ALAT1_MOUSE
ID ALAT1_MOUSE Reviewed; 496 AA.
AC Q8QZR5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alanine aminotransferase 1;
DE Short=ALT1;
DE EC=2.6.1.2;
DE AltName: Full=Glutamate pyruvate transaminase 1;
DE Short=GPT 1;
DE AltName: Full=Glutamic--alanine transaminase 1;
DE AltName: Full=Glutamic--pyruvic transaminase 1;
GN Name=Gpt; Synonyms=Gpt1;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15122758; DOI=10.1002/hep.20182;
RA Jadhao S.B., Yang R.-Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R.,
RA Gong D.-W.;
RT "Murine alanine aminotransferase: cDNA cloning, functional expression, and
RT differential gene regulation in mouse fatty liver.";
RL Hepatology 39:1297-1302(2004).
RN [2]
RP ERRATUM OF PUBMED:15122758.
RA Jadhao S.B., Yang R.-Z., Lin Q., Hu H., Anania F.A., Shuldiner A.R.,
RA Gong D.-W.;
RL Hepatology 40:269-269(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC 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: Catalyzes the reversible transamination between alanine and
CC 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular
CC nitrogen metabolism and also in liver gluconeogenesis starting with
CC precursors transported from skeletal muscles (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC pathway; pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in liver, intestine, colon and
CC white adipose tissue. {ECO:0000269|PubMed:15122758}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
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DR EMBL; BC022625; AAH22625.1; -; mRNA.
DR EMBL; BC026846; AAH26846.1; -; mRNA.
DR CCDS; CCDS27586.1; -.
DR RefSeq; NP_877957.1; NM_182805.3.
DR AlphaFoldDB; Q8QZR5; -.
DR SMR; Q8QZR5; -.
DR BioGRID; 218060; 1.
DR STRING; 10090.ENSMUSP00000023203; -.
DR iPTMnet; Q8QZR5; -.
DR PhosphoSitePlus; Q8QZR5; -.
DR SwissPalm; Q8QZR5; -.
DR jPOST; Q8QZR5; -.
DR MaxQB; Q8QZR5; -.
DR PaxDb; Q8QZR5; -.
DR PRIDE; Q8QZR5; -.
DR ProteomicsDB; 282072; -.
DR Antibodypedia; 14920; 409 antibodies from 31 providers.
DR DNASU; 76282; -.
DR Ensembl; ENSMUST00000023203; ENSMUSP00000023203; ENSMUSG00000022546.
DR Ensembl; ENSMUST00000229679; ENSMUSP00000155553; ENSMUSG00000022546.
DR GeneID; 76282; -.
DR KEGG; mmu:76282; -.
DR UCSC; uc007wls.1; mouse.
DR CTD; 2875; -.
DR MGI; MGI:95802; Gpt.
DR VEuPathDB; HostDB:ENSMUSG00000022546; -.
DR eggNOG; KOG0258; Eukaryota.
DR GeneTree; ENSGT00940000155265; -.
DR HOGENOM; CLU_014254_3_1_1; -.
DR InParanoid; Q8QZR5; -.
DR OMA; LDEEHAW; -.
DR OrthoDB; 477122at2759; -.
DR PhylomeDB; Q8QZR5; -.
DR TreeFam; TF300839; -.
DR BRENDA; 2.6.1.2; 3474.
DR Reactome; R-MMU-8964540; Alanine metabolism.
DR UniPathway; UPA00528; UER00586.
DR BioGRID-ORCS; 76282; 1 hit in 58 CRISPR screens.
DR PRO; PR:Q8QZR5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8QZR5; protein.
DR Bgee; ENSMUSG00000022546; Expressed in left lobe of liver and 212 other tissues.
DR ExpressionAtlas; Q8QZR5; baseline and differential.
DR Genevisible; Q8QZR5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; ISO:MGI.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR045088; ALAT1/2-like.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11751; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Cytoplasm; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P24298"
FT CHAIN 2..496
FT /note="Alanine aminotransferase 1"
FT /id="PRO_0000123934"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P24298"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P24298"
FT MOD_RES 314
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 496 AA; 55143 MW; 386AD33881DC7083 CRC64;
MASQRNDRIQ ASRNGLKGKV LTLDTMNPCV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF
TEVIRANIGD AQAMGQRPIT FFRQVLALCV YPNLLSSPDF PEDAKRRAER ILQACGGHSL
GAYSISSGIQ PIREDVAQYI ERRDGGIPAD PNNIFLSTGA SDAIVTMLKL LVAGEGRART
GVLIPIPQYP LYSAALAELD AVQVDYYLDE ERAWALDIAE LRRALCQARD RCCPRVLCVI
NPGNPTGQVQ TRECIEAVIR FAFEEGLFLM ADEVYQDNVY AEGSQFHSFK KVLTEMGPPY
ATQQELASFH SVSKGYMGEC GFRGGYVEVV NMDAEVQKQM AKLMSVRLCP PVPGQALMGM
VVSPPTPSEP SFKQFQAERQ EVLAELAAKA KLTEQVFNEA PGIRCNPVQG AMYSFPQIQL
PLKAVQRAQD LGLAPDMFFC LCLLEETGIC VVPGSGFGQQ EGTYHFRMTI LPPMEKLRVL
LEKLRHFHAK FTHEYS
