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Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

Abat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.

Cofactori

GO - Molecular functioni

  1. (S)-3-amino-2-methylpropionate transaminase activity Source: UniProtKB-EC
  2. 4-aminobutyrate transaminase activity Source: UniProtKB-EC
  3. protein homodimerization activity Source: UniProtKB
  4. pyridoxal phosphate binding Source: UniProtKB
  5. succinate-semialdehyde dehydrogenase binding Source: UniProtKB

GO - Biological processi

  1. behavioral response to cocaine Source: UniProtKB
  2. copulation Source: Ensembl
  3. gamma-aminobutyric acid metabolic process Source: InterPro
  4. locomotory behavior Source: Ensembl
  5. negative regulation of blood pressure Source: Ensembl
  6. neurotransmitter catabolic process Source: UniProtKB-KW
  7. response to drug Source: Ensembl
  8. response to ethanol Source: Ensembl
  9. response to hypoxia Source: Ensembl
  10. response to iron ion Source: Ensembl
  11. response to nicotine Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Neurotransmitter degradation

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_198642. Degradation of GABA.

Names & Taxonomyi

Protein namesi
Recommended name:
4-aminobutyrate aminotransferase, mitochondrial (EC:2.6.1.19)
Alternative name(s):
(S)-3-amino-2-methylpropionate transaminase (EC:2.6.1.22)
GABA aminotransferase
Short name:
GABA-AT
Gamma-amino-N-butyrate transaminase
Short name:
GABA transaminase
Short name:
GABA-T
L-AIBAT
Gene namesi
Name:Abat
Synonyms:Gabat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:2443582. Abat.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. 4-aminobutyrate transaminase complex Source: UniProtKB
  2. extracellular vesicular exosome Source: MGI
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: UniProtKB
  5. neuron projection Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionBy similarityAdd
BLAST
Chaini29 – 5004724-aminobutyrate aminotransferase, mitochondrialPRO_0000001250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi163 ↔ 166By similarity
Modified residuei231 – 2311N6-succinyllysine1 Publication
Modified residuei252 – 2521N6-acetyllysine; alternate1 Publication
Modified residuei252 – 2521N6-succinyllysine; alternate1 Publication
Modified residuei279 – 2791N6-acetyllysine1 Publication
Modified residuei318 – 3181N6-acetyllysine1 Publication
Disulfide bondi321 – 321InterchainBy similarity
Modified residuei357 – 3571N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei413 – 4131N6-acetyllysine; alternate1 Publication
Modified residuei413 – 4131N6-succinyllysine; alternate1 Publication
Modified residuei452 – 4521N6-acetyllysine1 Publication
Modified residuei470 – 4701N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP61922.
PaxDbiP61922.
PRIDEiP61922.

2D gel databases

REPRODUCTION-2DPAGEIPI00407499.

PTM databases

PhosphoSiteiP61922.

Expressioni

Gene expression databases

BgeeiP61922.
CleanExiMM_ABAT.
ExpressionAtlasiP61922. baseline and differential.
GenevestigatoriP61922.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

IntActiP61922. 2 interactions.
MINTiMINT-1842478.

Structurei

3D structure databases

ProteinModelPortaliP61922.
SMRiP61922. Positions 39-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00550000074885.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP61922.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG7ZPNJW.
PhylomeDBiP61922.
TreeFamiTF105021.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61922-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFLLITRRL ACSSQKNLHL FIPGSRYISQ AAAKVDIEFD YDGPLMKTEV
60 70 80 90 100
PGPRSKELMK QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI
110 120 130 140 150
SSVPIGYNHP ALAKLVQQPQ NASTFINRPA LGILPPENFV DKLQESLMSV
160 170 180 190 200
APRGMSQLIT MACGSCSNEN AFKTIFMWYR SKERGQRGFS KEELETCMVN
210 220 230 240 250
QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR
260 270 280 290 300
LKYPLEEFTT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG
310 320 330 340 350
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA
360 370 380 390 400
DVMTFSKKMM TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK
410 420 430 440 450
REDLLNNVAR VGKTLLTGLL DLQAQYPQFI SRVRGRGTFC SFDTPDEAIR
460 470 480 490 500
NKLILIARNK GVVLGGCGDK SIRFRPTLVF RDHHAHLFLS IFSGILADFK

Note: No experimental confirmation available.

