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P01340 (INS_KATPE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 attributes

Sequence length50 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
   Molecular functionHormone
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 2929Insulin B chain Ref.1
PRO_0000015826
Peptide30 – 5021Insulin A chain Ref.2
PRO_0000015827

Amino acid modifications

Disulfide bond7 ↔ 36Interchain (between B and A chains) By similarity
Disulfide bond19 ↔ 49Interchain (between B and A chains) By similarity
Disulfide bond35 ↔ 40 By similarity

Experimental info

Non-adjacent residues29 – 302

Sequences

Sequence LengthMass (Da)Tools
P01340 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3627578FE24CE92E

FASTA505,698
        10         20         30         40         50 
AANPHLCGSH LVEALYLVCG ERGFFYQPKG IHZZCCHKPC BIFZLZBYCN 

« Hide

References

[1]"Studies on insulin. V. On the structure of the glycyl chain of bonito insulin II."
Kotaki A.
J. Biochem. 53:61-70(1963) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-29.
[2]"Studies on insulin. III. On the structure of the alanyl chain of bonito insulin."
Kotaki A.
J. Biochem. 51:301-309(1962) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-50.

Cross-references

Sequence databases

PIRINBN2. A01607.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006137.

Family and domain databases

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

Entry information

Entry nameINS_KATPE
AccessionPrimary (citable) accession number: P01340
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2013
This is version 75 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