Reviewed, UniProtKB/Swiss-Prot P84537 (CAH_LOBCS)

Names and origin

Protein names	Recommended name:     Carbonic anhydrase     EC=4.2.1.1 Alternative name(s):     Carbonate dehydratase     Matrix protein MPL-2
Organism	Lobophytum crassum (Soft coral)
Taxonomic identifier	328265 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Cnidaria › Anthozoa › Octocorallia › Alcyonacea › Alcyoniidae › Lobophytum

Protein attributes

Sequence length	175 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reversible hydration of carbon dioxide. Also acts as a structural protein, having a role in calcium carbonate crystal formation in the bio-calcification process. Ref.1
Catalytic activity	H2CO3 = CO2 + H2O. Ref.1
Cofactor	Zinc By similarity. UniProtKB P00918
Enzyme regulation	Inhibited by diamox. Ref.1
Tissue specificity	Sclerites. Ref.1
Post-translational modification	Glycosylated. Ref.1
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›175	›175	Carbonic anhydrase		PRO_0000077443
Sites
	Metal binding	38	1	Zinc; catalytic By similarity UniProtKB P00918
	Metal binding	40	1	Zinc; catalytic By similarity UniProtKB P00918
Experimental info
	Non-terminal residue	175	1

Sequences

	Sequence		Length	Mass (Da)
	P84537-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: 58FE76F9BBB557B3	FASTA	175	20,383
	10 20 30 40 50 60 DELNKKVDSD ETISDDGVVA HGASMDEKHD YMDNGVRHVH NGRTRRKGSE HEVDGRFTPM 70 80 90 100 110 120 EARLVFHLTT PPCTESVLWV VQKDDDEHHT RREEGPHWHD THSFKHAEDL DVHLTPEDDL 130 140 150 160 170 EDDKRHDDTY TYEGSLTTEE VQVEGYKDEP EELEMVDNWR PAQKNKVTVY KASEH

References

[1]

"Studies on two closely related species of octocorallians: biochemical and molecular characteristics of the organic matrices of endoskeletal sclerites." Rahman M.D.A., Isa Y., Uehara T. Mar. Biotechnol. 8:415-424(2006) [PubMed: 16670968] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, GLYCOSYLATION. Tissue: Sclerite.

Cross-references

3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.1. 300307.
Family and domain databases
InterPro	IPR001148. Carbonic_anhydrase_a-class_cat. IPR018338. Carbonic_anhydrase_a-class_CS. [Graphical view]
Gene3D	G3DSA:3.10.200.10. Euk_COanhd. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
ProDom	PD000865. Euk_COanhd. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00162. ALPHA_CA_1. Partial match. PS51144. ALPHA_CA_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAH_LOBCS

Accession

Primary (citable) accession number: P84537

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 7, 2006
Last modified:	May 5, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)