P27139 (CAH2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 2
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase II
Short name=CA-II

Gene names

Name:

Ca2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Ref.5
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Enzyme regulation	Inhibited by acetazolamide By similarity.
Subunit structure	Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	kidney development Inferred from expression pattern. Source: RGD odontogenesis of dentin-containing tooth Inferred from expression pattern. Source: RGD one-carbon metabolic process Inferred from electronic annotation. Source: InterPro osteoclast differentiation Traceable author statement Ref.5. Source: RGD positive regulation of bone resorption Inferred from mutant phenotype. Source: RGD positive regulation of cellular pH reduction Inferred from mutant phenotype Ref.5. Source: RGD positive regulation of osteoclast differentiation Inferred from mutant phenotype. Source: RGD regulation of cellular pH Traceable author statement Ref.5. Source: RGD response to estrogen stimulus Inferred from expression pattern. Source: RGD response to pH Inferred from expression pattern. Source: RGD response to stress Inferred from expression pattern. Source: RGD response to zinc ion Inferred from expression pattern. Source: RGD
Cellular component	apical part of cell Inferred from direct assay. Source: RGD axon Inferred from direct assay. Source: RGD basolateral plasma membrane Inferred from direct assay. Source: RGD extracellular space Inferred from direct assay. Source: RGD microvillus Inferred from direct assay. Source: RGD
Molecular function	carbonate dehydratase activity Inferred from direct assay. Source: RGD protein binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 260	259	Carbonic anhydrase 2		PRO_0000077421
Regions
	Region	198 – 199	2	Substrate binding By similarity
Sites
	Active site	64	1	Proton acceptor By similarity
	Active site	67	1	By similarity
	Active site	127	1	By similarity
	Metal binding	94	1	Zinc; catalytic
	Metal binding	96	1	Zinc; catalytic
	Metal binding	119	1	Zinc; catalytic
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	87	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27139 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8263A3C0B9B5753D	FASTA	260	29,114
	10 20 30 40 50 60 MSHHWGYSKS NGPENWHKEF PIANGDRQSP VDIDTGTAQH DPSLQPLLIC YDKVASKSIV 70 80 90 100 110 120 NNGHSFNVEF DDSQDFAVLK EGPLSGSYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL 130 140 150 160 170 180 VHWNTKYGDF GKAVQHPDGL AVLGIFLKIG PASQGLQKIT EALHSIKTKG KRAAFANFDP 190 200 210 220 230 240 CSLLPGNLDY WTYPGSLTTP PLLECVTWIV LKEPITVSSE QMSHFRKLNF NSEGEAEELM 250 260 VDNWRPAQPL KNRKIKASFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA encoding rat brain carbonic anhydrase II and its deduced amino acid sequence." Stolle C.A., McGowan M.H., Heim R.A., Varia M., Neubauer J.A. Gene 109:265-267(1991) [PubMed: 1765271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[2]	"Characterization of the rat carbonic anhydrase II gene structure: sequence analysis of the 5' flanking region and 3' UTR." McGowan M.H., Neubauer J.A., Stolle C.A. Gene 186:181-188(1997) [PubMed: 9074494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[4]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 58-80; 81-110; 114-126; 133-158 AND 213-226, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[5]	"Carbonic anhydrase II plays a major role in osteoclast differentiation and bone resorption by effecting the steady state intracellular pH and Ca2+." Lehenkari P., Hentunen T.A., Laitala-Leinonen T., Tuukkanen J., Vaeaenaenen H.K. Exp. Cell Res. 242:128-137(1998) [PubMed: 9665810] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58294 mRNA. Translation: CAA41227.1. U60578 , U60572, U60573, U60574, U60575, U60576, U60577 Genomic DNA. Translation: AAC53104.1. BC065577 mRNA. Translation: AAH65577.1.
IPI	IPI00230787.
PIR	JH0527.
RefSeq	NP_062164.1. NM_019291.1.
UniGene	Rn.26083.
3D structure databases
ProteinModelPortal	P27139.
SMR	P27139. Positions 2-260.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27139. 1 interaction.
STRING	P27139.
PTM databases
PhosphoSite	P27139.
2D gel databases
World-2DPAGE	0004:P27139.
Proteomic databases
PRIDE	P27139.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000013354; ENSRNOP00000013354; ENSRNOG00000009629.
GeneID	54231.
KEGG	rno:54231.
UCSC	NM_019291. rat.
Organism-specific databases
CTD	12349.
RGD	2240. Ca2.
Phylogenomic databases
eggNOG	roNOG15031.
GeneTree	ENSGT00560000076828.
HOVERGEN	HBG002837.
InParanoid	P27139.
OMA	WRPCQPL.
OrthoDB	EOG4X97HR.
PhylomeDB	P27139.
Gene expression databases
ArrayExpress	P27139.
Genevestigator	P27139.
GermOnline	ENSRNOG00000009629. Rattus norvegicus.
Family and domain databases
InterPro	IPR001148. a_carbonic_anhydrase. IPR023561. Carbonic_anhydrase_a-class. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018440. Carbonic_anhydrase_CA2. [Graphical view]
Gene3D	G3DSA:3.10.200.10. Euk_COanhd. 1 hit.
KO	K01672.
PANTHER	PTHR18952:SF28. Carbonic_anhydrase_CA2. 1 hit. PTHR18952. Euk_COanhd. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
SMART	SM01057. Carb_anhydrase. 1 hit. [Graphical view]
SUPFAM	SSF51069. Euk_COanhd. 1 hit.
PROSITE	PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	610662.

Entry information

Entry name

CAH2_RAT

Accession

Primary (citable) accession number: P27139

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program