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Beta carbonic anhydrase 1, chloroplastic (AtbCA1) (AtbetaCA1) (EC 4.2.1.1) (Beta carbonate dehydratase 1) (Protein SALICYLIC ACID-BINDING PROTEIN 3) (AtSABP3)

 BCA1_ARATH              Reviewed;         347 AA.
P27140; Q0WWA9; Q56WK1; Q8RWW2; Q93VR8;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
21-NOV-2003, sequence version 2.
30-AUG-2017, entry version 145.
RecName: Full=Beta carbonic anhydrase 1, chloroplastic {ECO:0000303|PubMed:17407539};
Short=AtbCA1;
Short=AtbetaCA1;
EC=4.2.1.1 {ECO:0000255|RuleBase:RU003956};
AltName: Full=Beta carbonate dehydratase 1;
AltName: Full=Protein SALICYLIC ACID-BINDING PROTEIN 3;
Short=AtSABP3;
Flags: Precursor;
Name=BCA1 {ECO:0000303|PubMed:17407539};
Synonyms=CA1 {ECO:0000303|PubMed:20010812}, SABP3;
OrderedLocusNames=At3g01500 {ECO:0000312|Araport:AT3G01500};
ORFNames=F4P13.5 {ECO:0000312|EMBL:CAA46508.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. C24; TISSUE=Leaf;
PubMed=1463847; DOI=10.1007/BF00028900;
Raines C., Horsnell P.R., Holder C., Lloyd J.C.;
"Arabidopsis thaliana carbonic anhydrase: cDNA sequence and effect of
CO2 on mRNA levels.";
Plant Mol. Biol. 20:1143-1148(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=7520589; DOI=10.1104/pp.105.2.707;
Fett J.P., Coleman J.R.;
"Characterization and expression of two cDNAs encoding carbonic
anhydrase in Arabidopsis thaliana.";
Plant Physiol. 105:707-713(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, AND
NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=17407539; DOI=10.1111/j.1365-3040.2007.01651.x;
Fabre N., Reiter I.M., Becuwe-Linka N., Genty B., Rumeau D.;
"Characterization and expression analysis of genes encoding alpha and
beta carbonic anhydrases in Arabidopsis.";
Plant Cell Environ. 30:617-629(2007).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18434607; DOI=10.1104/pp.108.118661;
Ferreira F.J., Guo C., Coleman J.R.;
"Reduction of plastid-localized carbonic anhydrase activity results in
reduced Arabidopsis seedling survivorship.";
Plant Physiol. 147:585-594(2008).
[9]
FUNCTION, S-NITROSYLATION AT CYS-280, 3D-STRUCTURE MODELING,
MUTAGENESIS OF CYS-280, SALICYLIC ACID-BINDING, AND DISRUPTION
PHENOTYPE.
PubMed=19017644; DOI=10.1074/jbc.M806782200;
Wang Y.Q., Feechan A., Yun B.W., Shafiei R., Hofmann A., Taylor P.,
Xue P., Yang F.Q., Xie Z.S., Pallas J.A., Chu C.C., Loake G.J.;
"S-nitrosylation of AtSABP3 antagonizes the expression of plant
immunity.";
J. Biol. Chem. 284:2131-2137(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[11]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=20010812; DOI=10.1038/ncb2009;
Hu H., Boisson-Dernier A., Israelsson-Nordstrom M., Bohmer M., Xue S.,
Ries A., Godoski J., Kuhn J.M., Schroeder J.I.;
"Carbonic anhydrases are upstream regulators of CO2-controlled
stomatal movements in guard cells.";
Nat. Cell Biol. 12:87-93(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203 AND SER-266, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-114, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-113, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[14]
FUNCTION.
PubMed=25043023; DOI=10.1038/nature13452;
Engineer C.B., Ghassemian M., Anderson J.C., Peck S.C., Hu H.,
Schroeder J.I.;
"Carbonic anhydrases, EPF2 and a novel protease mediate CO2 control of
stomatal development.";
Nature 513:246-250(2014).
-!- FUNCTION: Reversible hydration of carbon dioxide. Required for
photosynthesis in cotyledons. Binds salicylic acid. Together with
BCA4, involved in the CO(2) signaling pathway which controls gas-
exchange between plants and the atmosphere by modulating stomatal
development and movements. Promotes water use efficiency.
{ECO:0000269|PubMed:18434607, ECO:0000269|PubMed:19017644,
ECO:0000269|PubMed:20010812, ECO:0000269|PubMed:25043023}.
-!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
{ECO:0000255|RuleBase:RU003956}.
-!- SUBUNIT: Homohexamer.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:17407539}. Cell membrane
{ECO:0000269|PubMed:20010812}; Peripheral membrane protein
{ECO:0000269|PubMed:20010812}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P27140-1; Sequence=Displayed;
Name=2;
IsoId=P27140-2; Sequence=VSP_009004;
Name=3;
IsoId=P27140-3; Sequence=VSP_009003;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
leaves, stems, flowers and siliques. Accumulates in both guard
cells and mesophyll cells. {ECO:0000269|PubMed:17407539,
ECO:0000269|PubMed:20010812}.
-!- INDUCTION: Expression reduced by 70% under dark conditions.
-!- PTM: S-nitrosylation at Cys-280 is up-regulated during nitrosative
burst and suppresses both binding of salicylic acid and carbonic
anhydrase activity. S-nitrosylated in response to an avirulent but
not to a virulent bacterial strain. {ECO:0000269|PubMed:19017644}.
