-108[»]
B25-54[»]
3FHPneutron diffraction2.00A/C88-108[»]
B/D25-54[»]
3GKYX-ray1.80A/C88-108[»]
B/D25-54[»]
3INSX-ray1.50A/C88-108[»]
B/D25-54[»]
3MTHX-ray1.90A/C88-108[»]
B/D25-54[»]
3RTOX-ray1.80A/C88-108[»]
B/D25-54[»]
3T2AX-ray2.10A88-108[»]
B25-54[»]
4A7EX-ray1.86A88-108[»]
B25-54[»]
4INSX-ray1.50A/C88-108[»]
B/D25-54[»]
6INSX-ray2.00E/F25-108[»]
7INSX-ray2.00A/C/E88-108[»]
B/D/F25-54[»]
9INSX-ray1.70A88-108[»]
B25-54[»]
ProteinModelPortaliP01315.
SMRiP01315. Positions 25-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01315.

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006137.
InParanoidiP01315.
KOiK04526.

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.

P01315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY
60 70 80 90 100
TPKARREAEN PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL

YQLENYCN
Length:108
Mass (Da):11,672
Last modified:December 1, 2000 - v2
Checksum:iCB4491B429858EBE
GO

Sequence cautioni

The sequence AAC77920.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064555 mRNA. Translation: AAC77920.1. Different initiation.
AY044828 Genomic DNA. Translation: AAL69550.1.
AY242098 Genomic DNA. Translation: AAQ00952.1.
AY242099 Genomic DNA. Translation: AAQ00954.1.
AY242100 Genomic DNA. Translation: AAQ00957.1.
AY242101 Genomic DNA. Translation: AAQ00960.1.
AY242102 Genomic DNA. Translation: AAQ00963.1.
AY242103 Genomic DNA. Translation: AAQ00966.1.
AY242104 Genomic DNA. Translation: AAQ00969.1.
AY242105 Genomic DNA. Translation: AAQ00972.1.
AY242106 Genomic DNA. Translation: AAQ00975.1.
AY242107 Genomic DNA. Translation: AAQ00978.1.
AY242108 Genomic DNA. Translation: AAQ00981.1.
AY242109 Genomic DNA. Translation: AAQ00983.1.
AY242110 Genomic DNA. Translation: AAQ00985.1.
AY242111 Genomic DNA. Translation: AAQ00987.1.
AY242112 Genomic DNA. Translation: AAQ00990.1.
PIRiA01583. IPPG.
RefSeqiNP_001103242.1. NM_001109772.1.
UniGeneiSsc.583.

Genome annotation databases

GeneIDi397415.
KEGGissc:397415.

