Reviewed, UniProtKB/Swiss-Prot P27140 (CAHC_ARATH)

Names and origin

Protein names

Recommended name:
    Carbonic anhydrase, chloroplastic
    EC=4.2.1.1
Alternative name(s):
    Carbonate dehydratase

Gene names

Name:	CA1
Ordered Locus Names:	At3g01500
ORF Names:	F4P13.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Subunit structure	Homohexamer.
Subcellular location	Plastid › chloroplast stroma. Ref.6
Induction	Expression reduced by 70% under dark conditions.
Sequence similarities	Belongs to the beta-class carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Zinc
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbon utilization Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from expression pattern. Source: TAIR response to cold Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Ref.6 Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR chloroplast thylakoid membrane Inferred from direct assay. Source: TAIR
Molecular function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449468,EBI-449157

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P27140-1)

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.

Isoform 2 (identifier: P27140-2)

The sequence of this isoform differs from the canonical sequence as follows:
     337-347: Missing.

Isoform 3 (identifier: P27140-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 113	113	Chloroplast Potential
	Chain	114 – 347	234	Carbonic anhydrase, chloroplastic		PRO_0000004267
Regions
	Compositional bias	39 – 50	12	Poly-Ser
Natural variations
	Alternative sequence	1 – 77	77	Missing in isoform 3.		VSP_009003
	Alternative sequence	337 – 347	11	Missing in isoform 2.		VSP_009004

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 21, 2003. Version 2. Checksum: 9061FF3EF64CAFD7	FASTA	347	37,450
	10 20 30 40 50 60 MSTAPLSGFF LTSLSPSQSS LQKLSLRTSS TVACLPPASS SSSSSSSSSS RSVPTLIRNE 70 80 90 100 110 120 PVFAAPAPII APYWSEEMGT EAYDEAIEAL KKLLIEKEEL KTVAAAKVEQ ITAALQTGTS 130 140 150 160 170 180 SDKKAFDPVE TIKQGFIKFK KEKYETNPAL YGELAKGQSP KYMVFACSDS RVCPSHVLDF 190 200 210 220 230 240 QPGDAFVVRN IANMVPPFDK VKYGGVGAAI EYAVLHLKVE NIVVIGHSAC GGIKGLMSFP 250 260 270 280 290 300 LDGNNSTDFI EDWVKICLPA KSKVISELGD SAFEDQCGRC EREAVNVSLA NLLTYPFVRE 310 320 330 340 GLVKGTLALK GGYYDFVKGA FELWGLEFGL SETSSVKDVA TILHWKL
	Isoform 2. Checksum: F1DAEA0AF21D96B0	FASTA	336	36,144
	10 20 30 40 50 60 MSTAPLSGFF LTSLSPSQSS LQKLSLRTSS TVACLPPASS SSSSSSSSSS RSVPTLIRNE 70 80 90 100 110 120 PVFAAPAPII APYWSEEMGT EAYDEAIEAL KKLLIEKEEL KTVAAAKVEQ ITAALQTGTS 130 140 150 160 170 180 SDKKAFDPVE TIKQGFIKFK KEKYETNPAL YGELAKGQSP KYMVFACSDS RVCPSHVLDF 190 200 210 220 230 240 QPGDAFVVRN IANMVPPFDK VKYGGVGAAI EYAVLHLKVE NIVVIGHSAC GGIKGLMSFP 250 260 270 280 290 300 LDGNNSTDFI EDWVKICLPA KSKVISELGD SAFEDQCGRC EREAVNVSLA NLLTYPFVRE 310 320 330 GLVKGTLALK GGYYDFVKGA FELWGLEFGL SETSSV
	Isoform 3. Checksum: 4A5DED1347C40124	FASTA	270	29,504
	10 20 30 40 50 60 MGTEAYDEAI EALKKLLIEK EELKTVAAAK VEQITAALQT GTSSDKKAFD PVETIKQGFI 70 80 90 100 110 120 KFKKEKYETN PALYGELAKG QSPKYMVFAC SDSRVCPSHV LDFQPGDAFV VRNIANMVPP 130 140 150 160 170 180 FDKVKYGGVG AAIEYAVLHL KVENIVVIGH SACGGIKGLM SFPLDGNNST DFIEDWVKIC 190 200 210 220 230 240 LPAKSKVISE LGDSAFEDQC GRCEREAVNV SLANLLTYPF VREGLVKGTL ALKGGYYDFV 250 260 270 KGAFELWGLE FGLSETSSVK DVATILHWKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis thaliana carbonic anhydrase: cDNA sequence and effect of CO2 on mRNA levels." Raines C., Horsnell P.R., Holder C., Lloyd J.C. Plant Mol. Biol. 20:1143-1148(1992) [PubMed: 1463847] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: cv. C24. Tissue: Leaf.
[2]	"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: 7520589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." 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. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." 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. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia.
[6]	"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: 12766230] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X65541 mRNA. Translation: CAA46508.1. AC009325 Genomic DNA. Translation: AAF01535.1. AF428284 mRNA. Translation: AAL16116.1. AF428459 mRNA. Translation: AAL16228.1. AY056175 mRNA. Translation: AAL07024.1. AY062785 mRNA. Translation: AAL32863.1. AY081658 mRNA. Translation: AAM10220.1. AY091066 mRNA. Translation: AAM13886.1. AK226447 mRNA. Translation: BAE98589.1.
IPI	IPI00518464. IPI00536510. IPI00544626.
PIR	S28412.
RefSeq	NP_186799.2.
UniGene	At.21999
3D structure databases
HSSP	HSSP built from PDB template 1EKJ based on UniProtKB P17067.
SMR	P27140. Positions 130-336.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27140. 1 interaction.
2-D gel databases
SWISS-2DPAGE	P27140.
Proteomic databases
PRIDE	P27140.
ProMEX	P27140.
Genome annotation databases
GeneID	821134.
GenomeReviews	Gene locus AT3G01500 in contig BA000014_GR.
KEGG	ath:AT3G01500.
Organism-specific databases
TAIR	At3g01500.
Phylogenomic databases
OMA	P27140. VATILHW.
Enzyme and pathway databases
BRENDA	4.2.1.1. 302.
Gene expression databases
ArrayExpress	P27140.
Family and domain databases
InterPro	IPR001765. Carbonic_anhydrase. IPR015892. Carbonic_anhydrase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1050.10. CO_anhd_prok_pln. 1 hit.
PANTHER	PTHR11002. Carbonic_anhydrase. 1 hit.
Pfam	PF00484. Pro_CA. 1 hit. [Graphical view]
PROSITE	PS00704. PROK_CO2_ANHYDRASE_1. 1 hit. PS00705. PROK_CO2_ANHYDRASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAHC_ARATH

Accession

Primary (citable) accession number: P27140
Secondary accession number(s): Q0WWA9, Q8RWW2, Q93VR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	November 21, 2003
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)