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ARATH:GCA2

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Species (Taxon ID) Arabidopsis thaliana (Mouse-ear cress). (3702)
Gene Name(s) GAMMACA2 (synonyms: APFI)
Protein Name(s) Gamma carbonic anhydrase 2, mitochondrial

AtCA2 GAMMA CA2 Transcription factor APFI

External Links
UniProt Q9C6B3
EMBL AF249876
AC079677
CP002684
AY045979
AY113936
PIR D96513
RefSeq NP_175159.1
UniGene At.397
ProteinModelPortal Q9C6B3
SMR Q9C6B3
BioGrid 26354
IntAct Q9C6B3
MINT MINT-7266055
STRING 3702.AT1G47260.1
PaxDb Q9C6B3
PRIDE Q9C6B3
EnsemblPlants [example_ID AT1G47260.1]
GeneID 841129
Gramene AT1G47260.1
KEGG ath:AT1G47260
TAIR AT1G47260
eggNOG ENOG410II35
COG0663
HOGENOM HOG000049430
InParanoid Q9C6B3
OMA RNSSIWY
PhylomeDB Q9C6B3
BioCyc ARA:AT1G47260-MONOMER
MetaCyc:AT1G47260-MONOMER
PRO PR:Q9C6B3
Proteomes UP000006548
Genevisible Q9C6B3
GO GO:0009507
GO:0016020
GO:0031966
GO:0005747
GO:0005739
GO:0045271
GO:0004089
GO:0042802
GO:0046872
GO:0009901
GO:0009853
GO:0070207
GO:2000377
GO:0009651
InterPro IPR001451
IPR011004
Pfam PF00132
SUPFAM SSF51161

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005747

mitochondrial respiratory chain complex I

PMID:26889912[1]

ECO:0000314

C

Figure 1d

complete
CACAO 11799

GO:2000375

negative regulation of oxygen metabolic process

PMID:26889912[1]

ECO:0000316

UniProtKB:Q9FWR5


P

Figure 5 shows that a double mutation in CA1 and CA2 result in increased oxygen consumption.

complete
CACAO 11800

GO:1904959

regulation of cytochrome-c oxidase activity

PMID:26889912[1]

ECO:0000316

UniProtKB:Q9FWR5


P

Figure 4d shows that a double mutation in ca1 and ca2 drastically increase cytochrome-c oxidase activity. This suggests that ca2 along with ca1 negatively regulates cytochrome-c oxidase activity

complete
CACAO 11804

involved_in

GO:0070207

protein homotrimerization

PMID:19808034[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

NOT|enables

GO:0004089

carbonate dehydratase activity

PMID:19808034[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:2000377

regulation of reactive oxygen species metabolic process

PMID:19326245[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0045271

respiratory chain complex I

PMID:16407270[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0031966

mitochondrial membrane

PMID:16407270[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:17432890[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009901

anther dehiscence

PMID:19326245[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009651

response to salt stress

PMID:17916636[6]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:15028209[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005747

mitochondrial respiratory chain complex I

PMID:20197505[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005747

mitochondrial respiratory chain complex I

PMID:18189341[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:22923678[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:15604675[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:15276431[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14671022[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:12837548[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:11743115[15]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004089

carbonate dehydratase activity

PMID:16407270[4]

ECO:0000250

sequence similarity evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

enables

GO:0042802

identical protein binding

PMID:19808034[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9C6B3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15821992[16]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9C6B3

F

Seeded From UniProt

complete

involved_in

GO:0009853

photorespiration

PMID:16407270[4]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0031966

mitochondrial membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0171

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Fromm, S et al. (2016) Mitochondrial gamma carbonic anhydrases are required for complex I assembly and plant reproductive development. New Phytol. PubMed GONUTS page
  2. 2.0 2.1 2.2 Martin, V et al. (2009) Recombinant plant gamma carbonic anhydrase homotrimers bind inorganic carbon. FEBS Lett. 583 3425-30 PubMed GONUTS page
  3. 3.0 3.1 Villarreal, F et al. (2009) Ectopic expression of mitochondrial gamma carbonic anhydrase 2 causes male sterility by anther indehiscence. Plant Mol. Biol. 70 471-85 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Sunderhaus, S et al. (2006) Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants. J. Biol. Chem. 281 6482-8 PubMed GONUTS page
  5. Mitra, SK et al. (2007) Membrane proteomic analysis of Arabidopsis thaliana using alternative solubilization techniques. J. Proteome Res. 6 1933-50 PubMed GONUTS page
  6. Jiang, Y et al. (2007) Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. J. Exp. Bot. 58 3591-607 PubMed GONUTS page
  7. Kleffmann, T et al. (2004) The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 14 354-62 PubMed GONUTS page
  8. Klodmann, J et al. (2010) Internal architecture of mitochondrial complex I from Arabidopsis thaliana. Plant Cell 22 797-810 PubMed GONUTS page
  9. Meyer, EH et al. (2008) Resolving and identifying protein components of plant mitochondrial respiratory complexes using three dimensions of gel electrophoresis. J. Proteome Res. 7 786-94 PubMed GONUTS page
  10. Nikolovski, N et al. (2012) Putative glycosyltransferases and other plant Golgi apparatus proteins are revealed by LOPIT proteomics. Plant Physiol. 160 1037-51 PubMed GONUTS page
  11. Parisi, G et al. (2004) Gamma carbonic anhydrases in plant mitochondria. Plant Mol. Biol. 55 193-207 PubMed GONUTS page
  12. Brugière, S et al. (2004) The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions. Phytochemistry 65 1693-707 PubMed GONUTS page
  13. Heazlewood, JL et al. (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16 241-56 PubMed GONUTS page
  14. Heazlewood, JL et al. (2003) Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits. Biochim. Biophys. Acta 1604 159-69 PubMed GONUTS page
  15. Millar, AH et al. (2001) Analysis of the Arabidopsis mitochondrial proteome. Plant Physiol. 127 1711-27 PubMed GONUTS page
  16. Perales, M et al. (2004) Gamma carbonic anhydrase like complex interact with plant mitochondrial complex I. Plant Mol. Biol. 56 947-57 PubMed GONUTS page