ATTY_MOUSE
ID ATTY_MOUSE Reviewed; 454 AA.
AC Q8QZR1; Q3UER7; Q8BTI1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Tyrosine aminotransferase;
DE Short=TAT;
DE EC=2.6.1.5;
DE AltName: Full=L-tyrosine:2-oxoglutarate aminotransferase;
GN Name=Tat;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 41-442, CATALYTIC ACTIVITY,
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21153519; DOI=10.1007/s13238-010-0128-5;
RA Mehere P., Han Q., Lemkul J.A., Vavricka C.J., Robinson H., Bevan D.R.,
RA Li J.;
RT "Tyrosine aminotransferase: biochemical and structural properties and
RT molecular dynamics simulations.";
RL Protein Cell 1:1023-1032(2010).
CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction,
CC using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has
CC much lower affinity and transaminase activity for phenylalanine.
CC {ECO:0000269|PubMed:21153519}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC Evidence={ECO:0000269|PubMed:21153519};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:21153519};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for tyrosine {ECO:0000269|PubMed:21153519};
CC KM=4.9 mM for glutamate {ECO:0000269|PubMed:21153519};
CC KM=11.4 mM for phenylalanine {ECO:0000269|PubMed:21153519};
CC KM=1.8 mM for 2-oxoglutarate {ECO:0000269|PubMed:21153519};
CC KM=0.7 mM for p-hydroxyphenylpyruvate {ECO:0000269|PubMed:21153519};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:21153519};
CC Temperature dependence:
CC Optimum temperature is 55-70 degrees Celsius.
CC {ECO:0000269|PubMed:21153519};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AK090244; BAC41146.1; -; mRNA.
DR EMBL; AK149383; BAE28844.1; -; mRNA.
DR EMBL; BC023949; AAH23949.1; -; mRNA.
DR EMBL; BC024120; AAH24120.1; -; mRNA.
DR EMBL; BC024264; AAH24264.1; -; mRNA.
DR EMBL; BC025934; AAH25934.1; -; mRNA.
DR EMBL; BC028821; AAH28821.1; -; mRNA.
DR EMBL; BC030728; AAH30728.1; -; mRNA.
DR EMBL; BC030729; AAH30729.1; -; mRNA.
DR EMBL; BC037526; AAH37526.1; -; mRNA.
DR CCDS; CCDS22658.1; -.
DR RefSeq; NP_666326.1; NM_146214.3.
DR PDB; 3PDX; X-ray; 2.91 A; A=41-442.
DR PDBsum; 3PDX; -.
DR AlphaFoldDB; Q8QZR1; -.
DR SMR; Q8QZR1; -.
DR STRING; 10090.ENSMUSP00000001720; -.
DR iPTMnet; Q8QZR1; -.
DR PhosphoSitePlus; Q8QZR1; -.
DR SwissPalm; Q8QZR1; -.
DR jPOST; Q8QZR1; -.
DR MaxQB; Q8QZR1; -.
DR PaxDb; Q8QZR1; -.
DR PRIDE; Q8QZR1; -.
DR ProteomicsDB; 273588; -.
DR Antibodypedia; 30099; 281 antibodies from 28 providers.
DR DNASU; 234724; -.
DR Ensembl; ENSMUST00000001720; ENSMUSP00000001720; ENSMUSG00000001670.
DR GeneID; 234724; -.
DR KEGG; mmu:234724; -.
DR UCSC; uc009njs.2; mouse.
DR CTD; 6898; -.
DR MGI; MGI:98487; Tat.
DR VEuPathDB; HostDB:ENSMUSG00000001670; -.
DR eggNOG; KOG0259; Eukaryota.
DR GeneTree; ENSGT00940000156704; -.
DR InParanoid; Q8QZR1; -.
DR OMA; WRMGWII; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q8QZR1; -.
DR TreeFam; TF105999; -.
DR BRENDA; 2.6.1.5; 3474.
DR Reactome; R-MMU-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00338.
DR BioGRID-ORCS; 234724; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Tat; mouse.
DR EvolutionaryTrace; Q8QZR1; -.
DR PRO; PR:Q8QZR1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8QZR1; protein.
DR Bgee; ENSMUSG00000001670; Expressed in left lobe of liver and 31 other tissues.
DR ExpressionAtlas; Q8QZR1; baseline and differential.
DR Genevisible; Q8QZR1; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISO:MGI.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
DR GO; GO:0046689; P:response to mercury ion; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0006572; P:tyrosine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011715; Tyr_aminoTrfase_ubiquitination.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR InterPro; IPR005957; Tyrosine_aminoTrfase.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF07706; TAT_ubiq; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01264; tyr_amTase_E; 1.
DR TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminotransferase; Phenylalanine catabolism;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase;
KW Tyrosine catabolism.
FT CHAIN 1..454
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000123888"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P04694"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17735"
FT CONFLICT 234
FT /note="L -> W (in Ref. 1; BAC41146)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="G -> V (in Ref. 1; BAC41146)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="I -> M (in Ref. 1; BAC41146)"
FT /evidence="ECO:0000305"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3PDX"
FT TURN 190..194
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:3PDX"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:3PDX"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3PDX"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:3PDX"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 336..359
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 389..400
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:3PDX"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:3PDX"
FT HELIX 424..438
FT /evidence="ECO:0007829|PDB:3PDX"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:3PDX"
SQ SEQUENCE 454 AA; 50565 MW; CDB6E1E6CDB5DC7D CRC64;
MDSYVIQTNV NDSLPSVLDV RVNIGGRSSV QGRAKGRKAR WNVRPSDMSN KTFNPIRAIV
DNMKVKPNPN KTVISLSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSIGYLSSRE
EVASYYHCPE APLEAKDVIL TSGCSQAIEL CLAVLANPGQ NILIPRPGFS LYRTLAESMG
IEVKLYNLLP EKSWEIDLKQ LESLIDEKTA CLVVNNPSNP CGSVFSKRHL QKILAVAERQ
CVPILADEIY GDMVFSDCKY EPMATLSTNV PILSCGGLAK RWLVPGWRLG WILIHDRRDI
FGNEIRDGLV KLSQRILGPC TIVQGALKSI LQRTPQEFYQ DTLSFLKSNA DLCYGALSAI
PGLQPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLIAEQ SVHCLPATCF EYPNFFRVVI
TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE ECDK
