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P01323 (INS2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 101. 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 namesRecommended name:
Insulin-2

Cleaved into the following 2 chains:

  1. Insulin-2 B chain
  2. Insulin-2 A chain
Gene names
Name:Ins2
Synonyms:Ins-2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.4
Peptide25 – 5430Insulin-2 B chain Ref.1 Ref.4
PRO_0000015898
Propeptide57 – 8731C peptide Ref.5 Ref.6
PRO_0000015899
Peptide90 – 11021Insulin-2 A chain Ref.1
PRO_0000015900

Amino acid modifications

Disulfide bond31 ↔ 96Interchain (between B and A chains)
Disulfide bond43 ↔ 109Interchain (between B and A chains)
Disulfide bond95 ↔ 100 Ref.4

Sequences

Sequence LengthMass (Da)Tools
P01323 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3A626DA98C86F3CA

FASTA11012,339
        10         20         30         40         50         60 
MALWIRFLPL LALLILWEPR PAQAFVKQHL CGSHLVEALY LVCGERGFFY TPMSRREVED 

        70         80         90        100        110 
PQVAQLELGG GPGAGDLQTL ALEVARQKRG IVDQCCTSIC SLYQLENYCN 

« Hide

References

[1]"The structure and evolution of the two nonallelic rat preproinsulin genes."
Lomedico P., Rosenthal N., Efstratiadis A., Gilbert W., Kolodner R., Tizard R.
Cell 18:545-558(1979) [PubMed: 498284] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"RNA-mediated gene duplication: the rat preproinsulin I gene is a functional retroposon."
Soares M.B., Schin E., Henderson A., Karathanasis S.K., Cate R., Zeitlin S., Chirgwin J., Efstratiadis A.
Mol. Cell. Biol. 5:2090-2103(1985) [PubMed: 2427930] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The structure of rat preproinsulin genes."
Lomedico P.T., Rosenthal N., Kolodner R., Efstratiadis A., Gilbert W.
Ann. N. Y. Acad. Sci. 343:425-432(1980) [PubMed: 6249167] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Proinsulin and the biosynthesis of insulin."
Steiner D.F., Clark J.L., Nolan C., Rubenstein A.H., Margoliash E., Aten B., Oyer P.E.
Recent Prog. Horm. Res. 25:207-282(1969) [PubMed: 4311938] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-54 AND 90-110.
[5]"Primary structures of the proinsulin connecting peptides of the rat and the horse."
Tager H.S., Steiner D.F.
J. Biol. Chem. 247:7936-7940(1972) [PubMed: 4640931] [Abstract]
Cited for: PROTEIN SEQUENCE OF 57-87.
[6]"Rat-proinsulin C-peptides. Amino-acid sequences."
Markussen J., Sundby F.
Eur. J. Biochem. 25:153-162(1972) [PubMed: 4554104] [Abstract]
Cited for: PROTEIN SEQUENCE OF 57-87, SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01243 Genomic DNA. Translation: CAA24560.1.
J00748 Genomic DNA. Translation: AAA41443.1.
M25585, M25583 Genomic DNA. Translation: AAA41440.1.
IPIIPI00212593.
PIRIPRT2. B90789.
RefSeqNP_062003.1. NM_019130.2.
UniGeneRn.989.

3D structure databases

ProteinModelPortalP01323.
SMRP01323. Positions 25-110.
ModBaseSearch...

Protein-protein interaction databases

STRINGP01323.

Proteomic databases

PRIDEP01323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027656; ENSRNOP00000027656; ENSRNOG00000020405.
GeneID24506.
KEGGrno:24506.
UCSCNM_019130. rat.

Organism-specific databases

CTD16334.
RGD2916. Ins2.

Phylogenomic databases

eggNOGroNOG17912.
GeneTreeENSGT00390000015440.
HOVERGENHBG006137.
InParanoidP01323.
OMAMAALWLQ.
OrthoDBEOG4RNB9Q.
PhylomeDBP01323.

Gene expression databases

ArrayExpressP01323.
GenevestigatorP01323.
GermOnlineENSRNOG00000020405. Rattus norvegicus.

Family and domain databases

InterProIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
Gene3DG3DSA:1.10.100.10. Ins/IGF/relaxin. 1 hit.
KOK04526.
PfamPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. Insulin-like. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603523.
PMAP-CutDBP01323.

Entry information

Entry nameINS2_RAT
AccessionPrimary (citable) accession number: P01323
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 16, 2011
This is version 101 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