CAH_ACRMI
ID CAH_ACRMI Reviewed; 148 AA.
AC B8V7P3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Putative carbonic anhydrase {ECO:0000303|PubMed:23765379};
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P83299};
DE AltName: Full=Carbonate dehydratase {ECO:0000250|UniProtKB:P83299};
DE Flags: Fragment;
OS Acropora millepora (Staghorn coral) (Heteropora millepora).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Acroporidae; Acropora.
OX NCBI_TaxID=45264;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT "Whole transcriptome analysis of the coral Acropora millepora reveals
RT complex responses to CO(2)-driven acidification during the initiation of
RT calcification.";
RL Mol. Ecol. 21:2440-2454(2012).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 38-59; 71-112 AND 122-141, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23765379; DOI=10.1093/molbev/mst109;
RA Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA Guichard N., Miller D.J., Marin F.;
RT "The skeletal proteome of the coral Acropora millepora: the evolution of
RT calcification by co-option and domain shuffling.";
RL Mol. Biol. Evol. 30:2099-2112(2013).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:P83299}.
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:0000250|UniProtKB:P83299};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00915};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23765379}.
CC -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix of
CC the aragonitic skeleton (at protein level).
CC {ECO:0000269|PubMed:23765379}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000255}.
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DR EMBL; JR998014; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B8V7P3; -.
DR SMR; B8V7P3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.10.200.10; -; 1.
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 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Metal-binding; Secreted; Zinc.
FT CHAIN <1..148
FT /note="Putative carbonic anhydrase"
FT /id="PRO_0000429492"
FT DOMAIN 1..146
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 17040 MW; 5ECC6BE711B334E7 CRC64;
CLKRLQPGEM SLQLLLSGCR LRLEQETGVL GRFADLTRKI IQPDSDETVR FSDGIFIRGL
IPQRCNTRFS RLAILNCYYT YKGSLTTPIC SENVTWLIVK PRLPATNNMM RKFRRLETPA
GKNPPLMCDN FRPVQPLNGR TVFEVHRI
