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UniProtKB - P01315 (INS_PIG)
Protein
Insulin
Gene
INS
Organism
Sus scrofa (Pig)
Status
Functioni
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.
GO - Molecular functioni
- hormone activity Source: AgBase
- identical protein binding Source: IntAct
- insulin-like growth factor receptor binding Source: AgBase
- insulin receptor binding Source: Ensembl
- protease binding Source: Ensembl
GO - Biological processi
- activation of protein kinase B activity Source: Ensembl
- acute-phase response Source: Ensembl
- alpha-beta T cell activation Source: Ensembl
- fatty acid homeostasis Source: Ensembl
- glucose homeostasis Source: GO_Central
- glucose metabolic process Source: UniProtKB-KW
- glycoprotein biosynthetic process Source: AgBase
- G protein-coupled receptor signaling pathway Source: Ensembl
- insulin receptor signaling pathway Source: Ensembl
- lactate biosynthetic process Source: AgBase
- lipid biosynthetic process Source: AgBase
- lipoprotein biosynthetic process Source: AgBase
- negative regulation of acute inflammatory response Source: Ensembl
- negative regulation of fatty acid metabolic process Source: Ensembl
- negative regulation of feeding behavior Source: Ensembl
- negative regulation of gene expression Source: Ensembl
- negative regulation of gluconeogenesis Source: AgBase
- negative regulation of glycogen catabolic process Source: Ensembl
- negative regulation of lipid catabolic process Source: Ensembl
- negative regulation of NAD(P)H oxidase activity Source: Ensembl
- negative regulation of protein catabolic process Source: Ensembl
- negative regulation of protein secretion Source: Ensembl
- negative regulation of proteolysis Source: Ensembl
- negative regulation of reactive oxygen species biosynthetic process Source: Ensembl
- negative regulation of respiratory burst involved in inflammatory response Source: Ensembl
- neuron projection maintenance Source: Ensembl
- nitric oxide-cGMP-mediated signaling pathway Source: Ensembl
- positive regulation of cell migration Source: BHF-UCL
- positive regulation of cell population proliferation Source: Ensembl
- positive regulation of cytokine production Source: Ensembl
- positive regulation of dendritic spine maintenance Source: Ensembl
- positive regulation of DNA replication Source: BHF-UCL
- positive regulation of fatty acid biosynthetic process Source: CACAO
- positive regulation of glucose import Source: Ensembl
- positive regulation of glucose metabolic process Source: CACAO
- positive regulation of glycogen biosynthetic process Source: Ensembl
- positive regulation of glycolytic process Source: Ensembl
- positive regulation of insulin receptor signaling pathway Source: BHF-UCL
- positive regulation of lipoprotein lipase activity Source: CACAO
- positive regulation of MAPK cascade Source: Ensembl
- positive regulation of mitotic nuclear division Source: Ensembl
- positive regulation of NF-kappaB transcription factor activity Source: Ensembl
- positive regulation of nitric oxide mediated signal transduction Source: Ensembl
- positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
- positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
- positive regulation of protein autophosphorylation Source: BHF-UCL
- positive regulation of protein kinase B signaling Source: Ensembl
- positive regulation of protein localization to nucleus Source: Ensembl
- positive regulation of protein secretion Source: GO_Central
- positive regulation of respiratory burst Source: Ensembl
- regulation of cellular amino acid metabolic process Source: Ensembl
- regulation of protein localization to plasma membrane Source: Ensembl
- regulation of transmembrane transporter activity Source: Ensembl
- response to L-arginine Source: AgBase
- vasodilation Source: Ensembl
- wound healing Source: Ensembl
Keywordsi
Molecular function | Hormone |
Biological process | Carbohydrate metabolism, Glucose metabolism |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:INS |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Organism-specific databases
VGNCi | VGNC:99778, INS |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: AgBase
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | 1 PublicationAdd BLAST | 24 | |
PeptideiPRO_0000015879 | 25 – 54 | Insulin B chainAdd BLAST | 30 | |
PropeptideiPRO_0000015880 | 57 – 85 | C peptideAdd BLAST | 29 | |
PeptideiPRO_0000015881 | 88 – 108 | Insulin A chainAdd BLAST | 21 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 31 ↔ 94 | Interchain (between B and A chains)Combined sources3 Publications | ||
Disulfide bondi | 43 ↔ 107 | Interchain (between B and A chains)Combined sources3 Publications | ||
Disulfide bondi | 93 ↔ 98 | Combined sources3 Publications |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bondProteomic databases
PaxDbi | P01315 |
Interactioni
Subunit structurei
Heterodimer of a B chain and an A chain linked by two disulfide bonds.
