ID   ALAT1_RAT               Reviewed;         496 AA.
AC   P25409; Q4V7F7;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 160.
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=Aat1, Gpt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Tanase S.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 2-496, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   ACETYLATION AT ALA-2.
RC   TISSUE=Liver;
RX   PubMed=2043642; DOI=10.1021/bi00238a031;
RA   Ishiguro M., Suzuki M., Takio K., Matsuzawa T., Titani K.;
RT   "Complete amino acid sequence of rat liver cytosolic alanine
RT   aminotransferase.";
RL   Biochemistry 30:6048-6053(1991).
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   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver, heart, skeletal muscle, etc.
CC   -!- INDUCTION: By glucocorticoids.
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; D10354; BAA01185.1; -; mRNA.
DR   EMBL; BC097937; AAH97937.1; -; mRNA.
DR   PIR; A39900; A39900.
DR   RefSeq; NP_112301.1; NM_031039.1.
DR   AlphaFoldDB; P25409; -.
DR   SMR; P25409; -.
DR   STRING; 10116.ENSRNOP00000044411; -.
DR   ChEMBL; CHEMBL3260; -.
DR   iPTMnet; P25409; -.
DR   PhosphoSitePlus; P25409; -.
DR   PaxDb; 10116-ENSRNOP00000044411; -.
DR   Ensembl; ENSRNOT00000050556.4; ENSRNOP00000044411.2; ENSRNOG00000033915.4.
DR   Ensembl; ENSRNOT00055047362; ENSRNOP00055038942; ENSRNOG00055027365.
DR   Ensembl; ENSRNOT00060047104; ENSRNOP00060039180; ENSRNOG00060027150.
DR   Ensembl; ENSRNOT00065052125; ENSRNOP00065042893; ENSRNOG00065030207.
DR   GeneID; 81670; -.
DR   KEGG; rno:81670; -.
DR   UCSC; RGD:621720; rat.
DR   AGR; RGD:621720; -.
DR   CTD; 2875; -.
DR   RGD; 621720; Gpt.
DR   eggNOG; KOG0258; Eukaryota.
DR   GeneTree; ENSGT00940000155265; -.
DR   HOGENOM; CLU_014254_3_1_1; -.
DR   InParanoid; P25409; -.
DR   OMA; ESNEWAL; -.
DR   OrthoDB; 5472891at2759; -.
DR   PhylomeDB; P25409; -.
DR   TreeFam; TF300839; -.
DR   Reactome; R-RNO-8964540; Alanine metabolism.
DR   SABIO-RK; P25409; -.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:P25409; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000033915; Expressed in jejunum and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; NAS:RGD.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IDA:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0042594; P:response to starvation; IEP:RGD.
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; P25409; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Aminotransferase; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2043642"
FT   CHAIN           2..496
FT                   /note="Alanine aminotransferase 1"
FT                   /id="PRO_0000123936"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:2043642"
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;  55110 MW;  7A4714E94146ABF8 CRC64;
     MASRVNDQSQ ASRNGLKGKV LTLDTMNPCV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF
     TEVIRANIGD AQAMGQRPIT FFRQVLALCV YPNLLSSPDF PEDAKRRAER ILQACGGHSL
     GAYSISSGIQ PIREDVAQYI ERRDGGIPAD PNNIFLSTGA SDAIVTMLKL LVSGEGRART
     GVLIPIPQYP LYSAALAELD AVQVDYYLDE ERAWALDIAE LRRALCQARD RCCPRVLCVI
     NPGNPTGQVQ TRECIEAVIR FAFKEGLFLM ADEVYQDNVY AEGSQFHSFK KVLMEMGPPY
     STQQELASFH SVSKGYMGEC GFRGGYVEVV NMDAEVQKQM GKLMSVRLCP PVPGQALMDM
     VVSPPTPSEP SFKQFQAERQ EVLAELAAKA KLTEQVFNEA PGIRCNPVQG AMYSFPQVQL
     PLKAVQRAQE LGLAPDMFFC LCLLEETGIC VVPGSGFGQQ EGTYHFRMTI LPPMEKLRLL
     LEKLSHFHAK FTHEYS
//