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Protein

Beta carbonic anhydrase 2, chloroplastic

Gene

BCA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide. This isoform ensures the supply of bicarbonate for pep carboxylase.

Catalytic activityi

H2CO3 = CO2 + H2O.

Pathwayi: C4 acid pathway

This protein is involved in the pathway C4 acid pathway, which is part of Photosynthesis.
View all proteins of this organism that are known to be involved in the pathway C4 acid pathway and in Photosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Zinc

Enzyme and pathway databases

BioCyciARA:GQT-159-MONOMER.
ARA:GQT-1930-MONOMER.
ARA:GQT-1931-MONOMER.
ARA:GQT-247-MONOMER.
UniPathwayiUPA00322.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta carbonic anhydrase 2, chloroplastic (EC:4.2.1.1)
Short name:
AtbCA2
Short name:
AtbetaCA2
Alternative name(s):
Beta carbonate dehydratase 2
Gene namesi
Name:BCA2
Synonyms:CA18, CA2
Ordered Locus Names:At5g14740
ORF Names:T9L3.40
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G14740.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Cytoplasm, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7171ChloroplastSequence analysisAdd
BLAST
Chaini72 – 331260Beta carbonic anhydrase 2, chloroplasticPRO_0000077458Add
BLAST
Isoform 2 (identifier: P42737-2)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071PhosphothreonineCombined sources
Modified residuei170 – 1701PhosphoserineCombined sources
Modified residuei198 – 1981PhosphotyrosineCombined sources
Modified residuei275 – 2751S-nitrosocysteineBy similarity
Isoform 2 (identifier: P42737-2)
Modified residuei2 – 21N-acetylglycineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP42737.
PRIDEiP42737.

2D gel databases

SWISS-2DPAGEP42737.

PTM databases

iPTMnetiP42737.

Expressioni

Tissue specificityi

Strongly expressed in aerial tissues including leaves, stems, flowers and siliques. Accumulates in mesophyll cells.2 Publications

Inductioni

Expression reduced by 20% under dark conditions.

Gene expression databases

ExpressionAtlasiP42737. baseline and differential.
GenevisibleiP42737. AT.

Interactioni

Protein-protein interaction databases

BioGridi16603. 2 interactions.
IntActiP42737. 50 interactions.
STRINGi3702.AT5G14740.1.

Structurei

3D structure databases

ProteinModelPortaliP42737.
SMRiP42737. Positions 125-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1578. Eukaryota.
COG0288. LUCA.
HOGENOMiHOG000125183.
InParanoidiP42737.
KOiK01673.
OMAiASINGWC.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. According to EST sequences.

Isoform 1 (identifier: P42737-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVPFWTTVSR NGSSDSETTL QSASKATKQY KYPSLRPSHR LSLLFLFPFH
60 70 80 90 100
LSANGACFRC TCFSHFKLEL RRMGNESYED AIEALKKLLI EKDDLKDVAA
110 120 130 140 150
AKVKKITAEL QAASSSDSKS FDPVERIKEG FVTFKKEKYE TNPALYGELA
160 170 180 190 200
KGQSPKYMVF ACSDSRVCPS HVLDFHPGDA FVVRNIANMV PPFDKVKYAG
210 220 230 240 250
VGAAIEYAVL HLKVENIVVI GHSACGGIKG LMSFPLDGNN STDFIEDWVK
260 270 280 290 300
ICLPAKSKVL AESESSAFED QCGRCEREAV NVSLANLLTY PFVREGVVKG
310 320 330
TLALKGGYYD FVNGSFELWE LQFGISPVHS I
Length:331
Mass (Da):36,615
Last modified:July 9, 2014 - v3
Checksum:i31F5B61B9D262254
GO
Isoform 2 (identifier: P42737-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MVPFWTTVSRNGSSDSETTLQSASKATKQYKYPSLRPSHRLSLLFLFPFHLSANGACFRCTCFSHFKLELRRM → M

Show »
Length:259
Mass (Da):28,344
Checksum:iE329D4DAEF350CE0
GO

Sequence cautioni

The sequence AAA50156.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG40063.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG41445.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAN31799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAN31810.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAC01873.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1102EL → DV in AAA50156 (PubMed:7520589).Curated
Sequence conflicti287 – 2882LL → RC in AAA50156 (PubMed:7520589).Curated
Sequence conflicti310 – 3101D → A in AAA50156 (PubMed:7520589).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7373MVPFW…ELRRM → M in isoform 2. 3 PublicationsVSP_055068Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391149 Genomic DNA. Translation: CAC01873.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED92068.1.
CP002688 Genomic DNA. Translation: AED92069.1.
AF324712 mRNA. Translation: AAG40063.1. Different initiation.
AF326863 mRNA. Translation: AAG41445.1. Different initiation.
AF339686 mRNA. Translation: AAK00368.1.
AF428428 mRNA. Translation: AAL16197.1.
BT000652 mRNA. Translation: AAN31799.1. Different initiation.
BT000663 mRNA. Translation: AAN31810.1. Different initiation.
AK317585 mRNA. Translation: BAH20249.1.
L18901 mRNA. Translation: AAA50156.1. Different initiation.
Z26538 mRNA. Translation: CAA81309.1.
RefSeqiNP_568303.2. NM_121478.3. [P42737-1]
NP_974782.1. NM_203053.2. [P42737-2]
UniGeneiAt.23743.

