GCA2_ARATH
ID GCA2_ARATH Reviewed; 278 AA.
AC Q9C6B3; Q9C5S7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Gamma carbonic anhydrase 2, mitochondrial;
DE Short=AtCA2;
DE Short=GAMMA CA2;
DE EC=4.2.1.-;
DE AltName: Full=Transcription factor APFI;
DE Flags: Precursor;
GN Name=GAMMACA2; Synonyms=APFI; OrderedLocusNames=At1g47260;
GN ORFNames=F8G22.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zabaleta E., Perales M., Lohrmann J., Walter M., Brennicke A., Harter K.,
RA Kudla J.;
RT "APFI: A novel transcription factor involved in the anther specific
RT expression of nuclear-encoded mitochondrial complex I genes.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND GENE FAMILY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12837548; DOI=10.1016/s0005-2728(03)00045-8;
RA Heazlewood J.L., Howell K.A., Millar A.H.;
RT "Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian
RT and fungal components coupled with plant-specific subunits.";
RL Biochim. Biophys. Acta 1604:159-169(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [7]
RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604675; DOI=10.1007/s11103-004-0149-7;
RA Parisi G., Perales M., Fornasari M.S., Colaneri A., Gonzalez-Schain N.,
RA Gomez-Casati D., Zimmermann S., Brennicke A., Araya A., Ferry J.G.,
RA Echave J., Zabaleta E.;
RT "Gamma carbonic anhydrases in plant mitochondria.";
RL Plant Mol. Biol. 55:193-207(2004).
RN [8]
RP INTERACTION WITH GAMMACAL1 AND GAMMACAL2.
RX PubMed=15821992; DOI=10.1007/s11103-004-6324-z;
RA Perales M., Parisi G., Fornasari M.S., Colaneri A., Villarreal F.,
RA Gonzalez-Schain N., Echave J., Gomez-Casati D., Braun H.-P., Araya A.,
RA Zabaleta E.;
RT "Gamma carbonic anhydrase like complex interact with plant mitochondrial
RT complex I.";
RL Plant Mol. Biol. 56:947-957(2004).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=15935378; DOI=10.1016/j.jmb.2005.04.062;
RA Perales M., Eubel H., Heinemeyer J., Colaneri A., Zabaleta E., Braun H.-P.;
RT "Disruption of a nuclear gene encoding a mitochondrial gamma carbonic
RT anhydrase reduces complex I and supercomplex I + III2 levels and alters
RT mitochondrial physiology in Arabidopsis.";
RL J. Mol. Biol. 350:263-277(2005).
RN [10]
RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407270; DOI=10.1074/jbc.m511542200;
RA Sunderhaus S., Dudkina N.V., Jaensch L., Klodmann J., Heinemeyer J.,
RA Perales M., Zabaleta E., Boekema E.J., Braun H.-P.;
RT "Carbonic anhydrase subunits form a matrix-exposed domain attached to the
RT membrane arm of mitochondrial complex I in plants.";
RL J. Biol. Chem. 281:6482-6488(2006).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19808034; DOI=10.1016/j.febslet.2009.09.055;
RA Martin V., Villarreal F., Miras I., Navaza A., Haouz A.,
RA Gonzalez-Lebrero R.M., Kaufman S.B., Zabaleta E.;
RT "Recombinant plant gamma carbonic anhydrase homotrimers bind inorganic
RT carbon.";
RL FEBS Lett. 583:3425-3430(2009).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=19326245; DOI=10.1007/s11103-009-9484-z;
RA Villarreal F., Martin V., Colaneri A., Gonzalez-Schain N., Perales M.,
RA Martin M., Lombardo C., Braun H.-P., Bartoli C., Zabaleta E.;
RT "Ectopic expression of mitochondrial gamma carbonic anhydrase 2 causes male
RT sterility by anther indehiscence.";
RL Plant Mol. Biol. 70:471-485(2009).
CC -!- FUNCTION: Enzyme involved in the catabolism of H(2)CO(3) but that does
CC not mediates the reversible hydration of carbon dioxide
CC (PubMed:19808034). Mediates complex I assembly in mitochondria and
CC respiration. Binds HCO(3)-. Required for male fertility during anther
CC development and dehiscence to regulate the secondary thickenings of the
CC endothecial cell wall, probably by modulating H(2)O(2)-dependent lignin
CC polymerization. {ECO:0000269|PubMed:15935378,
CC ECO:0000269|PubMed:19326245, ECO:0000269|PubMed:19808034}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotrimer. Component of the mitochondrial oxidoreductase
CC respiratory chain complex I; element of the extra matrix-exposed
CC domain, which is attached to the membrane arm of this complex.
CC Interacts with GAMMACAL1 and GAMMACAL2. {ECO:0000269|PubMed:12837548,
CC ECO:0000269|PubMed:15821992, ECO:0000269|PubMed:15935378,
CC ECO:0000269|PubMed:16407270, ECO:0000269|PubMed:19808034}.
