P01325 (INS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Insulin-1

Cleaved into the following 2 chains:

1. Insulin-1 B chain
2. Insulin-1 A chain

Gene names

Name:	Ins1
Synonyms:	Ins-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	108 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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	endocrine pancreas development Traceable author statement. Source: Reactome glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glucose transport Traceable author statement PubMed 12297296. Source: MGI response to cAMP Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara secretory granule Traceable author statement. Source: Reactome
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-1 B chain Ref.4		PRO_0000015842
	Propeptide	57 – 85	29	C peptide		PRO_0000015843
	Peptide	88 – 108	21	Insulin-1 A chain		PRO_0000015844
Amino acid modifications
	Disulfide bond	31 ↔ 94		Interchain (between B and A chains)
	Disulfide bond	43 ↔ 107		Interchain (between B and A chains)
	Disulfide bond	93 ↔ 98
Experimental info
	Sequence conflict	37	1	E → K in BAB25058. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P01325 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: F63D9B7B896E0F88	FASTA	108	12,160
	10 20 30 40 50 60 MALLVHFLPL LALLALWEPK PTQAFVKQHL CGPHLVEALY LVCGERGFFY TPKSRREVED 70 80 90 100 PQVEQLELGG SPGDLQTLAL EVARQKRGIV DQCCTSICSL YQLENYCN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04725 Genomic DNA. Translation: CAA28434.1.
AK007482 mRNA. Translation: BAB25058.1.

IPI

IPI00134310.

PIR

INMS1. B26342.

RefSeq

NP_032412.3. NM_008386.3.

UniGene

Mm.46269.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L6Q	model	-	C	39-47	[»]

ProteinModelPortal

P01325.

SMR

P01325. Positions 25-108.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1489487.

Proteomic databases

PaxDb

P01325.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000039652; ENSMUSP00000049095; ENSMUSG00000035804.

GeneID

16333.

KEGG

mmu:16333.

Organism-specific databases

CTD

16333.

MGI

MGI:96572. Ins1.

Phylogenomic databases

eggNOG

NOG45999.

HOGENOM

HOG000261669.

HOVERGEN

HBG006137.

InParanoid

P01325.

KO

K04526.

OMA

VEQCCHN.

OrthoDB

EOG4RNB9Q.

Enzyme and pathway databases

Reactome

REACT_112621. Metabolism.
REACT_118324. Disease.
REACT_127416. Developmental Biology.
REACT_13641. Regulation of Beta-Cell Development.

Gene expression databases

ArrayExpress

P01325.

Bgee

P01325.

CleanEx

MM_INS1.

Genevestigator

P01325.

GermOnline

ENSMUSG00000035804. Mus musculus.

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

ChiTaRS

Ins1. mouse.

NextBio

289426.

SOURCE

Search...

Entry information

Entry name

INS1_MOUSE

Accession

Primary (citable) accession number: P01325
Secondary accession number(s): Q9D907

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	April 3, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program