P01323 (INS2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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	Secreted.
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ER overload response Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from electronic annotation. Source: Compara canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara lipid catabolic process Inferred from electronic annotation. Source: Compara myoblast fusion Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from electronic annotation. Source: Compara regulation of protein binding Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from direct assay PubMed 12475375. Source: RGD nucleus Inferred from electronic annotation. Source: Compara secretory granule Inferred from direct assay PubMed 10806118. Source: RGD small nucleolar ribonucleoprotein complex Inferred from electronic annotation. Source: Compara
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.1 Ref.4		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

	Sequence		Length	Mass (Da)
	P01323 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 3A626DA98C86F3CA	FASTA	110	12,339
	10 20 30 40 50 60 MALWIRFLPL LALLILWEPR PAQAFVKQHL CGSHLVEALY LVCGERGFFY TPMSRREVED 70 80 90 100 110 PQVAQLELGG GPGAGDLQTL ALEVARQKRG IVDQCCTSIC SLYQLENYCN

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
IPI	IPI00212593.
PIR	IPRT2. B90789.
RefSeq	NP_062003.1. NM_019130.2.
UniGene	Rn.989.
3D structure databases
ProteinModelPortal	P01323.
SMR	P01323. Positions 25-110.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000027656.
PTM databases
PhosphoSite	P01323.
Proteomic databases
PaxDb	P01323.
PRIDE	P01323.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000027656; ENSRNOP00000027656; ENSRNOG00000020405.
GeneID	24506.
KEGG	rno:24506.
Organism-specific databases
CTD	16334.
RGD	2916. Ins2.
Phylogenomic databases
eggNOG	NOG45999.
GeneTree	ENSGT00390000015440.
HOGENOM	HOG000261669.
HOVERGEN	HBG006137.
InParanoid	P01323.
KO	K04526.
OMA	AMAPPQH.
OrthoDB	EOG4RNB9Q.
Gene expression databases
Genevestigator	P01323.
GermOnline	ENSRNOG00000020405. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.100.10. 1 hit.
InterPro	IPR004825. Insulin. IPR016179. Insulin-like. IPR022353. Insulin_CS. IPR022352. Insulin_family. [Graphical view]
Pfam	PF00049. Insulin. 1 hit. [Graphical view]
PRINTS	PR00277. INSULIN. PR00276. INSULINFAMLY.
SMART	SM00078. IlGF. 1 hit. [Graphical view]
SUPFAM	SSF56994. Insulin-like. 1 hit.
PROSITE	PS00262. INSULIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	603523.
PMAP-CutDB	P01323.

Entry information

Entry name

INS2_RAT

Accession

Primary (citable) accession number: P01323

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program