P00920 (CAH2_MOUSE) 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
Synonyms:	Car2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity. Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc.
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	carbon dioxide transport Inferred from mutant phenotype PubMed 16217040. Source: MGI kidney development Inferred from electronic annotation. Source: Compara morphogenesis of an epithelium Inferred from mutant phenotype PubMed 16217040. Source: MGI odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara one-carbon metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of bone resorption Inferred from electronic annotation. Source: Compara positive regulation of cellular pH reduction Inferred from electronic annotation. Source: Compara positive regulation of osteoclast differentiation Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to pH Inferred from electronic annotation. Source: Compara response to stress Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara secretion Inferred from mutant phenotype PubMed 16217040. Source: MGI
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara axon Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 15385584. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara microvillus Inferred from electronic annotation. Source: Compara
Molecular_function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: Compara
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_0000077419
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 Ref.9
Experimental info
	Sequence conflict	39	1	Q → H in AAA37356. Ref.1
	Sequence conflict	39	1	Q → H in AAH55291. Ref.4
	Sequence conflict	145	1	I → Y in AAA37356. Ref.1
	Sequence conflict	145	1	I → Y in AAA37357. Ref.2
	Sequence conflict	213	1	E → D in AAA37357. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P00920 [UniParc]. Last modified May 1, 2007. Version 4. Checksum: 095760368D446AA6	FASTA	260	29,033
	10 20 30 40 50 60 MSHHWGYSKH NGPENWHKDF PIANGDRQSP VDIDTATAQH DPALQPLLIS YDKAASKSIV 70 80 90 100 110 120 NNGHSFNVEF DDSQDNAVLK GGPLSDSYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL 130 140 150 160 170 180 VHWNTKYGDF GKAVQQPDGL AVLGIFLKIG PASQGLQKVL EALHSIKTKG KRAAFANFDP 190 200 210 220 230 240 CSLLPGNLDY WTYPGSLTTP PLLECVTWIV LREPITVSSE QMSHFRTLNF NEEGDAEEAM 250 260 VDNWRPAQPL KNRKIKASFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence and derived amino acid sequence of cDNA coding for mouse carbonic anhydrase II." Curtis P.J., Withers E., Demuth D., Watt R., Venta P.J., Tashian R.E. Gene 25:325-332(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and exon to protein domain relationships of the mouse carbonic anhydrase II gene." Venta P.J., Montgomery J.C., Hewett-Emmett D., Wiebauer K., Tashian R.E. J. Biol. Chem. 260:12130-12135(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
[5]	"Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements." Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E. Biochim. Biophys. Acta 826:195-201(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
[6]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 19-53; 58-80; 90-111; 114-126; 133-167 AND 213-226, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[7]	"Cloning of mouse carbonic anhydrase mRNA and its induction in mouse erythroleukemic cells." Curtis P.J. J. Biol. Chem. 258:4459-4463(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 155-178 AND 214-240.
[8]	"Organization of the mouse and human carbonic anhydrase II genes." Venta P.J., Montgomery J.C., Wiebauer K., Hewett-Emmett D., Tashian R.E. Ann. N. Y. Acad. Sci. 429:309-323(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-260.
[9]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	K00811 mRNA. Translation: AAA37356.1. M81022 , M81016, M81017, M81018, M81019, M81020, M81021 Genomic DNA. Translation: AAA37357.1. AK002333 mRNA. Translation: BAB22019.1. AK002498 mRNA. Translation: BAB22146.2. BC055291 mRNA. Translation: AAH55291.1. M25944 mRNA. Translation: AAA39505.1.
IPI	IPI00121534.
PIR	CRMS2. A23900.
RefSeq	NP_033931.4. NM_009801.4.
UniGene	Mm.1186.
3D structure databases
ProteinModelPortal	P00920.
SMR	P00920. Positions 2-260.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00920. 2 interactions.
PTM databases
PhosphoSite	P00920.
Proteomic databases
PaxDb	P00920.
PRIDE	P00920.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029078; ENSMUSP00000029078; ENSMUSG00000027562.
GeneID	12349.
KEGG	mmu:12349.
UCSC	uc008oqt.2. mouse.
Organism-specific databases
CTD	12349.
MGI	MGI:88269. Car2.
Phylogenomic databases
eggNOG	COG3338.
GeneTree	ENSGT00560000076828.
HOGENOM	HOG000112637.
HOVERGEN	HBG002837.
InParanoid	P00920.
KO	K01672.
OMA	TNFDPRG.
OrthoDB	EOG4X97HR.
Gene expression databases
Bgee	P00920.
CleanEx	MM_CAR2.
Genevestigator	P00920.
GermOnline	ENSMUSG00000027562. Mus musculus.
Family and domain databases
Gene3D	3.10.200.10. 1 hit.
InterPro	IPR001148. Carbonic_anhydrase_a. IPR023561. Carbonic_anhydrase_a-class. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018440. Carbonic_anhydrase_CA2. [Graphical view]
PANTHER	PTHR18952. PTHR18952. 1 hit. PTHR18952:SF28. PTHR18952:SF28. 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
ChEMBL	CHEMBL3689.
ChiTaRS	CA2. mouse.
NextBio	280996.
SOURCE	Search...

Entry information

Entry name

CAH2_MOUSE

Accession

Primary (citable) accession number: P00920
Secondary accession number(s): Q6LDQ7 , Q7TPE1, Q9DCT3, Q9DCY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 120 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program