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Protein

Insulin-1

Gene

Ins1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Enzyme and pathway databases

ReactomeiR-MMU-210745. Regulation of gene expression in beta cells.
R-MMU-264876. Insulin processing.
R-MMU-422085. Synthesis, secretion, and deacylation of Ghrelin.
R-MMU-422356. Regulation of insulin secretion.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-74713. IRS activation.
R-MMU-74749. Signal attenuation.
R-MMU-74751. Insulin receptor signalling cascade.
R-MMU-74752. Signaling by Insulin receptor.
R-MMU-77387. Insulin receptor recycling.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-1
Cleaved into the following 2 chains:
Gene namesi
Name:Ins1
Synonyms:Ins-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:96572. Ins1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: Ensembl
  • secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Peptidei25 – 5430Insulin-1 B chainPRO_0000015842Add
BLAST
Propeptidei57 – 8529C peptidePRO_0000015843Add
BLAST
Peptidei88 – 10821Insulin-1 A chainPRO_0000015844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 94Interchain (between B and A chains)By similarity
Disulfide bondi43 ↔ 107Interchain (between B and A chains)By similarity
Disulfide bondi93 ↔ 98By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP01325.
PRIDEiP01325.

Expressioni

Gene expression databases

BgeeiP01325.
CleanExiMM_INS1.
ExpressionAtlasiP01325. baseline and differential.
GenevisibleiP01325. MM.

Interactioni

Subunit structurei

Heterodimer of a B chain and an A chain linked by two disulfide bonds.By similarity

Protein-protein interaction databases

MINTiMINT-1489487.
STRINGi10090.ENSMUSP00000049095.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6Qmodel-C39-47[»]
3WS3X-ray2.34E/F101-107[»]
ProteinModelPortaliP01325.
SMRiP01325. Positions 25-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J0XC. Eukaryota.
ENOG4111VJB. LUCA.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01325.
KOiK04526.
OMAiDPQVGQV.
OrthoDBiEOG7TF7CG.
PhylomeDBiP01325.
TreeFamiTF332820.

Family and domain databases

Gene3Di1.10.100.10. 1 hit.
InterProiIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLVHFLPL LALLALWEPK PTQAFVKQHL CGPHLVEALY LVCGERGFFY
60 70 80 90 100
TPKSRREVED PQVEQLELGG SPGDLQTLAL EVARQKRGIV DQCCTSICSL

YQLENYCN
Length:108
Mass (Da):12,160
Last modified:August 13, 1987 - v1
Checksum:iF63D9B7B896E0F88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371E → K in BAB25058 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04725 Genomic DNA. Translation: CAA28434.1.
AK007482 mRNA. Translation: BAB25058.1.
CCDSiCCDS29898.1.
PIRiB26342. INMS1.
RefSeqiNP_032412.3. NM_008386.4.
UniGeneiMm.46269.

Genome annotation databases

EnsembliENSMUST00000039652; ENSMUSP00000049095; ENSMUSG00000035804.
GeneIDi16333.
KEGGimmu:16333.
UCSCiuc008hwd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04725 Genomic DNA. Translation: CAA28434.1.
AK007482 mRNA. Translation: BAB25058.1.
CCDSiCCDS29898.1.
PIRiB26342. INMS1.
RefSeqiNP_032412.3. NM_008386.4.
UniGeneiMm.46269.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6Qmodel-C39-47[»]
3WS3X-ray2.34E/F101-107[»]
ProteinModelPortaliP01325.
SMRiP01325. Positions 25-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1489487.
STRINGi10090.ENSMUSP00000049095.

Proteomic databases

PaxDbiP01325.
PRIDEiP01325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039652; ENSMUSP00000049095; ENSMUSG00000035804.
GeneIDi16333.
KEGGimmu:16333.
UCSCiuc008hwd.1. mouse.

Organism-specific databases

CTDi16333.
MGIiMGI:96572. Ins1.

Phylogenomic databases

eggNOGiENOG410J0XC. Eukaryota.
ENOG4111VJB. LUCA.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01325.
KOiK04526.
OMAiDPQVGQV.
OrthoDBiEOG7TF7CG.
PhylomeDBiP01325.
TreeFamiTF332820.

Enzyme and pathway databases

ReactomeiR-MMU-210745. Regulation of gene expression in beta cells.
R-MMU-264876. Insulin processing.
R-MMU-422085. Synthesis, secretion, and deacylation of Ghrelin.
R-MMU-422356. Regulation of insulin secretion.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-MMU-74713. IRS activation.
R-MMU-74749. Signal attenuation.
R-MMU-74751. Insulin receptor signalling cascade.
R-MMU-74752. Signaling by Insulin receptor.
R-MMU-77387. Insulin receptor recycling.

Miscellaneous databases

PROiP01325.
SOURCEiSearch...

Gene expression databases

BgeeiP01325.
CleanExiMM_INS1.
ExpressionAtlasiP01325. baseline and differential.
GenevisibleiP01325. MM.

Family and domain databases

Gene3Di1.10.100.10. 1 hit.
InterProiIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the two nonallelic genes encoding mouse preproinsulin."
    Wentworth B.M., Schaefer I.M., Villa-Komaroff L., Chirgwin J.M.
    J. Mol. Evol. 23:305-312(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and DNA sequence analysis of preproinsulin genes in the NON mouse, an animal model of human non-obese, non-insulin-dependent diabetes mellitus."
    Sawa T., Ohgaku S., Morioka H., Yano S.
    J. Mol. Endocrinol. 5:61-67(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: NON.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  4. "Amino acid sequence of the two insulins from mouse (Maus musculus)."
    Buenzli H.F., Glatthaar B., Kunz P., Muelhaupt E., Humbel R.E.
    Hoppe-Seyler's Z. Physiol. Chem. 353:451-458(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-54 AND 88-108.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas.

Entry informationi

Entry nameiINS1_MOUSE
AccessioniPrimary (citable) accession number: P01325
Secondary accession number(s): Q9D907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: June 8, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.