INS1_MOUSE
ID INS1_MOUSE Reviewed; 108 AA.
AC P01325; Q545I7; Q9D907;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Insulin-1;
DE Contains:
DE RecName: Full=Insulin-1 B chain;
DE Contains:
DE RecName: Full=Insulin-1 A chain;
DE Flags: Precursor;
GN Name=Ins1; Synonyms=Ins-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3104603; DOI=10.1007/bf02100639;
RA Wentworth B.M., Schaefer I.M., Villa-Komaroff L., Chirgwin J.M.;
RT "Characterization of the two nonallelic genes encoding mouse
RT preproinsulin.";
RL J. Mol. Evol. 23:305-312(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NON/ShiLtJ;
RX PubMed=2397023; DOI=10.1677/jme.0.0050061;
RA Sawa T., Ohgaku S., Morioka H., Yano S.;
RT "Molecular cloning and DNA sequence analysis of preproinsulin genes in the
RT NON mouse, an animal model of human non-obese, non-insulin-dependent
RT diabetes mellitus.";
RL J. Mol. Endocrinol. 5:61-67(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BTBR T+ tf/J;
RX PubMed=16682971; DOI=10.1038/ng1796;
RA Clee S.M., Yandell B.S., Schueler K.M., Rabaglia M.E., Richards O.C.,
RA Raines S.M., Kabara E.A., Klass D.M., Mui E.T.-K., Stapleton D.S.,
RA Gray-Keller M.P., Young M.B., Stoehr J.P., Lan H., Boronenkov I.,
RA Raess P.W., Flowers M.T., Attie A.D.;
RT "Positional cloning of Sorcs1, a type 2 diabetes quantitative trait
RT locus.";
RL Nat. Genet. 38:688-693(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, and Pancreas islet cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 25-54 AND 88-108.
RX PubMed=5063718; DOI=10.1515/bchm2.1972.353.1.451;
RA Buenzli H.F., Glatthaar B., Kunz P., Muelhaupt E., Humbel R.E.;
RT "Amino acid sequence of the two insulins from mouse (Maus musculus).";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:451-458(1972).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Insulin decreases blood glucose concentration. It increases
CC cell permeability to monosaccharides, amino acids and fatty acids. It
CC accelerates glycolysis, the pentose phosphate cycle, and glycogen
CC synthesis in liver.
CC -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC disulfide bonds. {ECO:0000250|UniProtKB:P01308}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; X04725; CAA28434.1; -; Genomic_DNA.
DR EMBL; DQ479923; ABF48502.1; -; Genomic_DNA.
DR EMBL; AK007345; BAB24974.1; -; mRNA.
DR EMBL; AK007482; BAB25058.1; -; mRNA.
DR EMBL; AK008358; BAB25628.1; -; mRNA.
DR EMBL; AK148541; BAE28611.1; -; mRNA.
DR EMBL; AC163452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466585; EDL01682.1; -; Genomic_DNA.
DR EMBL; CH466585; EDL01683.1; -; Genomic_DNA.
DR EMBL; BC098468; AAH98468.1; -; mRNA.
DR EMBL; BC145868; AAI45869.1; -; mRNA.
DR EMBL; BC145870; AAI45871.1; -; mRNA.
DR CCDS; CCDS29898.1; -.
DR PIR; B26342; INMS1.
DR RefSeq; NP_032412.3; NM_008386.4.
DR PDB; 3WS3; X-ray; 2.34 A; E/F=101-107.
DR PDBsum; 3WS3; -.
DR AlphaFoldDB; P01325; -.
DR SMR; P01325; -.
DR BioGRID; 200771; 1.
DR MINT; P01325; -.
DR STRING; 10090.ENSMUSP00000049095; -.
DR PaxDb; P01325; -.
DR PRIDE; P01325; -.
DR ProteomicsDB; 267143; -.
DR DNASU; 16333; -.
DR Ensembl; ENSMUST00000039652; ENSMUSP00000049095; ENSMUSG00000035804.
DR GeneID; 16333; -.
DR KEGG; mmu:16333; -.
DR UCSC; uc008hwd.1; mouse.
DR CTD; 16333; -.
DR MGI; MGI:96572; Ins1.
DR VEuPathDB; HostDB:ENSMUSG00000035804; -.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR GeneTree; ENSGT00390000015440; -.
DR HOGENOM; CLU_140421_1_0_1; -.
DR InParanoid; P01325; -.
DR OMA; IVEQCCN; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P01325; -.
DR TreeFam; TF332820; -.
DR BioGRID-ORCS; 16333; 2 hits in 71 CRISPR screens.
DR PRO; PR:P01325; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P01325; protein.
DR Bgee; ENSMUSG00000035804; Expressed in islet of Langerhans and 52 other tissues.
DR Genevisible; P01325; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1904659; P:glucose transmembrane transport; TAS:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR CDD; cd04367; IlGF_insulin_like; 1.
DR InterPro; IPR004825; Insulin.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR022352; Insulin_family.
DR PANTHER; PTHR11454; PTHR11454; 1.
DR Pfam; PF00049; Insulin; 1.
DR PRINTS; PR00277; INSULIN.
DR PRINTS; PR00276; INSULINFAMLY.
DR SMART; SM00078; IlGF; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:5063718"
FT PEPTIDE 25..54
FT /note="Insulin-1 B chain"
FT /id="PRO_0000015842"
FT PROPEP 57..85
FT /note="C peptide"
FT /id="PRO_0000015843"
FT PEPTIDE 88..108
FT /note="Insulin-1 A chain"
FT /id="PRO_0000015844"
FT DISULFID 31..94
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 43..107
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT DISULFID 93..98
FT /evidence="ECO:0000250|UniProtKB:P01308"
FT CONFLICT 37
FT /note="E -> K (in Ref. 4; BAB25058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 108 AA; 12160 MW; F63D9B7B896E0F88 CRC64;
MALLVHFLPL LALLALWEPK PTQAFVKQHL CGPHLVEALY LVCGERGFFY TPKSRREVED
PQVEQLELGG SPGDLQTLAL EVARQKRGIV DQCCTSICSL YQLENYCN
