Reviewed,
UniProtKB/Swiss-Prot P01323 (INS2_RAT)
Last modified
November 3, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Insulin-2 Cleaved into the following 2 chains: 1- Recommended name: Insulin-2 B chain 2- Recommended name: Insulin-2 A chain | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 110 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the insulin family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hormone |
| PTM | Cleavage on pair of basic residues Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular space Inferred from direct assay. Source: RGD secretory granuleInferred from direct assay. Source: RGD soluble fractionInferred from direct assay. Source: RGD |
| Molecular function | hormone activity Inferred from electronic annotation. Source: UniProtKB-KW protease bindingInferred from physical interaction. Source: RGD protein complex bindingInferred from physical interaction. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Ref.4 | ||||||||
| Peptide | 25 – 54 | 30 | Insulin-2 B chain Ref.4 Ref.1 | PRO_0000015898 | |||||||
| Propeptide | 57 – 87 | 31 | C peptide Ref.5 Ref.6 | PRO_0000015899 | |||||||
| Peptide | 90 – 110 | 21 | Insulin-2 A chain Ref.1 | PRO_0000015900 | |||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 31 ↔ 96 | Interchain (between B and A chains) | |||||||||
| Disulfide bond | 43 ↔ 109 | Interchain (between B and A chains) | |||||||||
| Disulfide bond | 95 ↔ 100 | Ref.4 | |||||||||
Sequences
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 | |
|---|---|
| V01243 Genomic DNA. Translation: CAA24560.1. J00748 Genomic DNA. Translation: AAA41443.1. M25585, M25583 Genomic DNA. Translation: AAA41440.1. | |
| IPI | IPI00212593. |
| PIR | IPRT2. B90789. |
| RefSeq | NP_062003.1. |
| UniGene | Rn.989 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1APH based on UniProtKB P01317. |
| SMR | P01323. Positions 25-84. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P01323. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000027656; ENSRNOP00000027656; ENSRNOG00000020405; Rattus norvegicus. [Genome view] |
| GeneID | 24506. |
| KEGG | rno:24506. |
| UCSC | NM_019130. rat. |
Organism-specific databases | |
| CTD | 24506. |
| RGD | 2916. Ins2. |
Phylogenomic databases | |
| HOVERGEN | P01323. |
| OMA | PAPAFVN. |
Gene expression databases | |
| ArrayExpress | P01323. |
| Genevestigator | P01323. |
| GermOnline | ENSRNOG00000020405. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR004825. Ins/IGF/relaxin. IPR016179. Insulin-like. [Graphical view] |
| Gene3D | G3DSA:1.10.100.10. Ins/IGF/relaxin. 1 hit. |
| Pfam | PF00049. Insulin. 1 hit. [Graphical view] |
| PRINTS | PR00277. INSULINB. |
| ProDom | PD015667. Mollusc_ins. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00078. IlGF. 1 hit. [Graphical view] |
| PROSITE | PS00262. INSULIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 603523. |
| PMAP-CutDB | P01323. |
Entry information
| Entry name | INS2_RAT | ||||||||
| Accession | Primary (citable) accession number: P01323 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


