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Database: UniProt
Entry: BCA5_ARATH
LinkDB: BCA5_ARATH
Original site: BCA5_ARATH 
ID   BCA5_ARATH              Reviewed;         301 AA.
AC   Q94CE3; B9DHL2; F4JJ03; O81875;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Beta carbonic anhydrase 5, chloroplastic;
DE            Short=AtbCA5;
DE            Short=AtbetaCA5;
DE            EC=4.2.1.1;
DE   AltName: Full=Beta carbonate dehydratase 5;
DE   Flags: Precursor;
GN   Name=BCA5; OrderedLocusNames=At4g33580; ORFNames=T16L1.70;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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].
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].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-301.
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   [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).
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: Plastid, chloroplast
CC       {ECO:0000269|PubMed:17407539}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q94CE3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q94CE3-2; Sequence=VSP_055072;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
CC       leaves, stems, flowers and siliques. {ECO:0000269|PubMed:17407539}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA20571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80075.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL031394; CAA20571.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161583; CAB80075.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86248.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86249.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66692.1; -; Genomic_DNA.
DR   EMBL; AY034930; AAK59437.1; -; mRNA.
DR   EMBL; AY122986; AAM67519.1; -; mRNA.
DR   EMBL; AK221870; BAD94173.1; -; mRNA.
DR   EMBL; AY088420; AAM65957.1; -; mRNA.
DR   EMBL; AK317565; BAH20229.1; -; mRNA.
DR   PIR; T04975; T04975.
DR   RefSeq; NP_001031784.1; NM_001036707.1. [Q94CE3-2]
DR   RefSeq; NP_001328574.1; NM_001342222.1. [Q94CE3-1]
DR   RefSeq; NP_567928.1; NM_119514.4. [Q94CE3-1]
DR   AlphaFoldDB; Q94CE3; -.
DR   SMR; Q94CE3; -.
DR   BioGRID; 14780; 1.
DR   STRING; 3702.Q94CE3; -.
DR   iPTMnet; Q94CE3; -.
DR   PaxDb; 3702-AT4G33580-2; -.
DR   ProteomicsDB; 240751; -. [Q94CE3-1]
DR   EnsemblPlants; AT4G33580.1; AT4G33580.1; AT4G33580. [Q94CE3-1]
DR   EnsemblPlants; AT4G33580.2; AT4G33580.2; AT4G33580. [Q94CE3-2]
DR   EnsemblPlants; AT4G33580.3; AT4G33580.3; AT4G33580. [Q94CE3-1]
DR   GeneID; 829498; -.
DR   Gramene; AT4G33580.1; AT4G33580.1; AT4G33580. [Q94CE3-1]
DR   Gramene; AT4G33580.2; AT4G33580.2; AT4G33580. [Q94CE3-2]
DR   Gramene; AT4G33580.3; AT4G33580.3; AT4G33580. [Q94CE3-1]
DR   KEGG; ath:AT4G33580; -.
DR   Araport; AT4G33580; -.
DR   TAIR; AT4G33580; BCA5.
DR   eggNOG; KOG1578; Eukaryota.
DR   HOGENOM; CLU_053879_0_0_1; -.
DR   InParanoid; Q94CE3; -.
DR   OMA; FIQNWVV; -.
DR   OrthoDB; 5392875at2759; -.
DR   PhylomeDB; Q94CE3; -.
DR   PRO; PR:Q94CE3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q94CE3; baseline and differential.
DR   Genevisible; Q94CE3; AT.
DR   GO; GO:0009507; C:chloroplast; 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; Carbonic anhydrase; 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:SF12; BETA CARBONIC ANHYDRASE 5, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR   PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Lyase; Phosphoprotein; Plastid;
KW   Reference proteome; S-nitrosylation; Transit peptide; Zinc.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..301
FT                   /note="Beta carbonic anhydrase 5, chloroplastic"
FT                   /id="PRO_0000429737"
FT   MOD_RES         65
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P42737"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42737"
FT   MOD_RES         231
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P27140"
FT   VAR_SEQ         98
FT                   /note="M -> IR (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_055072"
SQ   SEQUENCE   301 AA;  33401 MW;  6CE4F5FEE2B38052 CRC64;
     MAATPTHFSV SHDPFSSTSL LNLQTQAIFG PNHSLKTTQL RIPASFRRKA TNLQVMASGK
     TPGLTQEANG VAIDRQNNTD VFDDMKQRFL AFKKLKYMDD FEHYKNLADA QAPKFLVIAC
     ADSRVCPSAV LGFQPGDAFT VRNIANLVPP YESGPTETKA ALEFSVNTLN VENILVIGHS
     RCGGIQALMK MEDEGDSRSF IHNWVVVGKK AKESTKAVAS NLHFDHQCQH CEKASINHSL
     ERLLGYPWIE EKVRQGSLSL HGGYYNFVDC TFEKWTVDYA ASRGKKKEGS GIAVKDRSVW
     S
//
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