BCA6_ARATH
ID BCA6_ARATH Reviewed; 290 AA.
AC Q9C6F5; B9DFK8; F4I9R8; Q8L833; Q9C6R2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Beta carbonic anhydrase 6, mitochondrial;
DE Short=AtbCA6;
DE Short=AtbetaCA6;
DE EC=4.2.1.1;
DE AltName: Full=Beta carbonate dehydratase 6;
DE Flags: Precursor;
GN Name=BCA6; OrderedLocusNames=At1g58180; ORFNames=T15M6.18, T18I24.9;
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=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 [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 2).
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 3).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17407539; DOI=10.1111/j.1365-3040.2007.01651.x;
RA Fabre N., Reiter I.M., Becuwe-Linka N., Genty B., Rumeau D.;
RT "Characterization and expression analysis of genes encoding alpha and beta
RT carbonic anhydrases in Arabidopsis.";
RL Plant Cell Environ. 30:617-629(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=20010812; DOI=10.1038/ncb2009;
RA Hu H., Boisson-Dernier A., Israelsson-Nordstrom M., Bohmer M., Xue S.,
RA Ries A., Godoski J., Kuhn J.M., Schroeder J.I.;
RT "Carbonic anhydrases are upstream regulators of CO2-controlled stomatal
RT movements in guard cells.";
RL Nat. Cell Biol. 12:87-93(2010).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17407539}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C6F5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C6F5-2; Sequence=VSP_055074;
CC Name=3;
CC IsoId=Q9C6F5-3; Sequence=VSP_055073;
CC -!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
CC leaves, stems, flowers and siliques, and, to a lower extent, in roots.
CC Accumulates in guard cells. {ECO:0000269|PubMed:17407539,
CC ECO:0000269|PubMed:20010812}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50771.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079131; AAG50771.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079604; AAG50705.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33506.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33507.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33508.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33509.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58255.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58256.1; -; Genomic_DNA.
DR EMBL; AY120772; AAM53330.1; -; mRNA.
DR EMBL; BT000145; AAN15464.1; -; mRNA.
DR EMBL; AK316811; BAH19525.1; -; mRNA.
DR PIR; B96615; B96615.
DR RefSeq; NP_001031206.1; NM_001036129.3. [Q9C6F5-3]
DR RefSeq; NP_001185259.1; NM_001198330.1. [Q9C6F5-1]
DR RefSeq; NP_001320704.1; NM_001333818.1. [Q9C6F5-3]
DR RefSeq; NP_001320705.1; NM_001333817.1. [Q9C6F5-3]
DR RefSeq; NP_176114.2; NM_104599.5. [Q9C6F5-1]
DR RefSeq; NP_849823.1; NM_179492.4. [Q9C6F5-2]
DR AlphaFoldDB; Q9C6F5; -.
DR SMR; Q9C6F5; -.
DR STRING; 3702.AT1G58180.2; -.
DR PaxDb; Q9C6F5; -.
DR PRIDE; Q9C6F5; -.
DR ProteomicsDB; 240646; -. [Q9C6F5-1]
DR EnsemblPlants; AT1G58180.1; AT1G58180.1; AT1G58180. [Q9C6F5-2]
DR EnsemblPlants; AT1G58180.2; AT1G58180.2; AT1G58180. [Q9C6F5-1]
DR EnsemblPlants; AT1G58180.3; AT1G58180.3; AT1G58180. [Q9C6F5-3]
DR EnsemblPlants; AT1G58180.4; AT1G58180.4; AT1G58180. [Q9C6F5-1]
DR EnsemblPlants; AT1G58180.6; AT1G58180.6; AT1G58180. [Q9C6F5-3]
DR EnsemblPlants; AT1G58180.7; AT1G58180.7; AT1G58180. [Q9C6F5-3]
DR GeneID; 842185; -.
DR Gramene; AT1G58180.1; AT1G58180.1; AT1G58180. [Q9C6F5-2]
DR Gramene; AT1G58180.2; AT1G58180.2; AT1G58180. [Q9C6F5-1]
DR Gramene; AT1G58180.3; AT1G58180.3; AT1G58180. [Q9C6F5-3]
DR Gramene; AT1G58180.4; AT1G58180.4; AT1G58180. [Q9C6F5-1]
DR Gramene; AT1G58180.6; AT1G58180.6; AT1G58180. [Q9C6F5-3]
DR Gramene; AT1G58180.7; AT1G58180.7; AT1G58180. [Q9C6F5-3]
DR KEGG; ath:AT1G58180; -.
DR Araport; AT1G58180; -.
DR TAIR; locus:2196292; AT1G58180.
DR eggNOG; KOG1578; Eukaryota.
DR InParanoid; Q9C6F5; -.
DR OMA; HRRCEED; -.
DR OrthoDB; 1136193at2759; -.
DR PhylomeDB; Q9C6F5; -.
DR BioCyc; ARA:AT1G58180-MON; -.
DR PRO; PR:Q9C6F5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6F5; baseline and differential.
DR Genevisible; Q9C6F5; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00884; beta_CA_cladeB; 1.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR045066; Beta_CA_cladeB.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; PTHR11002; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lyase; Mitochondrion; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Transit peptide; Zinc.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..290
FT /note="Beta carbonic anhydrase 6, mitochondrial"
FT /id="PRO_0000429738"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42737"
FT MOD_RES 226
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P27140"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_055073"
FT VAR_SEQ 251..284
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_055074"
FT CONFLICT 38
FT /note="Missing (in Ref. 3; AAM53330/AAN15464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 33072 MW; 3F63FBA458DEB2A1 CRC64;
MAFTLGGRAR RLVSATSVHQ NGCLHKLQQI GSDRFQLGEA KAIRLLPRRT NMVQELGIRE
EFMDLNRETE TSYDFLDEMR HRFLKFKRQK YLPEIEKFKA LAIAQSPKVM VIGCADSRVC
PSYVLGFQPG EAFTIRNVAN LVTPVQNGPT ETNSALEFAV TTLQVENIIV MGHSNCGGIA
ALMSHQNHQG QHSSLVERWV MNGKAAKLRT QLASSHLSFD EQCRNCEKES IKDSVMNLIT
YSWIRDRVKR GEVKIHGCYY NLSDCSLEKW RLSSDKTNYG FYISDREIWS
