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P30410 (INS_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin

Cleaved into the following 2 chains:

  1. Insulin B chain
  2. Insulin A chain
Gene names
Name:INS
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Secreted.

Sequence similarities

Belongs to the insulin family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

MAPK cascade

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase B activity

Inferred from electronic annotation. Source: Ensembl

acute-phase response

Inferred from electronic annotation. Source: Ensembl

alpha-beta T cell activation

Inferred from electronic annotation. Source: Ensembl

fatty acid homeostasis

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

glucose transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of NAD(P)H oxidase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of feeding behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of glycogen catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein oligomerization

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

negative regulation of respiratory burst involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucose import

Inferred from electronic annotation. Source: Ensembl

positive regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of glycolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of respiratory burst

Inferred from electronic annotation. Source: Ensembl

regulation of cellular amino acid metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Peptide25 – 5430Insulin B chain
PRO_0000015870
Propeptide57 – 8731C peptide
PRO_0000015871
Peptide90 – 11021Insulin A chain
PRO_0000015872

Amino acid modifications

Disulfide bond31 ↔ 96Interchain (between B and A chains) By similarity
Disulfide bond43 ↔ 109Interchain (between B and A chains) By similarity
Disulfide bond95 ↔ 100 By similarity

Secondary structure

.... 110
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30410 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 41EB8DF79837CEF5

FASTA11012,025
        10         20         30         40         50         60 
MALWMRLLPL LVLLALWGPD PASAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED 

        70         80         90        100        110 
LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN 

« Hide

References

[1]"Sequences of primate insulin genes support the hypothesis of a slower rate of molecular evolution in humans and apes than in monkeys."
Seino S., Bell G.I., Li W.
Mol. Biol. Evol. 9:193-203(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Global haplotype diversity in the human insulin gene region."
Stead J.D.H., Hurles M.E., Jeffreys A.J.
Genome Res. 13:2101-2111(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61089 Genomic DNA. Translation: CAA43403.1.
AY137497 Genomic DNA. Translation: AAN06933.1.
PIRA42179.
RefSeqNP_001008996.1. NM_001008996.2.
UniGenePtr.6479.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZVNMR-B25-49[»]
ProteinModelPortalP30410.
SMRP30410. Positions 25-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000057962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000006075; ENSPTRP00000005606; ENSPTRG00000003172.
GeneID449570.
KEGGptr:449570.

Organism-specific databases

CTD3630.

Phylogenomic databases

eggNOGNOG45999.
GeneTreeENSGT00390000015440.
HOGENOMHOG000261669.
HOVERGENHBG006137.
KOK04526.
OMAVEQCCHN.
OrthoDBEOG7TF7CG.
TreeFamTF332820.

Family and domain databases

Gene3D1.10.100.10. 2 hits.
InterProIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. SSF56994. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30410.
NextBio20832685.

Entry information

Entry nameINS_PANTR
AccessionPrimary (citable) accession number: P30410
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 19, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references