-!- DISRUPTION PHENOTYPE: Reduced levels of seedling establishment
associated with altered cotyledon photosynthetic performance at
the onset of phototrophic growth and prior to the development of
true leaves. These phenotypes are reversed in high CO(2) or
sucrose supplemented conditions. Decreased resistance against
avirulent bacteria. In plants lacking both BCA1 and BCA4, impaired
CO(2)-regulation of stomatal movements associated with reduced
beta carbonic anhydrase activity in guard cells, and increased
stomatal density. {ECO:0000269|PubMed:18434607,
ECO:0000269|PubMed:19017644, ECO:0000269|PubMed:20010812}.
-!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD94771.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X65541; CAA46508.1; -; mRNA.
EMBL; AC009325; AAF01535.1; -; Genomic_DNA.
EMBL; CP002686; AEE73675.1; -; Genomic_DNA.
EMBL; CP002686; AEE73676.1; -; Genomic_DNA.
EMBL; CP002686; AEE73677.1; -; Genomic_DNA.
EMBL; AF428284; AAL16116.1; -; mRNA.
EMBL; AF428459; AAL16228.1; -; mRNA.
EMBL; AY056175; AAL07024.1; -; mRNA.
EMBL; AY062785; AAL32863.1; -; mRNA.
EMBL; AY081658; AAM10220.1; -; mRNA.
EMBL; AY091066; AAM13886.1; -; mRNA.
EMBL; AK226447; BAE98589.1; -; mRNA.
EMBL; AK222039; BAD94771.1; ALT_INIT; mRNA.
PIR; S28412; S28412.
RefSeq; NP_186799.2; NM_111016.4. [P27140-1]
RefSeq; NP_850490.1; NM_180159.2. [P27140-3]
RefSeq; NP_850491.1; NM_180160.4. [P27140-2]
UniGene; At.21999; -.
ProteinModelPortal; P27140; -.
SMR; P27140; -.
BioGrid; 6467; 15.
IntAct; P27140; 2.
STRING; 3702.AT3G01500.2; -.
iPTMnet; P27140; -.
SWISS-2DPAGE; P27140; -.
PaxDb; P27140; -.
PRIDE; P27140; -.
EnsemblPlants; AT3G01500.1; AT3G01500.1; AT3G01500. [P27140-3]
EnsemblPlants; AT3G01500.2; AT3G01500.2; AT3G01500. [P27140-1]
EnsemblPlants; AT3G01500.3; AT3G01500.3; AT3G01500. [P27140-2]
GeneID; 821134; -.
Gramene; AT3G01500.1; AT3G01500.1; AT3G01500.
Gramene; AT3G01500.2; AT3G01500.2; AT3G01500.
Gramene; AT3G01500.3; AT3G01500.3; AT3G01500.
KEGG; ath:AT3G01500; -.
Araport; AT3G01500; -.
TAIR; locus:2084198; AT3G01500.
eggNOG; KOG1578; Eukaryota.
eggNOG; COG0288; LUCA.
HOGENOM; HOG000125183; -.
InParanoid; P27140; -.
KO; K01673; -.
OMA; INSWCLT; -.
OrthoDB; EOG09360LL4; -.
PhylomeDB; P27140; -.
BioCyc; ARA:AT3G01500-MONOMER; -.
BioCyc; MetaCyc:AT3G01500-MONOMER; -.
PRO; PR:P27140; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P27140; baseline and differential.
Genevisible; P27140; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0010319; C:stromule; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0004089; F:carbonate dehydratase activity; IMP:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015976; P:carbon utilization; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IDA:TAIR.
GO; GO:2000122; P:negative regulation of stomatal complex development; IGI:TAIR.
GO; GO:0015979; P:photosynthesis; IMP:UniProtKB.
GO; GO:0010119; P:regulation of stomatal movement; IGI:TAIR.
GO; GO:0010037; P:response to carbon dioxide; IGI:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
Gene3D; 3.40.1050.10; -; 1.
InterPro; IPR001765; Carbonic_anhydrase.
InterPro; IPR015892; Carbonic_anhydrase_CS.
Pfam; PF00484; Pro_CA; 1.
SMART; SM00947; Pro_CA; 1.
SUPFAM; SSF53056; SSF53056; 1.
PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Chloroplast;
Complete proteome; Lyase; Membrane; Phosphoprotein; Plastid;
Reference proteome; S-nitrosylation; Transit peptide; Zinc.
TRANSIT 1 113 Chloroplast.
{ECO:0000244|PubMed:22223895,
ECO:0000305}.
CHAIN 114 347 Beta carbonic anhydrase 1, chloroplastic.
/FTId=PRO_0000004267.
COMPBIAS 39 50 Poly-Ser.
MOD_RES 114 114 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000250|UniProtKB:P42737}.
MOD_RES 203 203 Phosphotyrosine.
{ECO:0000244|PubMed:22092075}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
MOD_RES 280 280 S-nitrosocysteine.
{ECO:0000269|PubMed:19017644}.
VAR_SEQ 1 77 Missing (in isoform 3).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_009003.
VAR_SEQ 337 347 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172,
ECO:0000303|PubMed:1463847,
ECO:0000303|PubMed:7520589,
ECO:0000303|Ref.6}.
/FTId=VSP_009004.
MUTAGEN 280 280 C->S: Loss of nitrosylation and decreased
carbonic anhydrase activity, but no
effect on salicylic acid binding.
{ECO:0000269|PubMed:19017644}.
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


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