By similarityBinary interactionsi
P01315
With | #Exp. | IntAct |
---|---|---|
itself | 2 | EBI-8437944,EBI-8437944 |
GO - Molecular functioni
- hormone activity Source: AgBase
- identical protein binding Source: IntAct
- insulin-like growth factor receptor binding Source: AgBase
- insulin receptor binding Source: Ensembl
- protease binding Source: Ensembl
Protein-protein interaction databases
IntActi | P01315, 1 interactor |
MINTi | P01315 |
STRINGi | 9823.ENSSSCP00000025428 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P01315 |
BMRBi | P01315 |
SASBDBi | P01315 |
SMRi | P01315 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P01315 |
Family & Domainsi
Sequence similaritiesi
Belongs to the insulin family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG502S5P5, Eukaryota |
GeneTreei | ENSGT00390000015440 |
InParanoidi | P01315 |
OMAi | IVEQCCN |
OrthoDBi | 1644517at2759 |
Family and domain databases
CDDi | cd04367, IlGF_insulin_like, 1 hit |
InterProi | View protein in InterPro IPR004825, Insulin IPR016179, Insulin-like IPR036438, Insulin-like_sf IPR022353, Insulin_CS IPR022352, Insulin_family |
PANTHERi | PTHR11454, PTHR11454, 1 hit |
Pfami | View protein in Pfam PF00049, Insulin, 1 hit |
PRINTSi | PR00277, INSULIN PR00276, INSULINFAMLY |
SMARTi | View protein in SMART SM00078, IlGF, 1 hit |
SUPFAMi | SSF56994, SSF56994, 1 hit |
PROSITEi | View protein in PROSITE PS00262, INSULIN, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P01315-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY
60 70 80 90 100
TPKARREAEN PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL
YQLENYCN
Sequence cautioni
The sequence AAC77920 differs from that shown. Reason: Erroneous initiation.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF064555 mRNA Translation: AAC77920.1 Different initiation. AY044828 Genomic DNA Translation: AAL69550.1 AY242098 Genomic DNA Translation: AAQ00952.1 AY242099 Genomic DNA Translation: AAQ00954.1 AY242100 Genomic DNA Translation: AAQ00957.1 AY242101 Genomic DNA Translation: AAQ00960.1 AY242102 Genomic DNA Translation: AAQ00963.1 AY242103 Genomic DNA Translation: AAQ00966.1 AY242104 Genomic DNA Translation: AAQ00969.1 AY242105 Genomic DNA Translation: AAQ00972.1 AY242106 Genomic DNA Translation: AAQ00975.1 AY242107 Genomic DNA Translation: AAQ00978.1 AY242108 Genomic DNA Translation: AAQ00981.1 AY242109 Genomic DNA Translation: AAQ00983.1 AY242110 Genomic DNA Translation: AAQ00985.1 AY242111 Genomic DNA Translation: AAQ00987.1 AY242112 Genomic DNA Translation: AAQ00990.1 |
PIRi | A01583, IPPG |
RefSeqi | NP_001103242.1, NM_001109772.1 |
Genome annotation databases
Similar proteinsi
Cross-referencesi
Web resourcesi
Protein Spotlight Protein of the 20th century - Issue 9 of April 2001 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF064555 mRNA Translation: AAC77920.1 Different initiation. AY044828 Genomic DNA Translation: AAL69550.1 AY242098 Genomic DNA Translation: AAQ00952.1 AY242099 Genomic DNA Translation: AAQ00954.1 AY242100 Genomic DNA Translation: AAQ00957.1 AY242101 Genomic DNA Translation: AAQ00960.1 AY242102 Genomic DNA Translation: AAQ00963.1 AY242103 Genomic DNA Translation: AAQ00966.1 AY242104 Genomic DNA Translation: AAQ00969.1 AY242105 Genomic DNA Translation: AAQ00972.1 AY242106 Genomic DNA Translation: AAQ00975.1 AY242107 Genomic DNA Translation: AAQ00978.1 AY242108 Genomic DNA Translation: AAQ00981.1 AY242109 Genomic DNA Translation: AAQ00983.1 AY242110 Genomic DNA Translation: AAQ00985.1 AY242111 Genomic DNA Translation: AAQ00987.1 AY242112 Genomic DNA Translation: AAQ00990.1 |
PIRi | A01583, IPPG |
RefSeqi | NP_001103242.1, NM_001109772.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1B17 | X-ray | 1.70 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B18 | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B19 | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2A | X-ray | 1.70 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2B | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2C | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2D | X-ray | 1.70 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2E | X-ray | 1.90 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2F | X-ray | 1.90 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1B2G | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
