ATCA1_ARATH
ID ATCA1_ARATH Reviewed; 284 AA.
AC O04846; B9DH12; F4J831; Q940K9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Alpha carbonic anhydrase 1, chloroplastic;
DE Short=AtaCA1;
DE Short=AtalphaCA1;
DE EC=4.2.1.1;
DE AltName: Full=Alpha carbonate dehydratase 1;
DE Flags: Precursor;
GN Name=ACA1; Synonyms=CAH1; OrderedLocusNames=At3g52720; ORFNames=F3C22.120;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=16284624; DOI=10.1038/ncb1330;
RA Villarejo A., Buren S., Larsson S., Dejardin A., Monne M., Rudhe C.,
RA Karlsson J., Jansson S., Lerouge P., Rolland N., von Heijne G., Grebe M.,
RA Bako L., Samuelsson G.;
RT "Evidence for a protein transported through the secretory pathway en route
RT to the higher plant chloroplast.";
RL Nat. Cell Biol. 7:1224-1231(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP TISSUE SPECIFICITY, 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 CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-85; ASN-112; ASN-182; ASN-219 AND
RP ASN-249, MUTAGENESIS OF 52-CYS-ALA-53; ASN-85; ASN-112; ASN-182; CYS-216;
RP ASN-219 AND ASN-249, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RX PubMed=21695217; DOI=10.1371/journal.pone.0021021;
RA Buren S., Ortega-Villasante C., Blanco-Rivero A., Martinez-Bernardini A.,
RA Shutova T., Shevela D., Messinger J., Bako L., Villarejo A., Samuelsson G.;
RT "Importance of post-translational modifications for functionality of a
RT chloroplast-localized carbonic anhydrase (CAH1) in Arabidopsis thaliana.";
RL PLoS ONE 6:E21021-E21021(2011).
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 Evidence={ECO:0000269|PubMed:21695217};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}.
CC Note=When glycosylated and folded, targeted to the chloroplast via a
CC protein-targeting pathway that uses the secretory system via the
CC endoplasmic reticulum (ER) and Golgi apparatus.
CC {ECO:0000269|PubMed:16284624, ECO:0000269|PubMed:21695217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O04846-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04846-2; Sequence=VSP_055070;
CC Name=3;
CC IsoId=O04846-3; Sequence=VSP_055069;
CC -!- TISSUE SPECIFICITY: Strongly expressed in aerial tissues including
CC leaves, stems, flowers and siliques. {ECO:0000269|PubMed:17407539}.
CC -!- PTM: N-glycosylation is required for activity and chloroplast
CC targeting, probably by facilitating folding and endoplasmic reticulum
CC (ER) export. {ECO:0000269|PubMed:16284624,
CC ECO:0000269|PubMed:21695217}.
CC -!- PTM: Disulfide bridge between Cys-52 and Cys-216 is required for
CC correct folding.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH20029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73462; AAC32523.1; -; mRNA.
DR EMBL; AL353912; CAB89233.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78985.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78986.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64134.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64135.1; -; Genomic_DNA.
DR EMBL; AY054466; AAK96658.1; -; mRNA.
DR EMBL; AY081665; AAM10227.1; -; mRNA.
DR EMBL; AK317357; BAH20029.1; ALT_INIT; mRNA.
DR PIR; T49025; T49025.
DR RefSeq; NP_001319732.1; NM_001339583.1. [O04846-1]
DR RefSeq; NP_001326182.1; NM_001339584.1. [O04846-1]
DR RefSeq; NP_566971.2; NM_115132.3. [O04846-1]
DR RefSeq; NP_850685.1; NM_180354.2. [O04846-2]
DR AlphaFoldDB; O04846; -.
DR SMR; O04846; -.
DR STRING; 3702.AT3G52720.1; -.
DR iPTMnet; O04846; -.
DR PaxDb; O04846; -.
DR PRIDE; O04846; -.
DR ProteomicsDB; 246607; -. [O04846-1]
DR EnsemblPlants; AT3G52720.1; AT3G52720.1; AT3G52720. [O04846-1]
DR EnsemblPlants; AT3G52720.2; AT3G52720.2; AT3G52720. [O04846-2]
DR EnsemblPlants; AT3G52720.3; AT3G52720.3; AT3G52720. [O04846-1]
DR EnsemblPlants; AT3G52720.4; AT3G52720.4; AT3G52720. [O04846-1]
DR GeneID; 824438; -.
