CAH_LOBCS
ID CAH_LOBCS Reviewed; 175 AA.
AC P84537;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
DE AltName: Full=Matrix protein MPL-2;
DE Flags: Fragment;
OS Lobophytum crassum (Soft coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Alcyonacea;
OC Alcyoniina; Alcyoniidae; Lobophytum.
OX NCBI_TaxID=328265;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Sclerite {ECO:0000269|PubMed:16670968};
RX PubMed=16670968; DOI=10.1007/s10126-005-6150-6;
RA Rahman M.D.A., Isa Y., Uehara T.;
RT "Studies on two closely related species of octocorallians: biochemical and
RT molecular characteristics of the organic matrices of endoskeletal
RT sclerites.";
RL Mar. Biotechnol. 8:415-424(2006).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. Also acts as a
CC structural protein, having a role in calcium carbonate crystal
CC formation in the bio-calcification process.
CC {ECO:0000269|PubMed:16670968}.
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:16670968};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00918};
CC -!- ACTIVITY REGULATION: Inhibited by diamox.
CC {ECO:0000269|PubMed:16670968}.
CC -!- TISSUE SPECIFICITY: Sclerites. {ECO:0000269|PubMed:16670968}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16670968}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P84537; -.
DR SMR; P84537; -.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Lyase; Metal-binding; Zinc.
FT CHAIN 1..>175
FT /note="Carbonic anhydrase"
FT /id="PRO_0000077443"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 137..138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT NON_TER 175
FT /evidence="ECO:0000303|PubMed:16670968"
SQ SEQUENCE 175 AA; 20383 MW; 58FE76F9BBB557B3 CRC64;
DELNKKVDSD ETISDDGVVA HGASMDEKHD YMDNGVRHVH NGRTRRKGSE HEVDGRFTPM
EARLVFHLTT PPCTESVLWV VQKDDDEHHT RREEGPHWHD THSFKHAEDL DVHLTPEDDL
EDDKRHDDTY TYEGSLTTEE VQVEGYKDEP EELEMVDNWR PAQKNKVTVY KASEH
