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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.
31-JUL-2019, entry version 154.
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; Magnoliopsida; 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;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[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:
Reaction=H(+) + hydrogencarbonate = CO2 + H2O;
Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1;
Evidence={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]
SMR; P27140; -.
BioGrid; 6467; 15.
IntAct; P27140; 11.
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. [P27140-3]
Gramene; AT3G01500.2; AT3G01500.2; AT3G01500. [P27140-1]
Gramene; AT3G01500.3; AT3G01500.3; AT3G01500. [P27140-2]
KEGG; ath:AT3G01500; -.
Araport; AT3G01500; -.
TAIR; locus:2084198; AT3G01500.
eggNOG; KOG1578; Eukaryota.
eggNOG; COG0288; LUCA.
HOGENOM; HOG000125183; -.
InParanoid; P27140; -.
KO; K01673; -.
OrthoDB; 1136193at2759; -.
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:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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.
InterPro; IPR036874; Carbonic_anhydrase_sf.
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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WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP1675: Nitrogen metabolism
WP1982: SREBP signalling
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1207: Fatty Acid Beta Oxidation
WP419: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP731: Sterol regulatory element binding protein related
WP1654: gamma-Hexachlorocyclohexane degradation
WP448: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1237: Fatty Acid Beta Oxidation
WP1269: Fatty Acid Beta Oxidation
WP580: Dauer formation
WP1531: Vitamin D synthesis
WP1307: Fatty Acid Beta Oxidation
WP943: Fatty Acid Beta Oxidation
WP989: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP39: Fatty Acid Beta Oxidation 1
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP105: Fatty Acid Beta Oxidation 2
WP2292: Chemokine signaling pathway
WP143: Fatty Acid Beta Oxidation
WP187: Fatty Acid Beta Oxidation 2

Related Genes :
[BCA1 CA1 SABP3 At3g01500 F4P13.5] Beta carbonic anhydrase 1, chloroplastic (AtbCA1) (AtbetaCA1) (EC 4.2.1.1) (Beta carbonate dehydratase 1) (Protein SALICYLIC ACID-BINDING PROTEIN 3) (AtSABP3)
[CA2] Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase II) (Carbonic anhydrase C) (CAC) (Carbonic anhydrase II) (CA-II)
[Ca5a Ca5 Car5 Car5a] Carbonic anhydrase 5A, mitochondrial (EC 4.2.1.1) (Carbonate dehydratase VA) (CA Y) (Carbonic anhydrase VA) (CA-VA)
[Ca4] Carbonic anhydrase 4 (EC 4.2.1.1) (Carbonate dehydratase IV) (Carbonic anhydrase IV) (CA-IV)
[CA1] Carbonic anhydrase 1 (EC 4.2.1.1) (Carbonate dehydratase I) (Carbonic anhydrase I) (CA-I)
[Ca3 Car3] Carbonic anhydrase 3 (EC 4.2.1.1) (Carbonate dehydratase III) (Carbonic anhydrase III) (CA-III)
[atnM ANIA_07873] Fatty acid synthase beta subunit aflB (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein M) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BvCmsC61A_00149 BvCmsH15A_00510 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E5M00_18610 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EPS71_23885 FORC82_1921 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[DTX47 EDS5 IAP1 SCORD3 SID1 At4g39030 F19H22.130] Protein DETOXIFICATION 47, chloroplastic (AtDTX47) (Multidrug and toxic compound extrusion protein 47) (MATE protein 47) (Protein ENHANCED DISEASE SUSCEPTIBILITY 5) (Protein EDS5) (Protein IMPORTANT FOR THE ARR PATHWAY 1) (Protein IAP1) (Protein SALICYLIC ACID INDUCTION DEFICIENT 1) (Protein SID1) (Protein SUSCEPTIBLE TO CORONATINE-DEFICIENT PST DC3000 3) (Protein SCORD3)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); Serine protease nsp4 (3CLSP) (EC 3.4.21.-) (3C-like serine proteinase) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase nsp10 (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BvCmsSIP082_02402 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFB45_10990 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX32_14605 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[KAS2 FAB1 At1g74960 F25A4.7 F9E10.19] 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic (EC 2.3.1.41) (Beta-ketoacyl-acyl-carrier-protein synthase II) (AtKAS2) (Beta-ketoacyl-ACP synthetase 2) (Protein FATTY ACID BIOSYNTHESIS 1)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[mcl1 RHOS4_03500 RSP_1771] L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) ((S)-citramalyl-CoA lyase) (EC 4.1.3.25)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[GLU1] 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic (EC 3.2.1.182) (Beta-D-glucoside glucohydrolase) (Beta-glucosidase 1) (ZmGlu1) (EC 3.2.1.21)
[FAS2 YPL231W P1409] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[hexB DOTSEDRAFT_181128] Fatty acid synthase beta subunit hexB (EC 2.3.1.86) (S-acyl fatty acid synthase thioesterase) (EC 3.1.2.14) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39) (Dothistromin biosynthesis protein hexB)]
[GLU1B] 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1b, chloroplastic (EC 3.2.1.182) (Beta-glucosidase 1b) (Taglu1b) (EC 3.2.1.21)
[DLO1 SAG108 At4g10500 F3H7.16 F7L13.80] Protein DMR6-LIKE OXYGENASE 1 (EC 1.14.11.-) (2-oxoglutarate (2OG)-Fe(II) oxygenase-like protein DLO1) (Protein SENESCENCE-ASSOCIATED GENE 108) (Salicylate 3-hydroxylase DLO1) (S3H DLO1) (SA 3-hydroxylase DLO1) (Salicylic acid 3-hydroxylase DLO1) (EC 1.14.13.-)
[] 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase, chloroplastic (EC 3.2.1.182) (Beta-glucosidase) (ScGlu) (EC 3.2.1.21)
[TD2 TD] Threonine dehydratase 2 biosynthetic, chloroplastic (EC 4.3.1.17) (EC 4.3.1.19) (SlTD2) (Threonine deaminase 2) [Cleaved into: Processed threonine dehydratase 2 (Processed TD2) (pTD2)]
[hchA A8M42_01610 AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC007_02422 ExPECSC065_02714 HmCmsJML122_02218 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.19.12) (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[DMR6 At5g24530 K18P6.6] Protein DOWNY MILDEW RESISTANCE 6 (AtDMR6) (EC 1.14.11.-) (2-oxoglutarate (2OG)-Fe(II) oxygenase-like protein DMR6) (Salicylate 3-hydroxylase DMR6) (S3H DMR6) (SA 3-hydroxylase DMR6) (Salicylic acid 3-hydroxylase DMR6) (EC 1.14.13.-)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[BAM1 BMY7 TRBAMY At3g23920 F14O13.12] Beta-amylase 1, chloroplastic (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Beta-amylase 7) (Thioredoxin-regulated beta-amylase) (TR-BAMY)

Bibliography :