GCAT
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
Also known as: KBL, KBL_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O75600
- Gene
- GCAT
- Ensembl
- ENSG00000100116
- Chromosome
- 22
- Canonical length
- 419 aa
- Protein class
- Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Nuclear speckles,Mitochondria
OverviewNCBI Gene
The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is first converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. This gene encodes the second enzyme in this pathway, which then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The encoded enzyme is considered a class II pyridoxal-phosphate-dependent aminotransferase. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 14. [provided by RefSeq, Jan 2010]
Canonical amino-acid sequenceUniProt
419 residues, UniProt reviewed canonical sequence.
>O75600|GCAT
1 MWPGNAWRAA LFWVPRGRRA QSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV
61 DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA
121 RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD
181 MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG
241 PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP
301 AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS
361 RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALPLocalizationUniProt · AlphaFold · HPA
Whether an antibody against GCAT can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.26
- Highest tissue expression
- 132 nTPM
Expression across tissuesHPA
Tissue
- pancreas: 132 nTPM
- liver: 53 nTPM
- heart muscle: 41 nTPM
- midbrain: 25 nTPM
- cerebral cortex: 25 nTPM
- amygdala: 23 nTPM
Single-cell type
- oocytes: 212 nCPM
- esophageal apical cells: 151 nCPM
- pancreatic acinar cells: 75 nCPM
- hepatocytes: 74 nCPM
- breast lactating cells: 56 nCPM
- syncytiotrophoblasts: 54 nCPM
Immune cell
- naive CD4 T-cell: 3.5 nTPM
- T-reg: 1.7 nTPM
- memory CD4 T-cell: 1.6 nTPM
- naive CD8 T-cell: 1.4 nTPM
- total PBMC: 1.4 nTPM
- myeloid DC: 1.3 nTPM
Brain region
- thalamus: 27 nTPM
- pons: 27 nTPM
- midbrain: 26 nTPM
- cerebellum: 23 nTPM
- hippocampal formation: 22 nTPM
- medulla oblongata: 22 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.24
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.16
- DepMap mean gene effect
- -0.16
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- amino acid metabolic process
- L-threonine catabolic process
Molecular functions
- pyridoxal phosphate binding
- glycine C-acetyltransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Aminotransferase, class-II, pyridoxal-phosphate binding site
- Aminotransferase, class I/classII, large domain
- Pyridoxal phosphate-dependent transferase, major domain
- Pyridoxal phosphate-dependent transferase, small domain
- Pyridoxal phosphate-dependent transferase
- 8-amino-7-oxononanoate synthase class-II
- Aminotransferase class I and II
- 2-amino-3-ketobutyrate coenzyme A ligase
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads GCAT as an antibody target. Whether an autoantibody or antibody against GCAT could matter depends on whether native GCAT is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
GCAT is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label GCAT as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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