[1]	NUCLEOTIDE SEQUENCE. Han X.G., Tuch B.E.; "Complete porcine preproinsulin cDNA sequence."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Large white; DOI=10.1007/s00335-001-3059-x; PubMed=12140686 [NCBI, ExPASy, EBI, Israel, Japan] Amarger V., Nguyen M., Van Laere A.-S., Braunschweig M., Nezer C., Georges M., Andersson L.; "Comparative sequence analysis of the INS-IGF2-H19 gene cluster in pigs."; Mamm. Genome 13:388-398(2002).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=European wild boar, Hampshire, Japanese wild boar, Landrace, Large white, Meishan, and Pietrain; DOI=10.1038/nature02064; PubMed=14574411 [NCBI, ExPASy, EBI, Israel, Japan] Van Laere A.-S., Nguyen M., Braunschweig M., Nezer C., Collette C., Moreau L., Archibald A.L., Haley C., Buys N., Tally M., Andersson G., Georges M., Andersson L.; "A regulatory mutation in IGF2 causes a major QTL effect on muscle growth in the pig."; Nature 425:832-836(2003).
[4]	PROTEIN SEQUENCE OF 25-108. PubMed=5657063 [NCBI, ExPASy, EBI, Israel, Japan] Chance R.E., Ellis R.M., Bromer W.W.; "Porcine proinsulin: characterization and amino acid sequence."; Science 161:165-167(1968).
[5]	SEQUENCE REVISION TO 59. Chance R.E.; Submitted (JUL-1970) to the PIR data bank.
[6]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.; "Insulin. The structure in the crystal and its reflection in chemistry and biology."; Adv. Protein Chem. 26:279-402(1972).
[7]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). Isaacs N.W., Agarwal R.C.; "Experience with fast Fourier least squares in the refinement of the crystal structure of rhombohedral 2-zinc insulin at 1.5-A resolution."; Acta Crystallogr. A 34:782-791(1978).
[8]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). PubMed=2905485 [NCBI, ExPASy, EBI, Israel, Japan] Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Crowfoot Hodgkin D.M., Hubbard R.E., Isaacs N.W., Reynolds C.D., Sakabe K., Sakabe N., Vijayan N.M.; "The structure of 2Zn pig insulin crystals at 1.5-A resolution."; Philos. Trans. R. Soc. Lond., B, Biol. Sci. 319:369-456(1988).
[9]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1107/S010876819100842X; PubMed=1772633 [NCBI, ExPASy, EBI, Israel, Japan] Balschmidt P., Hansen F.B., Dodson E., Dodson G., Korber F.; "Structure of porcine insulin cocrystallized with clupeine Z."; Acta Crystallogr. B 47:975-986(1991).
[10]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). DOI=10.1107/S0108768190009570; PubMed=2025410 [NCBI, ExPASy, EBI, Israel, Japan] Badger J., Harris M.R., Reynolds C.D., Evans A.C., Dodson E.J., Dodson G.G., North A.C.T.; "Structure of the pig insulin dimer in the cubic crystal."; Acta Crystallogr. B 47:127-136(1991).
[11]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). DOI=10.1107/S0907444997004034; PubMed=15299880 [NCBI, ExPASy, EBI, Israel, Japan] Diao J.-S., Wan Z.-L., Chang W.-R., Liang D.-C.; "Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30) insulin at 1.65-A resolution."; Acta Crystallogr. D 53:507-512(1997).

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: Heterodimer of a B chain and an A chain linked by two disulfide bonds.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the insulin family.
WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th century - Issue 9 of April 2001; URL="http://www.expasy.org/spotlight/back_issues/sptlt009.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF064555; AAC77920.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY044828; AAL69550.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242098; AAQ00952.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242099; AAQ00954.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242100; AAQ00957.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242101; AAQ00960.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242102; AAQ00963.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242103; AAQ00966.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242104; AAQ00969.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242105; AAQ00972.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242106; AAQ00975.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242107; AAQ00978.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242108; AAQ00981.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242109; AAQ00983.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242110; AAQ00985.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242111; AAQ00987.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242112; AAQ00990.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A01583; IPPG.

NP_001103242.1; -.

3D structure databases

PDB

1B17; X-ray; 1.70 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B18; X-ray; 1.80 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B19; X-ray; 1.80 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2A; X-ray; 1.70 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2B; X-ray; 1.80 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2C; X-ray; 1.80 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2D; X-ray; 1.70 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2E; X-ray; 1.90 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2F; X-ray; 1.90 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1B2G; X-ray; 1.80 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
1DEI; X-ray; 1.60 A; A/C=88-108, B/D=25-47.	[ExPASy / RCSB / EBI]
1IZA; X-ray; 2.50 A; A/C=88-108, B/D=25-53.	[ExPASy / RCSB / EBI]
1IZB; X-ray; 2.00 A; A/C=88-108, B/D=25-53.	[ExPASy / RCSB / EBI]
1M5A; X-ray; 1.20 A; A/C=79-91, B/D=21-45.	[ExPASy / RCSB / EBI]
1MPJ; X-ray; 2.30 A; A/C=88-108, B/D=25-54.	[ExPASy / RCSB / EBI]
1SDB; X-ray; 1.65 A; A=88-108, B=27-49.	[ExPASy / RCSB / EBI]
1WAV; X-ray; 2.50 A; A/C/E/G/I/K=88-108, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1ZEI; X-ray; 1.90 A; A/B/C/D/E/F=25-54.	[ExPASy / RCSB / EBI]
1ZNI; X-ray; 1.50 A; A/C=88-108, B/D=25-54.	[ExPASy / RCSB / EBI]
2EFA; Neutron; 2.70 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
2G4M; X-ray; 1.80 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]
2TCI; X-ray; 1.80 A; A/C=88-108, B/D=25-54.	[ExPASy / RCSB / EBI]
3INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.	[ExPASy / RCSB / EBI]
3MTH; X-ray; 1.90 A; A/C=88-108, B/D=25-54.	[ExPASy / RCSB / EBI]
4INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.	[ExPASy / RCSB / EBI]
6INS; X-ray; 2.00 A; E/F=25-53.	[ExPASy / RCSB / EBI]
7INS; X-ray; 2.00 A; A/C/E=88-108, B/D/F=25-54.	[ExPASy / RCSB / EBI]
9INS; X-ray; 1.70 A; A=88-108, B=25-54.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B17; -.
1B18; -.
1B19; -.
1B2A; -.
1B2B; -.
1B2C; -.
1B2D; -.
1B2E; -.
1B2F; -.
1B2G; -.
1DEI; -.
1IZA; -.
1IZB; -.
1M5A; -.
1MPJ; -.
1SDB; -.
1WAV; -.
1ZEI; -.
1ZNI; -.
2EFA; -.
2G4M; -.
2TCI; -.
3INS; -.
3MTH; -.
4INS; -.
6INS; -.
7INS; -.
9INS; -.

SMR

P01315; 25-84.

ModBase

P01315.

Family and domain databases

InterPro

IPR004825; Ins/IGF/relaxin.
IPR003234; Insulin-related_peptide.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.100.10; Ins/IGF/relaxin; 1.

Pfam

PF00049; Insulin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00276; INSULINA.
PR00277; INSULINB.

ProDom

PD015667; Mollusc_ins; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00078; IlGF; 1.
SMART graphical view of domain structure.

PS00262; INSULIN; 1.

Other

Genome annotation databases

GeneID

397415; -.

Phylogenomic databases

HOVERGEN

P01315; -.

Other

P01315; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues; Direct protein sequencing; Glucose metabolism; Hormone; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`PEPTIDE`	`25 54`	`30`	`Insulin B chain.`	`PRO_0000015879`
`PROPEP`	`57 85`	`29`	`C peptide.`	`PRO_0000015880`
`PEPTIDE`	`88 108`	`21`	`Insulin A chain.`	`PRO_0000015881`
`DISULFID`	`31 94`		`Interchain (between B and A chains).`
`DISULFID`	`43 107`		`Interchain (between B and A chains).`
`DISULFID`	`93 98`
`HELIX`	`28 43`	`16`
`HELIX`	`44 46`	`3`
`STRAND`	`48 50`	`3`
`HELIX`	`89 95`	`7`
`HELIX`	`100 103`	`4`
`HELIX`	`104 106`	`3`

Sequence information

Length: 108 AA [This is the length of the unprocessed precursor]

Molecular weight: 11672 Da [This is the MW of the unprocessed precursor]

CRC64: CB4491B429858EBE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREAEN 

        70         80         90        100 
PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL YQLENYCN

P01315 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools