BCAT1_MOUSE
ID BCAT1_MOUSE Reviewed; 386 AA.
AC P24288; Q7TMT2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE Short=BCAT(c);
DE EC=2.6.1.42;
DE AltName: Full=Protein ECA39;
GN Name=Bcat1; Synonyms=Eca39;
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].
RX PubMed=8692959; DOI=10.1073/pnas.93.14.7143;
RA Schuldiner O., Eden A., Ben-Yosef T., Yanuka O., Simchen G., Benvenisty N.;
RT "ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S
RT cell cycle regulation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7143-7148(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129;
RX PubMed=2251142; DOI=10.1093/nar/18.22.6709;
RA Niwa O., Kumazaki T., Tsukiyama T., Soma G., Miyajima N., Yokoro K.;
RT "A cDNA clone overexpressed and amplified in a mouse teratocarcinoma
RT line.";
RL Nucleic Acids Res. 18:6709-6709(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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, and Kidney;
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 first reaction in the catabolism of the
CC essential branched chain amino acids leucine, isoleucine, and valine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in brain and kidney. Overexpressed in
CC MYC-induced brain tumors, lymphomas, as well as in a teratocarcinoma
CC cell line.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at day 9 of embryogenesis.
CC Expression decreases to moderate levels through day 13. In the
CC developing embryo, expressed in the brain, somites and mesenophric
CC tubules.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35543.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U42443; AAB05673.1; -; mRNA.
DR EMBL; X17502; CAA35543.1; ALT_FRAME; mRNA.
DR EMBL; BC053706; AAH53706.1; -; mRNA.
DR CCDS; CCDS39703.1; -.
DR PIR; S13108; S13108.
DR RefSeq; NP_031558.3; NM_007532.5.
DR AlphaFoldDB; P24288; -.
DR SMR; P24288; -.
DR BioGRID; 198311; 8.
DR STRING; 10090.ENSMUSP00000032402; -.
DR iPTMnet; P24288; -.
DR PhosphoSitePlus; P24288; -.
DR SwissPalm; P24288; -.
DR EPD; P24288; -.
DR jPOST; P24288; -.
DR PaxDb; P24288; -.
DR PeptideAtlas; P24288; -.
DR PRIDE; P24288; -.
DR ProteomicsDB; 277116; -.
DR Antibodypedia; 24197; 382 antibodies from 32 providers.
DR DNASU; 12035; -.
DR Ensembl; ENSMUST00000111742; ENSMUSP00000107371; ENSMUSG00000030268.
DR GeneID; 12035; -.
DR KEGG; mmu:12035; -.
DR UCSC; uc009eqt.2; mouse.
DR CTD; 586; -.
DR MGI; MGI:104861; Bcat1.
DR VEuPathDB; HostDB:ENSMUSG00000030268; -.
DR eggNOG; KOG0975; Eukaryota.
DR GeneTree; ENSGT00390000009532; -.
DR HOGENOM; CLU_031922_0_3_1; -.
DR InParanoid; P24288; -.
DR OMA; LTEVFAC; -.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR BioGRID-ORCS; 12035; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Bcat1; mouse.
DR PRO; PR:P24288; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P24288; protein.
DR Bgee; ENSMUSG00000030268; Expressed in cumulus cell and 237 other tissues.
DR ExpressionAtlas; P24288; baseline and differential.
DR Genevisible; P24288; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IDA:MGI.
DR GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR11825; PTHR11825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Lipid metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..386
FT /note="Branched-chain-amino-acid aminotransferase,
FT cytosolic"
FT /id="PRO_0000103293"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54687"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 238
FT /note="V -> A (in Ref. 3; AAH53706)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="L -> P (in Ref. 3; AAH53706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 42791 MW; 8185C4C227843B5E CRC64;
MKDCSNGCSA PFAGERGSEE VAETFRAKDL IITPATVLKE KPDPDSLVFG ATFTDHMLTV
EWSSASGWEK PHIKPFGNLP IHPAASVLHY AVELFEGLKA FRGVDNKIRL FRPDLNMDRM
CRSAVRTTLP MFDKEELLKC ILQLLQIDQE WVPYSTSASL YIRPTFIGTE PSLGVKKPSK
ALLFVILSPV GPYFSSGSFT PVSLWANPKY IRAWKGGTGD CKMGGNYGAS LLAQCEAVEN
GCQQVLWLYG KDNQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RQSILELAQQ
WGEFKVCERH LTMDDLATAL EGNRVKEMFG SGTACVVCPV SDILYKGQML HIPTMENGPK
LASRILGKLT DIQYGRVESD WTIELP
