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4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (GABA-T) (L-AIBAT)

 GABT_MOUSE              Reviewed;         500 AA.
P61922; Q8BZA3;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
25-OCT-2017, entry version 125.
RecName: Full=4-aminobutyrate aminotransferase, mitochondrial;
EC=2.6.1.19;
AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
EC=2.6.1.22;
AltName: Full=GABA aminotransferase;
Short=GABA-AT;
AltName: Full=Gamma-amino-N-butyrate transaminase;
Short=GABA transaminase;
Short=GABA-T;
AltName: Full=L-AIBAT;
Flags: Precursor;
Name=Abat; Synonyms=Gabat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 35-47; 61-173; 221-231; 236-279; 286-310; 318-337;
368-410; 414-432; 437-450 AND 461-470, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Friebe K., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-231; LYS-252 AND LYS-413,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-279; LYS-318;
LYS-413; LYS-452 AND LYS-470, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-
beta-aminoisobutyrate to succinate semialdehyde and methylmalonate
semialdehyde, respectively. Can also convert delta-aminovalerate
and beta-alanine (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 4-aminobutanoate + 2-oxoglutarate = succinate
semialdehyde + L-glutamate.
-!- CATALYTIC ACTIVITY: (S)-3-amino-2-methylpropanoate + 2-
oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P80147};
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250|UniProtKB:P80147};
Note=Binds 1 [2Fe-2S] cluster per homodimer.
{ECO:0000250|UniProtKB:P80147};
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P61922-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=P61922-2; Sequence=VSP_012005;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BC058079; AAH58079.1; -; mRNA.
EMBL; BC058521; AAH58521.1; -; mRNA.
EMBL; AK036128; BAC29312.1; -; mRNA.
CCDS; CCDS27939.1; -. [P61922-1]
CCDS; CCDS49754.1; -. [P61922-2]
RefSeq; NP_001164449.1; NM_001170978.1. [P61922-2]
RefSeq; NP_766549.2; NM_172961.3. [P61922-1]
UniGene; Mm.259315; -.
ProteinModelPortal; P61922; -.
SMR; P61922; -.
IntAct; P61922; 2.
MINT; MINT-1842478; -.
STRING; 10090.ENSMUSP00000063548; -.
iPTMnet; P61922; -.
PhosphoSitePlus; P61922; -.
SwissPalm; P61922; -.
REPRODUCTION-2DPAGE; IPI00407499; -.
MaxQB; P61922; -.
PaxDb; P61922; -.
PeptideAtlas; P61922; -.
PRIDE; P61922; -.
Ensembl; ENSMUST00000065987; ENSMUSP00000063548; ENSMUSG00000057880. [P61922-1]
Ensembl; ENSMUST00000115839; ENSMUSP00000111505; ENSMUSG00000057880. [P61922-2]
GeneID; 268860; -.
KEGG; mmu:268860; -.
UCSC; uc007yco.2; mouse. [P61922-1]
UCSC; uc007ycp.2; mouse. [P61922-2]
CTD; 18; -.
MGI; MGI:2443582; Abat.
eggNOG; KOG1405; Eukaryota.
eggNOG; COG0160; LUCA.
GeneTree; ENSGT00550000074885; -.
HOGENOM; HOG000020208; -.
HOVERGEN; HBG000634; -.
InParanoid; P61922; -.
KO; K13524; -.
OMA; ALGMNHP; -.
OrthoDB; EOG091G08T5; -.
PhylomeDB; P61922; -.
TreeFam; TF105021; -.
Reactome; R-MMU-916853; Degradation of GABA.
ChiTaRS; Abat; mouse.
PRO; PR:P61922; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000057880; -.
CleanEx; MM_ABAT; -.
ExpressionAtlas; P61922; baseline and differential.
Genevisible; P61922; MM.
GO; GO:0032144; C:4-aminobutyrate transaminase complex; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048148; P:behavioral response to cocaine; IMP:UniProtKB.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0007620; P:copulation; IEA:Ensembl.
GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
GO; GO:0033602; P:negative regulation of dopamine secretion; IEA:Ensembl.
GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
GO; GO:1904450; P:positive regulation of aspartate secretion; IEA:Ensembl.
GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0031652; P:positive regulation of heat generation; IEA:Ensembl.
GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl.
GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
CDD; cd00610; OAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004631; 4NH2But_aminotransferase_euk.
InterPro; IPR005814; Aminotrans_3.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00202; Aminotran_3; 1.
PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Aminotransferase;
Complete proteome; Direct protein sequencing; Disulfide bond; Iron;
Iron-sulfur; Metal-binding; Mitochondrion;
Neurotransmitter degradation; Pyridoxal phosphate; Reference proteome;
Transferase; Transit peptide.
TRANSIT 1 28 Mitochondrion. {ECO:0000250}.
CHAIN 29 500 4-aminobutyrate aminotransferase,
mitochondrial.
/FTId=PRO_0000001250.
REGION 164 165 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P80147}.
METAL 163 163 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:P80147}.
METAL 166 166 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:P80147}.
BINDING 220 220 Substrate.
{ECO:0000250|UniProtKB:P80147}.
BINDING 381 381 Pyridoxal phosphate; shared with dimeric
partner. {ECO:0000250|UniProtKB:P80147}.
MOD_RES 231 231 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 252 252 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 252 252 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 318 318 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 357 357 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P80147}.
MOD_RES 413 413 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 413 413 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 452 452 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 470 470 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
DISULFID 321 321 Interchain. {ECO:0000250}.
VAR_SEQ 319 374 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_012005.
SEQUENCE 500 AA; 56452 MW; 85AA331AB48355F3 CRC64;
MAFLLITRRL ACSSQKNLHL FIPGSRYISQ AAAKVDIEFD YDGPLMKTEV PGPRSKELMK
QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYNHP ALAKLVQQPQ
NASTFINRPA LGILPPENFV DKLQESLMSV APRGMSQLIT MACGSCSNEN AFKTIFMWYR
SKERGQRGFS KEELETCMVN QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS
FDWPIAPFPR LKYPLEEFTT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM
TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNVAR VGKTLLTGLL
DLQAQYPQFI SRVRGRGTFC SFDTPDEAIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF
RDHHAHLFLS IFSGILADFK


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