ALAT1_RAT
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 03-AUG-2022, 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=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; P25409; -.
DR PRIDE; P25409; -.
DR Ensembl; ENSRNOT00000050556; ENSRNOP00000044411; ENSRNOG00000033915.
DR GeneID; 81670; -.
DR KEGG; rno:81670; -.
DR UCSC; RGD:621720; rat.
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; LDEEHAW; -.
DR OrthoDB; 477122at2759; -.
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 tissues.
DR Genevisible; P25409; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; NAS:RGD.
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:0042594; P:response to starvation; IEP:RGD.
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; 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
