BCA2_ARATH
ID BCA2_ARATH Reviewed; 331 AA.
AC P42737; B9DHN2; F4K874; Q42116; Q9FDZ0; Q9LER2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 25-MAY-2022, entry version 171.
DE RecName: Full=Beta carbonic anhydrase 2, chloroplastic;
DE Short=AtbCA2;
DE Short=AtbetaCA2;
DE EC=4.2.1.1;
DE AltName: Full=Beta carbonate dehydratase 2;
DE Flags: Precursor;
GN Name=BCA2; Synonyms=CA18, CA2; OrderedLocusNames=At5g14740;
GN ORFNames=T9L3.40;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] OF 41-331 (ISOFORMS 1 AND 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] OF 57-331 (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 62-331 (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 276-331 (ISOFORM 1/2).
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [8]
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 [9]
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 [10]
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-170 AND TYR-198, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS 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).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. This isoform ensures
CC the supply of bicarbonate for pep carboxylase.
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 -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC {ECO:0000269|PubMed:12766230}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:17407539}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P42737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42737-2; Sequence=VSP_055068;
CC -!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
CC leaves, stems, flowers and siliques. Accumulates in mesophyll cells.
CC {ECO:0000269|PubMed:17407539, ECO:0000269|PubMed:20010812}.
CC -!- INDUCTION: Expression reduced by 20% under dark conditions.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50156.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG40063.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG41445.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN31799.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN31810.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC01873.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391149; CAC01873.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92068.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92069.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68481.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68482.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68483.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68484.1; -; Genomic_DNA.
DR EMBL; AF324712; AAG40063.1; ALT_INIT; mRNA.
DR EMBL; AF326863; AAG41445.1; ALT_INIT; mRNA.
DR EMBL; AF339686; AAK00368.1; -; mRNA.
DR EMBL; AF428428; AAL16197.1; -; mRNA.
DR EMBL; BT000652; AAN31799.1; ALT_INIT; mRNA.
DR EMBL; BT000663; AAN31810.1; ALT_INIT; mRNA.
DR EMBL; AK317585; BAH20249.1; -; mRNA.
DR EMBL; L18901; AAA50156.1; ALT_INIT; mRNA.
DR EMBL; Z26538; CAA81309.1; -; mRNA.
DR RefSeq; NP_001330235.1; NM_001343359.1. [P42737-2]
DR RefSeq; NP_001330236.1; NM_001343360.1. [P42737-2]
DR RefSeq; NP_001330237.1; NM_001343361.1. [P42737-2]
DR RefSeq; NP_001330238.1; NM_001343362.1. [P42737-2]
DR RefSeq; NP_568303.2; NM_121478.4. [P42737-1]
DR RefSeq; NP_974782.1; NM_203053.2. [P42737-2]
DR AlphaFoldDB; P42737; -.
DR SMR; P42737; -.
DR BioGRID; 16603; 2.
DR IntAct; P42737; 50.
DR STRING; 3702.AT5G14740.1; -.
DR iPTMnet; P42737; -.
DR SWISS-2DPAGE; P42737; -.
DR PaxDb; P42737; -.
DR PRIDE; P42737; -.
DR EnsemblPlants; AT5G14740.1; AT5G14740.1; AT5G14740. [P42737-1]
DR EnsemblPlants; AT5G14740.2; AT5G14740.2; AT5G14740. [P42737-2]
DR EnsemblPlants; AT5G14740.6; AT5G14740.6; AT5G14740. [P42737-2]
DR EnsemblPlants; AT5G14740.7; AT5G14740.7; AT5G14740. [P42737-2]
DR EnsemblPlants; AT5G14740.8; AT5G14740.8; AT5G14740. [P42737-2]
DR EnsemblPlants; AT5G14740.9; AT5G14740.9; AT5G14740. [P42737-2]
DR GeneID; 831326; -.
DR Gramene; AT5G14740.1; AT5G14740.1; AT5G14740. [P42737-1]
DR Gramene; AT5G14740.2; AT5G14740.2; AT5G14740. [P42737-2]
DR Gramene; AT5G14740.6; AT5G14740.6; AT5G14740. [P42737-2]
DR Gramene; AT5G14740.7; AT5G14740.7; AT5G14740. [P42737-2]
DR Gramene; AT5G14740.8; AT5G14740.8; AT5G14740. [P42737-2]
DR Gramene; AT5G14740.9; AT5G14740.9; AT5G14740. [P42737-2]
DR KEGG; ath:AT5G14740; -.
DR Araport; AT5G14740; -.
DR TAIR; locus:2185460; AT5G14740.
DR eggNOG; KOG1578; Eukaryota.
DR HOGENOM; CLU_053879_5_0_1; -.
DR InParanoid; P42737; -.
DR OMA; DLYVMRT; -.
DR OrthoDB; 1136193at2759; -.
DR UniPathway; UPA00322; -.
DR PRO; PR:P42737; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42737; baseline and differential.
DR Genevisible; P42737; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Cytoplasm; Lyase;
KW Phosphoprotein; Plastid; Reference proteome; S-nitrosylation;
KW Transit peptide; Zinc.
FT TRANSIT 1..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..331
FT /note="Beta carbonic anhydrase 2, chloroplastic"
FT /id="PRO_0000077458"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 275
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P27140"
FT VAR_SEQ 1..73
FT /note="MVPFWTTVSRNGSSDSETTLQSASKATKQYKYPSLRPSHRLSLLFLFPFHLS
FT ANGACFRCTCFSHFKLELRRM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19423640, ECO:0000303|PubMed:7520589"
FT /id="VSP_055068"
FT CONFLICT 109..110
FT /note="EL -> DV (in Ref. 5; AAA50156)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="LL -> RC (in Ref. 5; AAA50156)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="D -> A (in Ref. 5; AAA50156)"
FT /evidence="ECO:0000305"
FT INIT_MET P42737-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES P42737-2:2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 331 AA; 36615 MW; 31F5B61B9D262254 CRC64;
MVPFWTTVSR NGSSDSETTL QSASKATKQY KYPSLRPSHR LSLLFLFPFH LSANGACFRC
TCFSHFKLEL RRMGNESYED AIEALKKLLI EKDDLKDVAA AKVKKITAEL QAASSSDSKS
FDPVERIKEG FVTFKKEKYE TNPALYGELA KGQSPKYMVF ACSDSRVCPS HVLDFHPGDA
FVVRNIANMV PPFDKVKYAG VGAAIEYAVL HLKVENIVVI GHSACGGIKG LMSFPLDGNN
STDFIEDWVK ICLPAKSKVL AESESSAFED QCGRCEREAV NVSLANLLTY PFVREGVVKG
TLALKGGYYD FVNGSFELWE LQFGISPVHS I
