AATC2_MOUSE
ID AATC2_MOUSE Reviewed; 404 AA.
AC Q7TSV6; Q9D9F3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative aspartate aminotransferase, cytoplasmic 2;
DE EC=2.6.1.1;
DE AltName: Full=Glutamate oxaloacetate transaminase 1-like protein 1;
DE AltName: Full=Transaminase A-like protein 1;
GN Name=Got1l1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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] (ISOFORM 1).
RC TISSUE=Brain;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TSV6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSV6-2; Sequence=VSP_033430;
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: The residues that bind the substrate in other aspartate
CC aminotransferases are not conserved. {ECO:0000305}.
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DR EMBL; AK006984; BAB24820.1; -; mRNA.
DR EMBL; BC052754; AAH52754.1; -; mRNA.
DR CCDS; CCDS22212.1; -. [Q7TSV6-1]
DR RefSeq; NP_083950.1; NM_029674.1. [Q7TSV6-1]
DR RefSeq; XP_006509274.1; XM_006509211.3. [Q7TSV6-1]
DR AlphaFoldDB; Q7TSV6; -.
DR SMR; Q7TSV6; -.
DR STRING; 10090.ENSMUSP00000041337; -.
DR MaxQB; Q7TSV6; -.
DR PaxDb; Q7TSV6; -.
DR PRIDE; Q7TSV6; -.
DR ProteomicsDB; 285699; -. [Q7TSV6-1]
DR Antibodypedia; 23475; 79 antibodies from 19 providers.
DR DNASU; 76615; -.
DR Ensembl; ENSMUST00000038174; ENSMUSP00000041337; ENSMUSG00000039720. [Q7TSV6-1]
DR GeneID; 76615; -.
DR KEGG; mmu:76615; -.
DR UCSC; uc009lic.1; mouse. [Q7TSV6-1]
DR UCSC; uc009lid.1; mouse. [Q7TSV6-2]
DR CTD; 137362; -.
DR MGI; MGI:1923865; Got1l1.
DR VEuPathDB; HostDB:ENSMUSG00000039720; -.
DR eggNOG; KOG1412; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; Q7TSV6; -.
DR OMA; LAYKVCM; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; Q7TSV6; -.
DR TreeFam; TF314089; -.
DR BRENDA; 5.1.1.13; 3474.
DR BioGRID-ORCS; 76615; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Got1l1; mouse.
DR PRO; PR:Q7TSV6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q7TSV6; protein.
DR Bgee; ENSMUSG00000039720; Expressed in spermatid and 162 other tissues.
DR ExpressionAtlas; Q7TSV6; baseline and differential.
DR Genevisible; Q7TSV6; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Putative aspartate aminotransferase, cytoplasmic 2"
FT /id="PRO_0000333000"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 255..404
FT /note="DEGVGILVVAALSNQHLLCVLSQLMDYVQALWGNPPATGARIITSILCNPAL
FT FGEWKQSLKGVVENMMLIKEKVKEKLRLLGTPGSWDHITRQSGTHGYLGLTYQQVEFLV
FT KKKHIYLPKTSRINFTCINARNIDYITQSIHEAVMLTEG -> GLLWVEGREK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033430"
SQ SEQUENCE 404 AA; 45458 MW; 3BFF5A2D3E790329 CRC64;
MTSLSVFRDV PTAQKLEGSL LKIYRQDGYP SKLFLAYKVC MTEEGHPWVS LVVHKTRLQI
AEDPSLDYEY LPLVGLKSFI QSSLELLFGK HSEAIAEKRV GGVHIVGESG AFQLGAQFLK
TWRKNVKIVC IVSCQKEQCG LIFQDMGFIV YEYSIWNASD LCSDPSMFVE VLQHIPVGSI
LVIGNITDCK FTQNQWTKLM SIIKSKQIFP FFDIPCQGLS TGDLEEDTKI LQYFVSLGLE
FFCSQSLSKN FGIYDEGVGI LVVAALSNQH LLCVLSQLMD YVQALWGNPP ATGARIITSI
LCNPALFGEW KQSLKGVVEN MMLIKEKVKE KLRLLGTPGS WDHITRQSGT HGYLGLTYQQ
VEFLVKKKHI YLPKTSRINF TCINARNIDY ITQSIHEAVM LTEG
