ATCA3_ARATH
ID ATCA3_ARATH Reviewed; 277 AA.
AC Q9FYE3; A0MFD7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alpha carbonic anhydrase 3;
DE Short=AtaCA3;
DE Short=AtalphaCA3;
DE EC=4.2.1.1;
DE AltName: Full=Alpha carbonate dehydratase 3;
DE Flags: Precursor;
GN Name=ACA3; OrderedLocusNames=At5g04180; ORFNames=F21E1.100;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP TISSUE SPECIFICITY, INDUCTION BY CO2, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC Note=Targeted to the chloroplast via a protein-targeting pathway that
CC uses the secretory system. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC {ECO:0000269|PubMed:17407539}.
CC -!- INDUCTION: Accumulates in low CO(2) conditions.
CC {ECO:0000269|PubMed:17407539}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28680.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL391716; CAC05500.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90708.1; -; Genomic_DNA.
DR EMBL; DQ446916; ABE66129.1; -; mRNA.
DR EMBL; DQ653263; ABK28680.1; ALT_SEQ; mRNA.
DR EMBL; AK221569; BAD95018.1; -; mRNA.
DR EMBL; AY088872; AAM67178.1; -; mRNA.
DR RefSeq; NP_196038.1; NM_120500.3.
DR AlphaFoldDB; Q9FYE3; -.
DR SMR; Q9FYE3; -.
DR STRING; 3702.AT5G04180.1; -.
DR PaxDb; Q9FYE3; -.
DR PRIDE; Q9FYE3; -.
DR ProteomicsDB; 246723; -.
DR EnsemblPlants; AT5G04180.1; AT5G04180.1; AT5G04180.
DR GeneID; 830296; -.
DR Gramene; AT5G04180.1; AT5G04180.1; AT5G04180.
DR KEGG; ath:AT5G04180; -.
DR Araport; AT5G04180; -.
DR TAIR; locus:2146723; AT5G04180.
DR eggNOG; KOG0382; Eukaryota.
DR HOGENOM; CLU_039326_0_0_1; -.
DR InParanoid; Q9FYE3; -.
DR OMA; CTSENEN; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9FYE3; -.
DR BioCyc; ARA:AT5G04180-MON; -.
DR PRO; PR:Q9FYE3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FYE3; baseline and differential.
DR Genevisible; Q9FYE3; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0010037; P:response to carbon dioxide; IEP:TAIR.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Disulfide bond; Glycoprotein; Lyase; Metal-binding; Plastid;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..277
FT /note="Alpha carbonic anhydrase 3"
FT /id="PRO_0000429729"
FT DOMAIN 24..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 257..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..209
FT /evidence="ECO:0000250"
SQ SEQUENCE 277 AA; 31398 MW; 7EAAA78F99B73438 CRC64;
MKTIILFVTF LALSSSSLAD ETETEFHYKP GEIADPSKWS SIKAEWKICG TGKRQSPINL
TPKIARIVHN STEILQTYYK PVEAILKNRG FDMKVKWEDD AGKIVINDTD YKLVQSHWHA
PSEHFLDGQR LAMELHMVHK SVEGHLAVIG VLFREGEPNA FISRIMDKIH KIADVQDGEV
SIGKIDPREF GWDLTKFYEY RGSLTTPPCT EDVMWTIINK VGTVSREQID VLTDARRGGY
EKNARPAQPL NGRLVYLNEQ SSPSPTPRLR IPRVGPV
