Reviewed, UniProtKB/Swiss-Prot P01317 (INS_BOVIN)

Names and origin

Protein names

Recommended name:
    Insulin
Cleaved into the following 2 chains:
    1- Recommended name:
            Insulin B chain
    2- Recommended name:
            Insulin A chain

Gene names

Name:

INS

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	105 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	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.2 Ref.3 Ref.7

Peptide

25 – 54

30

Insulin B chain Ref.1

PRO_0000015764

Propeptide

57 – 82

26

C peptide

PRO_0000015765

Peptide

85 – 105

21

Insulin A chain Ref.1

PRO_0000015766

Amino acid modifications

Disulfide bond

31 ↔ 91

Interchain (between B and A chains) Ref.7

Disulfide bond

43 ↔ 104

Interchain (between B and A chains) Ref.7

Disulfide bond

90 ↔ 95

Ref.2 Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

105

Helix Strand Turn

Details...

Helix

32 – 43

12

Helix

44 – 46

3

Helix

86 – 90

5

Helix

97 – 101

5

Sequences

	Sequence		Length	Mass (Da)
	P01317-1 [UniParc]. Last modified August 1, 1992. Version 2. Checksum: 75307CF78E61C06A	FASTA	105	11,393
	10 20 30 40 50 60 MALWTRLRPL LALLALWPPP PARAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG 70 80 90 100 PQVGALELAG GPGAGGLEGP PQKRGIVEQC CASVCSLYQL ENYCN

References

[1]	"Cloning and nucleotide sequence analysis of complementary deoxyribonucleic acid for bovine preproinsulin." D'Agostino J., Younes M.A., White J.W., Besch P.K., Field J.B., Frazier M.L. Mol. Endocrinol. 1:327-331(1987) [PubMed: 2456452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The structure of bovine proinsulin." Nolan C., Margoliash E., Peterson J.D., Steiner D.F. J. Biol. Chem. 246:2780-2795(1971) [PubMed: 4928892] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-105.
[3]	"The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates." Sanger F., Tuppy H. Biochem. J. 49:481-490(1951) [PubMed: 14886311] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-54.
[4]	"Isolation and characterization of proinsulin C-peptide from bovine pancreas." Steiner D.F., Cho S., Oyer P.E., Terris S., Peterson J.D., Rubenstein A.H. J. Biol. Chem. 246:1365-1374(1971) [PubMed: 5545080] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-82.
[5]	"Bovine proinsulin: amino acid sequence of the C-peptide isolated from pancreas." Salokangas A., Smyth D.G., Markussen J., Sundby F. Eur. J. Biochem. 20:183-189(1971) [PubMed: 5105368] [Abstract] Cited for: PROTEIN SEQUENCE OF 57-82.
[6]	"The amino-acid sequence in the glycyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates." Sanger F., Thompson E.O.P. Biochem. J. 53:366-374(1953) [PubMed: 13032079] [Abstract] Cited for: PROTEIN SEQUENCE OF 85-105.
[7]	"The disulphide bonds of insulin." Ryle A.P., Sanger F., Smith L.F., Kitai R. Biochem. J. 60:541-556(1955) [PubMed: 13249947] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-54 AND 85-105, DISULFIDE BONDS.
[8]	"The structure of des-Phe b1 bovine insulin." Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G., Reynolds C.D. Acta Crystallogr. B 38:3028-3032(1982) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-54.
[9]	"A model of insulin fibrils derived from the X-ray crystal structure of a monomeric insulin (despentapeptide insulin)." Brange J., Dodson G.G., Edwards D.J., Holden P.H., Whittingham J.L. Proteins 27:507-516(1997) [PubMed: 9141131] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-49.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Protein of the 20th century - Issue 9 of April 2001

Cross-references

Sequence databases

EMBLGenBankDDBJ

M54979 mRNA. Translation: AAA30722.1.

IPI

IPI00687020.

PIR

IPBO. A40909.

RefSeq

NP_776351.1.

UniGene

Bt.453

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APH	X-ray	2.00	A	85-105	[»]
			B	25-54	[»]
1BPH	X-ray	2.00	A	85-105	[»]
			B	25-54	[»]
1CPH	X-ray	1.90	A	85-105	[»]
			B	25-54	[»]
1DPH	X-ray	1.90	A	85-105	[»]
			B	25-54	[»]
1HO0	NMR	-	A	25-54	[»]
1PID	X-ray	1.30	A/C	85-105	[»]
			B/D	25-49	[»]
2A3G	X-ray	2.25	A/C	85-105	[»]
			B/D	25-54	[»]
2BN1	X-ray	1.40	A	85-105	[»]
			B	25-54	[»]
2BN3	X-ray	1.40	A	85-105	[»]
			B	25-54	[»]
2INS	X-ray	2.50	A/C	85-105	[»]
			B/D	26-54	[»]
2ZP6	X-ray	2.56	A/C	85-105	[»]
			B/D	25-54	[»]

SMR

P01317. Positions 25-105.

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000013003. Bos taurus. [Contig view]

GeneID

280829.

KEGG

bta:280829.

Phylogenomic databases

HOVERGEN

P01317.

Family and domain databases

InterPro

IPR004825. Ins/IGF/relaxin.
[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

PMAP-CutDB

P01317.

Entry information

Entry name

INS_BOVIN

Accession

Primary (citable) accession number: P01317

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)