1DEI | X-ray | 1.60 | A/C | 88-108 | [»] | |
B/D | 25-47 | [»] | ||||
1IZA | X-ray | 2.50 | A/C | 88-108 | [»] | |
B/D | 25-53 | [»] | ||||
1IZB | X-ray | 2.00 | A/C | 88-108 | [»] | |
B/D | 25-53 | [»] | ||||
1M5A | X-ray | 1.20 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
1MPJ | X-ray | 2.30 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
1SDB | X-ray | 1.65 | A | 88-108 | [»] | |
B | 27-49 | [»] | ||||
1WAV | X-ray | 2.50 | A/C/E/G/I/K | 88-108 | [»] | |
B/D/F/H/J/L | 25-54 | [»] | ||||
1ZEI | X-ray | 1.90 | A/B/C/D/E/F | 25-54 | [»] | |
A/B/C/D/E/F | 88-108 | [»] | ||||
1ZNI | X-ray | 1.50 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
2EFA | neutron diffraction | 2.70 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
2G4M | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
2TCI | X-ray | 1.80 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
2ZPP | neutron diffraction | 2.50 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
3FHP | neutron diffraction | 2.00 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
3GKY | X-ray | 1.80 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
3INS | X-ray | 1.50 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
3MTH | X-ray | 1.90 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
3RTO | X-ray | 1.80 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
3T2A | X-ray | 2.10 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
4A7E | X-ray | 1.86 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
4INS | X-ray | 1.50 | A/C | 88-108 | [»] | |
B/D | 25-54 | [»] | ||||
5D52 | X-ray | 1.80 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
5D53 | X-ray | 1.50 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
5D54 | X-ray | 1.50 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
5D5E | X-ray | 2.41 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
5FB6 | X-ray | 1.90 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
5LIS | X-ray | 2.29 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
6INS | X-ray | 2.00 | E/F | 25-108 | [»] | |
6Z7Z | X-ray | 2.40 | E/G | 88-108 | [»] | |
F/H | 25-54 | [»] | ||||
7AC4 | X-ray | 1.46 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
7INS | X-ray | 2.00 | A/C/E | 88-108 | [»] | |
B/D/F | 25-54 | [»] | ||||
9INS | X-ray | 1.70 | A | 88-108 | [»] | |
B | 25-54 | [»] | ||||
AlphaFoldDBi | P01315 | |||||
BMRBi | P01315 | |||||
SASBDBi | P01315 | |||||
SMRi | P01315 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P01315, 1 interactor |
MINTi | P01315 |
STRINGi | 9823.ENSSSCP00000025428 |
Protein family/group databases
Allergomei | 2122, Sus s Insulin |
Proteomic databases
PaxDbi | P01315 |
Genome annotation databases
Organism-specific databases
CTDi | 3630 |
VGNCi | VGNC:99778, INS |
Phylogenomic databases
eggNOGi | ENOG502S5P5, Eukaryota |
GeneTreei | ENSGT00390000015440 |
InParanoidi | P01315 |
OMAi | IVEQCCN |
OrthoDBi | 1644517at2759 |
Miscellaneous databases
EvolutionaryTracei | P01315 |
Family and domain databases
CDDi | cd04367, IlGF_insulin_like, 1 hit |
InterProi | View protein in InterPro IPR004825, Insulin IPR016179, Insulin-like IPR036438, Insulin-like_sf IPR022353, Insulin_CS IPR022352, Insulin_family |
PANTHERi | PTHR11454, PTHR11454, 1 hit |
Pfami | View protein in Pfam PF00049, Insulin, 1 hit |
PRINTSi | PR00277, INSULIN PR00276, INSULINFAMLY |
SMARTi | View protein in SMART SM00078, IlGF, 1 hit |
SUPFAMi | SSF56994, SSF56994, 1 hit |
PROSITEi | View protein in PROSITE PS00262, INSULIN, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | INS_PIG | |
Accessioni | P01315Primary (citable) accession number: P01315 Secondary accession number(s): Q9TSJ5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | December 1, 2000 | |
Last modified: | May 25, 2022 | |
This is version 184 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries