BCA3_ARATH
ID BCA3_ARATH Reviewed; 258 AA.
AC Q9ZUC2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Beta carbonic anhydrase 3;
DE Short=AtbCA3;
DE Short=AtbetaCA3;
DE EC=4.2.1.1;
DE AltName: Full=Beta carbonate dehydratase 3;
DE Flags: Precursor;
GN Name=BCA3; OrderedLocusNames=At1g23730; ORFNames=F5O8.28;
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].
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 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: Cytoplasm, cytosol {ECO:0000269|PubMed:17407539}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
CC leaves, stems, flowers and siliques, and, to a lower extent, in roots.
CC {ECO:0000269|PubMed:17407539}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AC005990; AAC98028.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30426.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59400.1; -; Genomic_DNA.
DR EMBL; AY081265; AAL91154.1; -; mRNA.
DR EMBL; AY114551; AAM47870.1; -; mRNA.
DR PIR; D86371; D86371.
DR RefSeq; NP_001321762.1; NM_001332620.1.
DR RefSeq; NP_173785.1; NM_102221.5.
DR AlphaFoldDB; Q9ZUC2; -.
DR SMR; Q9ZUC2; -.
DR BioGRID; 24221; 4.
DR IntAct; Q9ZUC2; 4.
DR STRING; 3702.AT1G23730.1; -.
DR iPTMnet; Q9ZUC2; -.
DR PaxDb; Q9ZUC2; -.
DR PRIDE; Q9ZUC2; -.
DR ProteomicsDB; 240749; -.
DR EnsemblPlants; AT1G23730.1; AT1G23730.1; AT1G23730.
DR EnsemblPlants; AT1G23730.2; AT1G23730.2; AT1G23730.
DR GeneID; 838983; -.
DR Gramene; AT1G23730.1; AT1G23730.1; AT1G23730.
DR Gramene; AT1G23730.2; AT1G23730.2; AT1G23730.
DR KEGG; ath:AT1G23730; -.
DR Araport; AT1G23730; -.
DR TAIR; locus:2034797; AT1G23730.
DR eggNOG; KOG1578; Eukaryota.
DR HOGENOM; CLU_053879_5_0_1; -.
DR InParanoid; Q9ZUC2; -.
DR OMA; CAPAKNR; -.
DR OrthoDB; 1136193at2759; -.
DR PhylomeDB; Q9ZUC2; -.
DR BioCyc; ARA:AT1G23730-MON; -.
DR PRO; PR:Q9ZUC2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZUC2; baseline and differential.
DR Genevisible; Q9ZUC2; AT.
DR GO; GO:0005829; C:cytosol; 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.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Lyase; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Signal; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..258
FT /note="Beta carbonic anhydrase 3"
FT /id="PRO_0000429735"
FT COILED 24..54
FT /evidence="ECO:0000255"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42737"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42737"
FT MOD_RES 201
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P27140"
SQ SEQUENCE 258 AA; 28829 MW; F122A6B3F18E5946 CRC64;
MSTESYEDAI KRLGELLSKK SDLGNVAAAK IKKLTDELEE LDSNKLDAVE RIKSGFLHFK
TNNYEKNPTL YNSLAKSQTP KFLVFACADS RVSPSHILNF QLGEAFIVRN IANMVPPYDK
TKHSNVGAAL EYPITVLNVE NILVIGHSCC GGIKGLMAIE DNTAPTKTEF IENWIQICAP
AKNRIKQDCK DLSFEDQCTN CEKEAVNVSL GNLLSYPFVR ERVVKNKLAI RGAHYDFVKG
TFDLWELDFK TTPAFALS