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
AF064555 mRNA. Translation: AAC77920.1. Different initiation.
AY044828 Genomic DNA. Translation: AAL69550.1.
AY242098 Genomic DNA. Translation: AAQ00952.1.
AY242099 Genomic DNA. Translation: AAQ00954.1.
AY242100 Genomic DNA. Translation: AAQ00957.1.
AY242101 Genomic DNA. Translation: AAQ00960.1.
AY242102 Genomic DNA. Translation: AAQ00963.1.
AY242103 Genomic DNA. Translation: AAQ00966.1.
AY242104 Genomic DNA. Translation: AAQ00969.1.
AY242105 Genomic DNA. Translation: AAQ00972.1.
AY242106 Genomic DNA. Translation: AAQ00975.1.
AY242107 Genomic DNA. Translation: AAQ00978.1.
AY242108 Genomic DNA. Translation: AAQ00981.1.
AY242109 Genomic DNA. Translation: AAQ00983.1.
AY242110 Genomic DNA. Translation: AAQ00985.1.
AY242111 Genomic DNA. Translation: AAQ00987.1.
AY242112 Genomic DNA. Translation: AAQ00990.1.
PIRiA01583. IPPG.
RefSeqiNP_001103242.1. NM_001109772.1.
UniGeneiSsc.583.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B17X-ray1.70A88-108[»]
B25-54[»]
1B18X-ray1.80A88-108[»]
B25-54[»]
1B19X-ray1.80A88-108[»]
B25-54[»]
1B2AX-ray1.70A88-108[»]
B25-54[»]
1B2BX-ray1.80A88-108[»]
B25-54[»]
1B2CX-ray1.80A88-108[»]
B25-54[»]
1B2DX-ray1.70A88-108[»]
B25-54[»]
1B2EX-ray1.90A88-108[»]
B25-54[»]
1B2FX-ray1.90A88-108[»]
B25-54[»]
1B2GX-ray1.80A88-108[»]
B25-54[»]
1DEIX-ray1.60A/C88-108[»]
B/D25-47[»]
1IZAX-ray2.50A/C88-108[»]
B/D25-53[»]
1IZBX-ray2.00A/C88-108[»]
B/D25-53[»]
1M5AX-ray1.20A/C88-108[»]
B/D25-54[»]
1MPJX-ray2.30A/C88-108[»]
B/D25-54[»]
1SDBX-ray1.65A88-108[»]
B27-49[»]
1WAVX-ray2.50A/C/E/G/I/K88-108[»]
B/D/F/H/J/L25-54[»]
1ZEIX-ray1.90A/B/C/D/E/F25-54[»]
A/B/C/D/E/F88-108[»]
1ZNIX-ray1.50A/C88-108[»]
B/D25-54[»]
2EFAneutron diffraction2.70A88-108[»]
B25-54[»]
2G4MX-ray1.80A88-108[»]
B25-54[»]
2TCIX-ray1.80A/C88-108[»]
B/D25-54[»]
2ZPPneutron diffraction2.50A88-108[»]
B25-54[»]
3FHPneutron diffraction2.00A/C88-108[»]
B/D25-54[»]
3GKYX-ray1.80A/C88-108[»]
B/D25-54[»]
3INSX-ray1.50A/C88-108[»]
B/D25-54[»]
3MTHX-ray1.90A/C88-108[»]
B/D25-54[»]
3RTOX-ray1.80A/C88-108[»]
B/D25-54[»]
3T2AX-ray2.10A88-108[»]
B25-54[»]
4A7EX-ray1.86A88-108[»]
B25-54[»]
4INSX-ray1.50A/C88-108[»]
B/D25-54[»]
6INSX-ray2.00E/F25-108[»]
7INSX-ray2.00A/C/E88-108[»]
B/D/F25-54[»]
9INSX-ray1.70A88-108[»]
B25-54[»]
ProteinModelPortaliP01315.
SMRiP01315. Positions 25-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01315. 1 interaction.
MINTiMINT-1505666.

Protein family/group databases

Allergomei2122. Sus s Insulin.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397415.
KEGGissc:397415.

Organism-specific databases

CTDi3630.

Phylogenomic databases

HOVERGENiHBG006137.
InParanoidiP01315.
KOiK04526.

Miscellaneous databases

EvolutionaryTraceiP01315.

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. "Complete porcine preproinsulin cDNA sequence."
    Han X.G., Tuch B.E.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Comparative sequence analysis of the INS-IGF2-H19 gene cluster in pigs."
    Amarger V., Nguyen M., Van Laere A.-S., Braunschweig M., Nezer C., Georges M., Andersson L.
    Mamm. Genome 13:388-398(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Large white.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: European wild boar, Hampshire, Japanese wild boar, Landrace, Large white, Meishan and Pietrain.
  4. "Porcine proinsulin: characterization and amino acid sequence."
    Chance R.E., Ellis R.M., Bromer W.W.
    Science 161:165-167(1968) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-108.
  5. Chance R.E.
    Submitted (JUL-1970) to the PIR data bank
    Cited for: SEQUENCE REVISION TO 59.
  6. "Insulin. The structure in the crystal and its reflection in chemistry and biology."
    Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.
    Adv. Protein Chem. 26:279-402(1972)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  7. "Experience with fast Fourier least squares in the refinement of the crystal structure of rhombohedral 2-zinc insulin at 1.5-A resolution."
    Isaacs N.W., Agarwal R.C.
    Acta Crystallogr. A 34:782-791(1978)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  9. "Structure of porcine insulin cocrystallized with clupeine Z."
    Balschmidt P., Hansen F.B., Dodson E., Dodson G., Korber F.
    Acta Crystallogr. B 47:975-986(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  11. "Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30) insulin at 1.65-A resolution."
    Diao J.-S., Wan Z.-L., Chang W.-R., Liang D.-C.
    Acta Crystallogr. D 53:507-512(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Entry informationi

Entry nameiINS_PIG
AccessioniPrimary (citable) accession number: P01315
Secondary accession number(s): Q9TSJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 2000
Last modified: January 7, 2015
This is version 140 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.