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P01315

- INS_PIG

UniProt

P01315 - INS_PIG

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Protein
Insulin
Gene
INS
Organism
Sus scrofa (Pig)
Status
Reviewed - 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 DNA replication Source: BHF-UCL
  3. positive regulation of cell migration 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 Publication
Add
BLAST
Peptidei25 – 5430Insulin B chain
PRO_0000015879Add
BLAST
Propeptidei57 – 8529C peptide
PRO_0000015880Add
BLAST
Peptidei88 – 10821Insulin A chain
PRO_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

MINTiMINT-1505666.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP01315.

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006137.
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

MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY    50
TPKARREAEN PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL 100
YQLENYCN 108
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A01583. IPPG.
RefSeqi NP_001103242.1. NM_001109772.1.
UniGenei Ssc.583.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B17 X-ray 1.70 A 88-108 [» ]
B 25-54 [» ]
1B18 X-ray 1.80 A 88-108 [» ]
B 25-54 [» ]
1B19 X-ray 1.80 A 88-108 [» ]
B 25-54 [» ]
1B2A X-ray 1.70 A 88-108 [» ]
B 25-54 [» ]
1B2B X-ray 1.80 A 88-108 [» ]
B 25-54 [» ]
1B2C X-ray 1.80 A 88-108 [» ]
B 25-54 [» ]
1B2D X-ray 1.70 A 88-108 [» ]
B 25-54 [» ]
1B2E X-ray 1.90 A 88-108 [» ]
B 25-54 [» ]
1B2F X-ray 1.90 A 88-108 [» ]
B 25-54 [» ]
1B2G X-ray 1.80 A 88-108 [» ]
B 25-54 [» ]
1DEI X-ray 1.60 A/C 88-108 [» ]
B/D 25-47 [» ]
1IZA X-ray 2.50 A/C 88-108 [» ]
B/D 25-53 [» ]
1IZB X-ray 2.00 A/C 88-108 [» ]
B/D 25-53 [» ]
1M5A X-ray 1.20 A/C 88-108 [» ]
B/D 25-54 [» ]
1MPJ X-ray 2.30 A/C 88-108 [» ]
B/D 25-54 [» ]
1SDB X-ray 1.65 A 88-108 [» ]
B 27-49 [» ]
1WAV X-ray 2.50 A/C/E/G/I/K 88-108 [» ]
B/D/F/H/J/L 25-54 [» ]
1ZEI X-ray 1.90 A/B/C/D/E/F 25-54 [» ]
A/B/C/D/E/F 88-108 [» ]
1ZNI X-ray 1.50 A/C 88-108 [» ]
B/D 25-54 [» ]
2EFA neutron diffraction 2.70 A 88-108 [» ]
B 25-54 [» ]
2G4M X-ray 1.80 A 88-108 [» ]
B 25-54 [» ]
2TCI X-ray 1.80 A/C 88-108 [» ]
B/D 25-54 [» ]
2ZPP neutron diffraction 2.50 A 88-108 [» ]
B 25-54 [» ]
3FHP neutron diffraction 2.00 A/C 88-108 [» ]
B/D 25-54 [» ]
3GKY X-ray 1.80 A/C 88-108 [» ]
B/D 25-54 [» ]
3INS X-ray 1.50 A/C 88-108 [» ]
B/D 25-54 [» ]
3MTH X-ray 1.90 A/C 88-108 [» ]
B/D 25-54 [» ]
3RTO X-ray 1.80 A/C 88-108 [» ]
B/D 25-54 [» ]
3T2A X-ray 2.10 A 88-108 [» ]
B 25-54 [» ]
4A7E X-ray 1.86 A 88-108 [» ]
B 25-54 [» ]
4INS X-ray 1.50 A/C 88-108 [» ]
B/D 25-54 [» ]
6INS X-ray 2.00 E/F 25-108 [» ]
7INS X-ray 2.00 A/C/E 88-108 [» ]
B/D/F 25-54 [» ]
9INS X-ray 1.70 A 88-108 [» ]
B 25-54 [» ]
ProteinModelPortali P01315.
SMRi P01315. Positions 25-108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1505666.

Protein family/group databases

Allergomei 2122. Sus s Insulin.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397415.
KEGGi ssc:397415.

Organism-specific databases

CTDi 3630.

Phylogenomic databases

HOVERGENi HBG006137.
KOi K04526.

Miscellaneous databases

EvolutionaryTracei P01315.

Family and domain databases

Gene3Di 1.10.100.10. 1 hit.
InterProi IPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view ]
Pfami PF00049. Insulin. 1 hit.
[Graphical view ]
PRINTSi PR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTi SM00078. IlGF. 1 hit.
[Graphical view ]
SUPFAMi SSF56994. SSF56994. 1 hit.
PROSITEi PS00262. INSULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 136 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

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