Length:500
Mass (Da):56,452
Last modified:June 7, 2004 - v1
Checksum:i85AA331AB48355F3
GO
Isoform 2 (identifier: P61922-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     319-374: Missing.

Note: No experimental confirmation available.

Show »
Length:444
Mass (Da):50,237
Checksum:i1E7C6A3DFDDD639D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei319 – 37456Missing in isoform 2. 1 PublicationVSP_012005Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC058079 mRNA. Translation: AAH58079.1.
BC058521 mRNA. Translation: AAH58521.1.
AK036128 mRNA. Translation: BAC29312.1.
CCDSiCCDS27939.1. [P61922-1]
CCDS49754.1. [P61922-2]
RefSeqiNP_001164449.1. NM_001170978.1. [P61922-2]
NP_766549.2. NM_172961.3. [P61922-1]
UniGeneiMm.259315.

Genome annotation databases

EnsembliENSMUST00000065987; ENSMUSP00000063548; ENSMUSG00000057880. [P61922-1]
ENSMUST00000115839; ENSMUSP00000111505; ENSMUSG00000057880. [P61922-2]
GeneIDi268860.
KEGGimmu:268860.
UCSCiuc007yco.2. mouse. [P61922-1]
uc007ycp.2. mouse. [P61922-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC058079 mRNA. Translation: AAH58079.1.
BC058521 mRNA. Translation: AAH58521.1.
AK036128 mRNA. Translation: BAC29312.1.
CCDSiCCDS27939.1. [P61922-1]
CCDS49754.1. [P61922-2]
RefSeqiNP_001164449.1. NM_001170978.1. [P61922-2]
NP_766549.2. NM_172961.3. [P61922-1]
UniGeneiMm.259315.

3D structure databases

ProteinModelPortaliP61922.
SMRiP61922. Positions 39-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP61922. 2 interactions.
MINTiMINT-1842478.

PTM databases

PhosphoSiteiP61922.

2D gel databases

REPRODUCTION-2DPAGEIPI00407499.

Proteomic databases

MaxQBiP61922.
PaxDbiP61922.
PRIDEiP61922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065987; ENSMUSP00000063548; ENSMUSG00000057880. [P61922-1]
ENSMUST00000115839; ENSMUSP00000111505; ENSMUSG00000057880. [P61922-2]
GeneIDi268860.
KEGGimmu:268860.
UCSCiuc007yco.2. mouse. [P61922-1]
uc007ycp.2. mouse. [P61922-2]

Organism-specific databases

CTDi18.
MGIiMGI:2443582. Abat.

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00550000074885.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP61922.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG7ZPNJW.
PhylomeDBiP61922.
TreeFamiTF105021.

Enzyme and pathway databases

ReactomeiREACT_198642. Degradation of GABA.

Miscellaneous databases

ChiTaRSiAbat. mouse.
NextBioi392544.
PROiP61922.
SOURCEiSearch...

Gene expression databases

BgeeiP61922.
CleanExiMM_ABAT.
ExpressionAtlasiP61922. baseline and differential.
GenevestigatoriP61922.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  3. Lubec G., Klug S., Friebe K., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 35-47; 61-173; 221-231; 236-279; 286-310; 318-337; 368-410; 414-432; 437-450 AND 461-470, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-231; LYS-252 AND LYS-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-279; LYS-318; LYS-413; LYS-452 AND LYS-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGABT_MOUSE
AccessioniPrimary (citable) accession number: P61922
Secondary accession number(s): Q8BZA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: February 4, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.