Genome annotation databases

EnsemblPlantsiAT5G14740.1; AT5G14740.1; AT5G14740. [P42737-1]
AT5G14740.2; AT5G14740.2; AT5G14740. [P42737-2]
GeneIDi831326.
KEGGiath:AT5G14740.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL391149 Genomic DNA. Translation: CAC01873.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED92068.1.
CP002688 Genomic DNA. Translation: AED92069.1.
AF324712 mRNA. Translation: AAG40063.1. Different initiation.
AF326863 mRNA. Translation: AAG41445.1. Different initiation.
AF339686 mRNA. Translation: AAK00368.1.
AF428428 mRNA. Translation: AAL16197.1.
BT000652 mRNA. Translation: AAN31799.1. Different initiation.
BT000663 mRNA. Translation: AAN31810.1. Different initiation.
AK317585 mRNA. Translation: BAH20249.1.
L18901 mRNA. Translation: AAA50156.1. Different initiation.
Z26538 mRNA. Translation: CAA81309.1.
RefSeqiNP_568303.2. NM_121478.3. [P42737-1]
NP_974782.1. NM_203053.2. [P42737-2]
UniGeneiAt.23743.

3D structure databases

ProteinModelPortaliP42737.
SMRiP42737. Positions 125-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16603. 2 interactions.
IntActiP42737. 50 interactions.
STRINGi3702.AT5G14740.1.

PTM databases

iPTMnetiP42737.

2D gel databases

SWISS-2DPAGEP42737.

Proteomic databases

PaxDbiP42737.
PRIDEiP42737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G14740.1; AT5G14740.1; AT5G14740. [P42737-1]
AT5G14740.2; AT5G14740.2; AT5G14740. [P42737-2]
GeneIDi831326.
KEGGiath:AT5G14740.

Organism-specific databases

TAIRiAT5G14740.

Phylogenomic databases

eggNOGiKOG1578. Eukaryota.
COG0288. LUCA.
HOGENOMiHOG000125183.
InParanoidiP42737.
KOiK01673.
OMAiASINGWC.

Enzyme and pathway databases

UniPathwayiUPA00322.
BioCyciARA:GQT-159-MONOMER.
ARA:GQT-1930-MONOMER.
ARA:GQT-1931-MONOMER.
ARA:GQT-247-MONOMER.

Miscellaneous databases

PROiP42737.

Gene expression databases

ExpressionAtlasiP42737. baseline and differential.
GenevisibleiP42737. AT.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-331 (ISOFORMS 1 AND 2).
    Strain: cv. Columbia.
  4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-331 (ISOFORM 2).
    Strain: cv. Columbia.
    Tissue: Flower and Silique.
  5. "Characterization and expression of two cDNAs encoding carbonic anhydrase in Arabidopsis thaliana."
    Fett J.P., Coleman J.R.
    Plant Physiol. 105:707-713(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-331 (ISOFORM 2).
    Strain: cv. Columbia.
    Tissue: Leaf.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 276-331 (ISOFORM 1/2).
    Strain: cv. Columbia.
    Tissue: Seedling.
  7. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  8. "Characterization and expression analysis of genes encoding alpha and beta carbonic anhydrases in Arabidopsis."
    Fabre N., Reiter I.M., Becuwe-Linka N., Genty B., Rumeau D.
    Plant Cell Environ. 30:617-629(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  9. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Carbonic anhydrases are upstream regulators of CO2-controlled stomatal movements in guard cells."
    Hu H., Boisson-Dernier A., Israelsson-Nordstrom M., Bohmer M., Xue S., Ries A., Godoski J., Kuhn J.M., Schroeder J.I.
    Nat. Cell Biol. 12:87-93(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Identification of phosphoproteins in Arabidopsis thaliana leaves using polyethylene glycol fractionation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry."
    Aryal U.K., Krochko J.E., Ross A.R.
    J. Proteome Res. 11:425-437(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-170 AND TYR-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBCA2_ARATH
AccessioniPrimary (citable) accession number: P42737
Secondary accession number(s): B9DHN2
, F4K874, Q42116, Q9FDZ0, Q9LER2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 9, 2014
Last modified: June 8, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.