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P61922 (GABT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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Names and origin

Protein namesRecommended 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 names
Name:Abat
Synonyms:Gabat
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

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

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to cocaine

Inferred from mutant phenotype PubMed 10850552. Source: UniProtKB

copulation

Inferred from electronic annotation. Source: Compara

gamma-aminobutyric acid metabolic process

Inferred from electronic annotation. Source: InterPro

locomotory behavior

Inferred from electronic annotation. Source: Compara

negative regulation of blood pressure

Inferred from electronic annotation. Source: Compara

neurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to drug

Inferred from electronic annotation. Source: Compara

response to ethanol

Inferred from electronic annotation. Source: Compara

response to hypoxia

Inferred from electronic annotation. Source: Compara

response to iron ion

Inferred from electronic annotation. Source: Compara

response to nicotine

Inferred from electronic annotation. Source: Compara

   Cellular_component4-aminobutyrate transaminase complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Compara

   Molecular_function(S)-3-amino-2-methylpropionate transaminase activity

Inferred from electronic annotation. Source: EC

4-aminobutyrate transaminase activity

Inferred from electronic annotation. Source: EC

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

pyridoxal phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

succinate-semialdehyde dehydrogenase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61922-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: P61922-2)

The sequence of this isoform differs from the canonical sequence as follows:
     319-374: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion By similarity
Chain29 – 5004724-aminobutyrate aminotransferase, mitochondrial
PRO_0000001250

Amino acid modifications

Modified residue3181N6-acetyllysine Ref.4
Modified residue3571N6-(pyridoxal phosphate)lysine By similarity
Disulfide bond163 ↔ 166 By similarity
Disulfide bond321Interchain By similarity

Natural variations

Alternative sequence319 – 37456Missing in isoform 2.
VSP_012005

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 85AA331AB48355F3

FASTA50056,452
        10         20         30         40         50         60 
MAFLLITRRL ACSSQKNLHL FIPGSRYISQ AAAKVDIEFD YDGPLMKTEV PGPRSKELMK 

        70         80         90        100        110        120 
QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYNHP ALAKLVQQPQ 

       130        140        150        160        170        180 
NASTFINRPA LGILPPENFV DKLQESLMSV APRGMSQLIT MACGSCSNEN AFKTIFMWYR 

       190        200        210        220        230        240 
SKERGQRGFS KEELETCMVN QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS 

       250        260        270        280        290        300 
FDWPIAPFPR LKYPLEEFTT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG 

       310        320        330        340        350        360 
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM 

       370        380        390        400        410        420 
TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNVAR VGKTLLTGLL 

       430        440        450        460        470        480 
DLQAQYPQFI SRVRGRGTFC SFDTPDEAIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF 

       490        500 
RDHHAHLFLS IFSGILADFK

« Hide

Isoform 2 [UniParc].

Checksum: 1E7C6A3DFDDD639D
Show »

FASTA44450,237

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC058079 mRNA. Translation: AAH58079.1.
BC058521 mRNA. Translation: AAH58521.1.
AK036128 mRNA. Translation: BAC29312.1.
IPIIPI00227445.
IPI00407499.
RefSeqNP_001164449.1. NM_001170978.1.
NP_766549.2. NM_172961.3.
UniGeneMm.259315.

3D structure databases

ProteinModelPortalP61922.
SMRP61922. Positions 39-499.
ModBaseSearch...

PTM databases

PhosphoSiteP61922.

2D gel databases

REPRODUCTION-2DPAGEIPI00407499.

Proteomic databases

PaxDbP61922.
PRIDEP61922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000065987; ENSMUSP00000063548; ENSMUSG00000057880.
ENSMUST00000115839; ENSMUSP00000111505; ENSMUSG00000057880.
GeneID268860.
KEGGmmu:268860.
UCSCuc007yco.2. mouse.
uc007ycp.2. mouse.

Organism-specific databases

CTD18.
MGIMGI:2443582. Abat.

Phylogenomic databases

eggNOGCOG0160.
GeneTreeENSGT00550000074885.
HOGENOMHOG000020208.
HOVERGENHBG000634.
InParanoidP61922.
KOK13524.
OMARLACSFQ.
OrthoDBEOG441QB6.

Gene expression databases

ArrayExpressP61922.
BgeeP61922.
CleanExMM_ABAT.
GenevestigatorP61922.
GermOnlineENSMUSG00000057880. Mus musculus.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABAT. mouse.
NextBio392544.
SOURCESearch...

Entry information

Entry nameGABT_MOUSE
AccessionPrimary (citable) accession number: P61922
Secondary accession number(s): Q8BZA3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents