BCA1_ARATH
ID BCA1_ARATH Reviewed; 347 AA.
AC P27140; Q0WWA9; Q56WK1; Q8RWW2; Q93VR8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Beta carbonic anhydrase 1, chloroplastic {ECO:0000303|PubMed:17407539};
DE Short=AtbCA1;
DE Short=AtbetaCA1;
DE EC=4.2.1.1 {ECO:0000255|RuleBase:RU003956};
DE AltName: Full=Beta carbonate dehydratase 1;
DE AltName: Full=Protein SALICYLIC ACID-BINDING PROTEIN 3;
DE Short=AtSABP3;
DE Flags: Precursor;
GN Name=BCA1 {ECO:0000303|PubMed:17407539};
GN Synonyms=CA1 {ECO:0000303|PubMed:20010812}, SABP3;
GN OrderedLocusNames=At3g01500 {ECO:0000312|Araport:AT3G01500};
GN ORFNames=F4P13.5 {ECO:0000312|EMBL:CAA46508.1};
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] (ISOFORM 2).
RC STRAIN=cv. C24; TISSUE=Leaf;
RX PubMed=1463847; DOI=10.1007/bf00028900;
RA Raines C., Horsnell P.R., Holder C., Lloyd J.C.;
RT "Arabidopsis thaliana carbonic anhydrase: cDNA sequence and effect of CO2
RT on mRNA levels.";
RL Plant Mol. Biol. 20:1143-1148(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=7520589; DOI=10.1104/pp.105.2.707;
RA Fett J.P., Coleman J.R.;
RT "Characterization and expression of two cDNAs encoding carbonic anhydrase
RT in Arabidopsis thaliana.";
RL Plant Physiol. 105:707-713(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18434607; DOI=10.1104/pp.108.118661;
RA Ferreira F.J., Guo C., Coleman J.R.;
RT "Reduction of plastid-localized carbonic anhydrase activity results in
RT reduced Arabidopsis seedling survivorship.";
RL Plant Physiol. 147:585-594(2008).
RN [9]
RP FUNCTION, S-NITROSYLATION AT CYS-280, 3D-STRUCTURE MODELING, MUTAGENESIS OF
RP CYS-280, SALICYLIC ACID-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=19017644; DOI=10.1074/jbc.m806782200;
RA Wang Y.Q., Feechan A., Yun B.W., Shafiei R., Hofmann A., Taylor P., Xue P.,
RA Yang F.Q., Xie Z.S., Pallas J.A., Chu C.C., Loake G.J.;
RT "S-nitrosylation of AtSABP3 antagonizes the expression of plant immunity.";
RL J. Biol. Chem. 284:2131-2137(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203 AND SER-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-114, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP FUNCTION.
RX PubMed=25043023; DOI=10.1038/nature13452;
RA Engineer C.B., Ghassemian M., Anderson J.C., Peck S.C., Hu H.,
RA Schroeder J.I.;
RT "Carbonic anhydrases, EPF2 and a novel protease mediate CO2 control of
RT stomatal development.";
RL Nature 513:246-250(2014).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. Required for
CC photosynthesis in cotyledons. Binds salicylic acid. Together with BCA4,
CC involved in the CO(2) signaling pathway which controls gas-exchange
CC between plants and the atmosphere by modulating stomatal development
CC and movements. Promotes water use efficiency.
CC {ECO:0000269|PubMed:18434607, ECO:0000269|PubMed:19017644,
CC ECO:0000269|PubMed:20010812, ECO:0000269|PubMed:25043023}.
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 Evidence={ECO:0000255|RuleBase:RU003956};
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:17407539}. Cell membrane
CC {ECO:0000269|PubMed:20010812}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20010812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P27140-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27140-2; Sequence=VSP_009004;
CC Name=3;
CC IsoId=P27140-3; Sequence=VSP_009003;
CC -!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
CC leaves, stems, flowers and siliques. Accumulates in both guard cells
CC and mesophyll cells. {ECO:0000269|PubMed:17407539,
CC ECO:0000269|PubMed:20010812}.
CC -!- INDUCTION: Expression reduced by 70% under dark conditions.
CC -!- PTM: S-nitrosylation at Cys-280 is up-regulated during nitrosative
CC burst and suppresses both binding of salicylic acid and carbonic
CC anhydrase activity. S-nitrosylated in response to an avirulent but not
CC to a virulent bacterial strain. {ECO:0000269|PubMed:19017644}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of seedling establishment
CC associated with altered cotyledon photosynthetic performance at the
CC onset of phototrophic growth and prior to the development of true
CC leaves. These phenotypes are reversed in high CO(2) or sucrose
CC supplemented conditions. Decreased resistance against avirulent
CC bacteria. In plants lacking both BCA1 and BCA4, impaired CO(2)-
CC regulation of stomatal movements associated with reduced beta carbonic
CC anhydrase activity in guard cells, and increased stomatal density.
