BCA4_ARATH
ID BCA4_ARATH Reviewed; 280 AA.
AC Q94CE4; O64595; Q56Y84;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta carbonic anhydrase 4 {ECO:0000303|PubMed:17407539};
DE Short=AtbCA4 {ECO:0000303|PubMed:17407539};
DE Short=AtbetaCA4 {ECO:0000303|PubMed:17407539};
DE EC=4.2.1.1 {ECO:0000269|PubMed:20010812};
DE AltName: Full=Beta carbonate dehydratase 4 {ECO:0000303|PubMed:17407539};
GN Name=BCA4 {ECO:0000303|PubMed:17407539};
GN Synonyms=CA4 {ECO:0000303|PubMed:20010812};
GN OrderedLocusNames=At1g70410 {ECO:0000312|Araport:AT1G70410};
GN ORFNames=F17O7.5 {ECO:0000312|EMBL:AAC18799.1};
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 [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 1).
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 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-280 (ISOFORM 1/2).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP SUBCELLULAR 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
RN [10]
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).
RN [11]
RP INTERACTION WITH DTX56.
RX PubMed=25599916; DOI=10.1038/ncomms7057;
RA Tian W., Hou C., Ren Z., Pan Y., Jia J., Zhang H., Bai F., Zhang P.,
RA Zhu H., He Y., Luo S., Li L., Luan S.;
RT "A molecular pathway for CO(2) response in Arabidopsis guard cells.";
RL Nat. Commun. 6:6057-6057(2015).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. Together with BCA1,
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: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:0000269|PubMed:20010812};
CC -!- SUBUNIT: Interacts with DTX56. {ECO:0000269|PubMed:25599916}.
CC -!- INTERACTION:
CC Q94CE4; O49660: DTX56; NbExp=2; IntAct=EBI-4430840, EBI-11174814;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17407539,
CC ECO:0000269|PubMed:20010812}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17407539, ECO:0000269|PubMed:20010812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94CE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94CE4-2; Sequence=VSP_055071;
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 -!- DISRUPTION PHENOTYPE: In plants lacking both BCA1 and BCA4, impaired
CC CO(2)-regulation of stomatal movements associated with reduced beta
CC carbonic anhydrase activity in guard cells, and increased stomatal
CC density. {ECO:0000269|PubMed:20010812}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94475.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC003671; AAC18799.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35057.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35058.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35059.1; -; Genomic_DNA.
DR EMBL; AY034926; AAK59433.1; -; mRNA.
DR EMBL; AY113922; AAM44970.1; -; mRNA.
DR EMBL; AY087827; AAM65380.1; -; mRNA.
DR EMBL; AK221439; BAD94475.1; ALT_INIT; mRNA.
DR PIR; T01481; T01481.
DR RefSeq; NP_177198.1; NM_105709.4. [Q94CE4-1]
DR RefSeq; NP_849872.1; NM_179541.3. [Q94CE4-2]
DR RefSeq; NP_974119.1; NM_202390.3. [Q94CE4-2]
DR AlphaFoldDB; Q94CE4; -.
DR SMR; Q94CE4; -.
DR BioGRID; 28597; 10.
DR IntAct; Q94CE4; 9.
DR STRING; 3702.AT1G70410.2; -.
DR iPTMnet; Q94CE4; -.
DR PaxDb; Q94CE4; -.
DR PRIDE; Q94CE4; -.
DR ProteomicsDB; 240750; -. [Q94CE4-1]
DR EnsemblPlants; AT1G70410.1; AT1G70410.1; AT1G70410. [Q94CE4-2]
DR EnsemblPlants; AT1G70410.2; AT1G70410.2; AT1G70410. [Q94CE4-1]
DR EnsemblPlants; AT1G70410.3; AT1G70410.3; AT1G70410. [Q94CE4-2]
DR GeneID; 843377; -.
DR Gramene; AT1G70410.1; AT1G70410.1; AT1G70410. [Q94CE4-2]
DR Gramene; AT1G70410.2; AT1G70410.2; AT1G70410. [Q94CE4-1]
DR Gramene; AT1G70410.3; AT1G70410.3; AT1G70410. [Q94CE4-2]
DR KEGG; ath:AT1G70410; -.
DR Araport; AT1G70410; -.
DR TAIR; locus:2016109; AT1G70410.
DR eggNOG; KOG1578; Eukaryota.
DR InParanoid; Q94CE4; -.
DR OrthoDB; 1136193at2759; -.
DR PhylomeDB; Q94CE4; -.
DR BioCyc; ARA:AT1G70410-MON; -.
DR PRO; PR:Q94CE4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94CE4; baseline and differential.
DR Genevisible; Q94CE4; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:2000122; P:negative regulation of stomatal complex development; IGI:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IGI:TAIR.
DR GO; GO:0010037; P:response to carbon dioxide; IGI: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; Coiled coil; Lyase;
KW Membrane; Phosphoprotein; Reference proteome; S-nitrosylation; Zinc.
FT CHAIN 1..280
FT /note="Beta carbonic anhydrase 4"
FT /id="PRO_0000429736"
FT COILED 47..76
FT /evidence="ECO:0000255"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P42737"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42737"
FT MOD_RES 223
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P27140"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_055071"
FT INIT_MET Q94CE4-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q94CE4-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 280 AA; 30836 MW; E7342B72D7AEDEF8 CRC64;
MAPAFGKCFM FCCAKTSPEK DEMATESYEA AIKGLNDLLS TKADLGNVAA AKIKALTAEL
KELDSSNSDA IERIKTGFTQ FKTEKYLKNS TLFNHLAKTQ TPKFLVFACS DSRVCPSHIL
NFQPGEAFVV RNIANMVPPF DQKRHSGVGA AVEYAVVHLK VENILVIGHS CCGGIKGLMS
IEDDAAPTQS DFIENWVKIG ASARNKIKEE HKDLSYDDQC NKCEKEAVNV SLGNLLSYPF
VRAEVVKNTL AIRGGHYNFV KGTFDLWELD FKTTPAFAFS