CC -!- INTERACTION:
CC Q9C6B3; Q9C6B3: GAMMACA2; NbExp=3; IntAct=EBI-531995, EBI-531995;
CC Q9C6B3; Q9FMV1: GAMMACAL1; NbExp=2; IntAct=EBI-531995, EBI-532008;
CC Q9C6B3; Q9SMN1: GAMMACAL2; NbExp=3; IntAct=EBI-531995, EBI-532001;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:15604675,
CC ECO:0000269|PubMed:16407270}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:15604675,
CC ECO:0000269|PubMed:16407270}; Matrix side {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:15604675, ECO:0000269|PubMed:16407270}.
CC Note=Probably integral to the membrane. {ECO:0000269|PubMed:16407270}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots and leaves, with
CC higher levels in flowers, particularly in tapetal tissue of anthers,
CC inflorescence (IM) and floral meristems (FM).
CC {ECO:0000269|PubMed:19326245}.
CC -!- DEVELOPMENTAL STAGE: During flower development, first expressed in
CC anthers and later in seeds. {ECO:0000269|PubMed:19326245}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of complex I and supercomplex I +
CC III(2) in mitochondrion. Reduced growth rates and respiration of
CC suspension cell culture. {ECO:0000269|PubMed:15935378}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AF249876; AAK28403.1; -; mRNA.
DR EMBL; AC079677; AAG52641.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32144.1; -; Genomic_DNA.
DR EMBL; AY045979; AAK76653.1; -; mRNA.
DR EMBL; AY113936; AAM44984.1; -; mRNA.
DR PIR; D96513; D96513.
DR RefSeq; NP_175159.1; NM_103620.4.
DR PDB; 7AQQ; EM; 3.06 A; y=1-278.
DR PDB; 7AR7; EM; 3.72 A; y=2-269.
DR PDB; 7AR8; EM; 3.53 A; y=1-278.
DR PDB; 7ARB; EM; 3.41 A; y=1-278.
DR PDBsum; 7AQQ; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; Q9C6B3; -.
DR SMR; Q9C6B3; -.
DR BioGRID; 26354; 60.
DR IntAct; Q9C6B3; 64.
DR MINT; Q9C6B3; -.
DR STRING; 3702.AT1G47260.1; -.
DR PaxDb; Q9C6B3; -.
DR PRIDE; Q9C6B3; -.
DR ProteomicsDB; 221934; -.
DR EnsemblPlants; AT1G47260.1; AT1G47260.1; AT1G47260.
DR GeneID; 841129; -.
DR Gramene; AT1G47260.1; AT1G47260.1; AT1G47260.
DR KEGG; ath:AT1G47260; -.
DR Araport; AT1G47260; -.
DR TAIR; locus:2036741; AT1G47260.
DR eggNOG; ENOG502QTES; Eukaryota.
DR HOGENOM; CLU_064827_0_0_1; -.
DR InParanoid; Q9C6B3; -.
DR OMA; QIHASEN; -.
DR OrthoDB; 1270774at2759; -.
DR PhylomeDB; Q9C6B3; -.
DR BioCyc; ARA:AT1G47260-MON; -.
DR BioCyc; MetaCyc:AT1G47260-MON; -.
DR BRENDA; 4.2.1.1; 399.
DR PRO; PR:Q9C6B3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6B3; baseline and differential.
DR Genevisible; Q9C6B3; AT.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0045271; C:respiratory chain complex I; IDA:TAIR.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009901; P:anther dehiscence; IMP:TAIR.
DR GO; GO:0009853; P:photorespiration; TAS:TAIR.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Membrane; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..278
FT /note="Gamma carbonic anhydrase 2, mitochondrial"
FT /id="PRO_0000417611"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 101..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 112
FT /note="N -> T (in Ref. 1; AAK28403)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> E (in Ref. 1; AAK28403)"
FT /evidence="ECO:0000305"
FT HELIX 3..29
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7AQQ"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 194..218
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:7AQQ"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7AQQ"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:7AQQ"
SQ SEQUENCE 278 AA; 30065 MW; 15396A4C3D61F731 CRC64;
MGTLGRAIYT VGNWIRGTGQ ALDRVGSLLQ GSHRIEEHLS RHRTLMNVFD KSPLVDKDVF
VAPSASVIGD VQIGKGSSIW YGCVLRGDVN NISVGSGTNI QDNTLVHVAK TNISGKVLPT
LIGDNVTVGH SAVIHGCTVE DDAFVGMGAT LLDGVVVEKH AMVAAGSLVK QNTRIPSGEV
WGGNPAKFMR KLTDEEIVYI SQSAKNYINL AQIHASENSK SFEQIEVERA LRKKYARKDE
DYDSMLGITR ETPPELILPD NVLPGGKPVA KVPSTQYF