CC {ECO:0000269|PubMed:18434607, ECO:0000269|PubMed:19017644,
CC ECO:0000269|PubMed:20010812}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94771.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X65541; CAA46508.1; -; mRNA.
DR EMBL; AC009325; AAF01535.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73675.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73676.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73677.1; -; Genomic_DNA.
DR EMBL; AF428284; AAL16116.1; -; mRNA.
DR EMBL; AF428459; AAL16228.1; -; mRNA.
DR EMBL; AY056175; AAL07024.1; -; mRNA.
DR EMBL; AY062785; AAL32863.1; -; mRNA.
DR EMBL; AY081658; AAM10220.1; -; mRNA.
DR EMBL; AY091066; AAM13886.1; -; mRNA.
DR EMBL; AK226447; BAE98589.1; -; mRNA.
DR EMBL; AK222039; BAD94771.1; ALT_INIT; mRNA.
DR PIR; S28412; S28412.
DR RefSeq; NP_186799.2; NM_111016.4. [P27140-1]
DR RefSeq; NP_850490.1; NM_180159.2. [P27140-3]
DR RefSeq; NP_850491.1; NM_180160.4. [P27140-2]
DR AlphaFoldDB; P27140; -.
DR SMR; P27140; -.
DR BioGRID; 6467; 16.
DR IntAct; P27140; 11.
DR STRING; 3702.AT3G01500.2; -.
DR iPTMnet; P27140; -.
DR SWISS-2DPAGE; P27140; -.
DR PaxDb; P27140; -.
DR PRIDE; P27140; -.
DR ProteomicsDB; 240719; -. [P27140-1]
DR EnsemblPlants; AT3G01500.1; AT3G01500.1; AT3G01500. [P27140-3]
DR EnsemblPlants; AT3G01500.2; AT3G01500.2; AT3G01500. [P27140-1]
DR EnsemblPlants; AT3G01500.3; AT3G01500.3; AT3G01500. [P27140-2]
DR GeneID; 821134; -.
DR Gramene; AT3G01500.1; AT3G01500.1; AT3G01500. [P27140-3]
DR Gramene; AT3G01500.2; AT3G01500.2; AT3G01500. [P27140-1]
DR Gramene; AT3G01500.3; AT3G01500.3; AT3G01500. [P27140-2]
DR KEGG; ath:AT3G01500; -.
DR Araport; AT3G01500; -.
DR TAIR; locus:2084198; AT3G01500.
DR eggNOG; KOG1578; Eukaryota.
DR InParanoid; P27140; -.
DR PhylomeDB; P27140; -.
DR BioCyc; ARA:AT3G01500-MON; -.
DR BioCyc; MetaCyc:AT3G01500-MON; -.
DR PRO; PR:P27140; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P27140; baseline and differential.
DR Genevisible; P27140; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0004089; F:carbonate dehydratase activity; IMP:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:2000122; P:negative regulation of stomatal complex development; IGI:TAIR.
DR GO; GO:0015979; P:photosynthesis; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IGI:TAIR.
DR GO; GO:0010037; P:response to carbon dioxide; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Chloroplast; Lyase;
KW Membrane; Phosphoprotein; Plastid; Reference proteome; S-nitrosylation;
KW Transit peptide; Zinc.
FT TRANSIT 1..113
FT /note="Chloroplast"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:22223895"
FT CHAIN 114..347
FT /note="Beta carbonic anhydrase 1, chloroplastic"
FT /id="PRO_0000004267"
FT MOD_RES 114
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42737"
FT MOD_RES 203
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 280
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:19017644"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009003"
FT VAR_SEQ 337..347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:1463847, ECO:0000303|PubMed:7520589,
FT ECO:0000303|Ref.6"
FT /id="VSP_009004"
FT MUTAGEN 280
FT /note="C->S: Loss of nitrosylation and decreased carbonic
FT anhydrase activity, but no effect on salicylic acid
FT binding."
FT /evidence="ECO:0000269|PubMed:19017644"
SQ SEQUENCE 347 AA; 37450 MW; 9061FF3EF64CAFD7 CRC64;
MSTAPLSGFF LTSLSPSQSS LQKLSLRTSS TVACLPPASS SSSSSSSSSS RSVPTLIRNE
PVFAAPAPII APYWSEEMGT EAYDEAIEAL KKLLIEKEEL KTVAAAKVEQ ITAALQTGTS
SDKKAFDPVE TIKQGFIKFK KEKYETNPAL YGELAKGQSP KYMVFACSDS RVCPSHVLDF
QPGDAFVVRN IANMVPPFDK VKYGGVGAAI EYAVLHLKVE NIVVIGHSAC GGIKGLMSFP
LDGNNSTDFI EDWVKICLPA KSKVISELGD SAFEDQCGRC EREAVNVSLA NLLTYPFVRE
GLVKGTLALK GGYYDFVKGA FELWGLEFGL SETSSVKDVA TILHWKL
