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   24-JAN-2024, entry version 153.
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   GlyGen; Q8QZR5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8QZR5; -.
DR   PhosphoSitePlus; Q8QZR5; -.
DR   SwissPalm; Q8QZR5; -.
DR   jPOST; Q8QZR5; -.
DR   MaxQB; Q8QZR5; -.
DR   PaxDb; 10090-ENSMUSP00000023203; -.
DR   ProteomicsDB; 282072; -.
DR   Antibodypedia; 14920; 436 antibodies from 31 providers.
DR   DNASU; 76282; -.
DR   Ensembl; ENSMUST00000023203.6; ENSMUSP00000023203.5; ENSMUSG00000022546.6.
DR   Ensembl; ENSMUST00000229679.2; ENSMUSP00000155553.2; ENSMUSG00000022546.6.
DR   GeneID; 76282; -.
DR   KEGG; mmu:76282; -.
DR   UCSC; uc007wls.1; mouse.
DR   AGR; MGI:95802; -.
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; ESNEWAL; -.
DR   OrthoDB; 5472891at2759; -.
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 61 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 215 other cell types or tissues.
DR   ExpressionAtlas; Q8QZR5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF308; ALANINE AMINOTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q8QZR5; MM.
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
//