GCA3_ARATH
ID GCA3_ARATH Reviewed; 258 AA.
AC Q94AU7; A8MRL3; Q9FJY8;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Gamma carbonic anhydrase 3, mitochondrial;
DE Short=AtCA3;
DE Short=GAMMA CA3;
DE EC=4.2.1.-;
DE Flags: Precursor;
GN Name=GAMMACA3; OrderedLocusNames=At5g66510; ORFNames=K1F13.17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 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).
CC -!- FUNCTION: Enzyme involved in the catabolism of H(2)CO(3) but that does
CC not mediates the reversible hydration of carbon dioxide. Mediates
CC complex I assembly in mitochondria and respiration (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotrimer (Probable). Component of the 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 {ECO:0000269|PubMed:12837548, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:15604675}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:15604675}; Matrix side {ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:15604675}. Note=Probably integral to the membrane.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94AU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94AU7-2; Sequence=VSP_043830;
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10927.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB013389; BAB10927.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98222.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98223.1; -; Genomic_DNA.
DR EMBL; AY045784; AAK76458.1; -; mRNA.
DR EMBL; AY079385; AAL85116.1; -; mRNA.
DR EMBL; AY087379; AAM64929.1; -; mRNA.
DR RefSeq; NP_001078808.1; NM_001085339.1. [Q94AU7-2]
DR RefSeq; NP_569036.1; NM_126049.4. [Q94AU7-1]
DR AlphaFoldDB; Q94AU7; -.
DR SMR; Q94AU7; -.
DR BioGRID; 22025; 1.
DR IntAct; Q94AU7; 2.
DR STRING; 3702.AT5G66510.2; -.
DR PaxDb; Q94AU7; -.
DR PRIDE; Q94AU7; -.
DR ProteomicsDB; 221886; -. [Q94AU7-1]
DR EnsemblPlants; AT5G66510.1; AT5G66510.1; AT5G66510. [Q94AU7-1]
DR EnsemblPlants; AT5G66510.2; AT5G66510.2; AT5G66510. [Q94AU7-2]
DR GeneID; 836783; -.
DR Gramene; AT5G66510.1; AT5G66510.1; AT5G66510. [Q94AU7-1]
DR Gramene; AT5G66510.2; AT5G66510.2; AT5G66510. [Q94AU7-2]
DR KEGG; ath:AT5G66510; -.
DR Araport; AT5G66510; -.
DR TAIR; locus:2154840; AT5G66510.
DR eggNOG; ENOG502QTES; Eukaryota.
DR HOGENOM; CLU_064827_0_0_1; -.
DR InParanoid; Q94AU7; -.
DR OMA; AHVRQNT; -.
DR OrthoDB; 1270774at2759; -.
DR PhylomeDB; Q94AU7; -.
DR BioCyc; ARA:AT5G66510-MON; -.
DR BioCyc; MetaCyc:AT5G66510-MON; -.
DR PRO; PR:Q94AU7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AU7; baseline and differential.
DR Genevisible; Q94AU7; 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:0009536; C:plastid; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009853; P:photorespiration; TAS:TAIR.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
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 Alternative splicing; 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..258
FT /note="Gamma carbonic anhydrase 3, mitochondrial"
FT /id="PRO_0000417612"
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 VAR_SEQ 86
FT /note="R -> RDIPFDLMTDSA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043830"
SQ SEQUENCE 258 AA; 27837 MW; A85CBF4E5FA61AFF CRC64;
MGTMGKAFYS VGFWIRETGQ ALDRLGCRLQ GKNHFREQLS RHRTLMNVFD KTPNVDKGAF
VAPNASLSGD VHVGRGSSIW YGCVLRGDAN SISVGAGTNI QDNALVHVAK TNLSGKVLPT
VIGDNVTIGH SAVLHGCTVE DEAYIGTSAT VLDGAHVEKH AMVASGALVR QNTRIPSGEV
WGGNPAKFLR KVTEEERVFF SSSAVEYSNL AQAHATENAK NLDEAEFKKL LNKKNARDTE
YDSVLDDLTL PENVPKAA