DR Gramene; AT3G52720.1; AT3G52720.1; AT3G52720. [O04846-1]
DR Gramene; AT3G52720.2; AT3G52720.2; AT3G52720. [O04846-2]
DR Gramene; AT3G52720.3; AT3G52720.3; AT3G52720. [O04846-1]
DR Gramene; AT3G52720.4; AT3G52720.4; AT3G52720. [O04846-1]
DR KEGG; ath:AT3G52720; -.
DR Araport; AT3G52720; -.
DR TAIR; locus:2083213; AT3G52720.
DR eggNOG; KOG0382; Eukaryota.
DR HOGENOM; CLU_039326_0_0_1; -.
DR InParanoid; O04846; -.
DR OMA; RMRMENN; -.
DR PhylomeDB; O04846; -.
DR BioCyc; ARA:AT3G52720-MON; -.
DR PRO; PR:O04846; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O04846; baseline and differential.
DR Genevisible; O04846; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:TAIR.
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 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 InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Lyase; Metal-binding; Plastid; Reference proteome; Signal;
KW Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..284
FT /note="Alpha carbonic anhydrase 1, chloroplastic"
FT /id="PRO_0000429727"
FT DOMAIN 29..266
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 244..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21695217"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21695217"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21695217"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:21695217"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21695217"
FT DISULFID 52..216
FT /evidence="ECO:0000269|PubMed:21695217"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_055069"
FT VAR_SEQ 229..284
FT /note="RSMSKEQVELLRSPLDTSFKNNSRPCQPLNGRRVEMFHDHERVDKKETGNKK
FT KKPN -> IF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055070"
FT MUTAGEN 52..53
FT /note="CA->LE: Folding loss; when associated with S-216."
FT /evidence="ECO:0000269|PubMed:21695217"
FT MUTAGEN 85
FT /note="N->A: Loss of N-glycosylation and impaired
FT trafficking from endoplasmic reticulum (ER) to chloroplast;
FT when associated with A-112; A-182; A-219 and A-249."
FT /evidence="ECO:0000269|PubMed:21695217"
FT MUTAGEN 112
FT /note="N->A: Loss of N-glycosylation and impaired
FT trafficking from endoplasmic reticulum (ER) to chloroplast;
FT when associated with A-85; A-182; A-219 and A-249."
FT /evidence="ECO:0000269|PubMed:21695217"
FT MUTAGEN 182
FT /note="N->A: Loss of N-glycosylation and impaired
FT trafficking from endoplasmic reticulum (ER) to chloroplast;
FT when associated with A-85; A-112; A-219 and A-249."
FT /evidence="ECO:0000269|PubMed:21695217"
FT MUTAGEN 216
FT /note="C->S: Folding loss; when associated with 52-L-E-53."
FT /evidence="ECO:0000269|PubMed:21695217"
FT MUTAGEN 219
FT /note="N->A: Loss of N-glycosylation and impaired
FT trafficking from endoplasmic reticulum (ER) to chloroplast;
FT when associated with A-85; A-112; A-182 and A-249."
FT /evidence="ECO:0000269|PubMed:21695217"
FT MUTAGEN 249
FT /note="N->A: Loss of N-glycosylation and impaired
FT trafficking from endoplasmic reticulum (ER) to chloroplast;
FT when associated with A-85; A-112; A-182 and A-219."
FT /evidence="ECO:0000269|PubMed:21695217"
FT CONFLICT 1
FT /note="M -> R (in Ref. 5; BAH20029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32698 MW; E0CA26DCCA7D2829 CRC64;
MKIMMMIKLC FFSMSLICIA PADAQTEGVV FGYKGKNGPN QWGHLNPHFT TCAVGKLQSP
IDIQRRQIFY NHKLNSIHRE YYFTNATLVN HVCNVAMFFG EGAGDVIIEN KNYTLLQMHW
HTPSEHHLHG VQYAAELHMV HQAKDGSFAV VASLFKIGTE EPFLSQMKEK LVKLKEERLK
GNHTAQVEVG RIDTRHIERK TRKYYRYIGS LTTPPCSENV SWTILGKVRS MSKEQVELLR
SPLDTSFKNN SRPCQPLNGR RVEMFHDHER VDKKETGNKK KKPN
