Reviewed, UniProtKB/Swiss-Prot Q9QZA0 (CAH5B_MOUSE)

Names and origin

Protein names

Recommended name:
    Carbonic anhydrase 5B, mitochondrial
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase VB
      Short name=CA-VB
    Carbonate dehydratase VB

Gene names

Name:	Ca5b
Synonyms:	Car5b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Lyase
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Ref.1 Inferred from direct assay. Source: MGI
Molecular function	carbonate dehydratase activity Ref.1 Inferred from direct assay. Source: MGI 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
	Transit peptide	1 – 33	33	Mitochondrion By similarity
	Chain	34 – 317	284	Carbonic anhydrase 5B, mitochondrial		PRO_0000004238
Sites
	Metal binding	130	1	Zinc; catalytic By similarity
	Metal binding	132	1	Zinc; catalytic By similarity
	Metal binding	155	1	Zinc; catalytic By similarity
Experimental info
	Sequence conflict	269	1	S → F in BAC39501. Ref.2
	Sequence conflict	308	1	P → A in AAF08291. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9QZA0-1 [UniParc]. Last modified May 9, 2003. Version 2. Checksum: 719016A75305BFD3	FASTA	317	36,623
	10 20 30 40 50 60 MAVMNHLRVI LQVSSSTLPW RRCWVPRLVP RRSCSLYTCT YRTRNRALPP LWENLDLVPA 70 80 90 100 110 120 GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY SFLVEFEDST DKSVVEGGPL 130 140 150 160 170 180 EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY PAELHLVHWN AVKFESFEDA ALEENGLAVI 190 200 210 220 230 240 GVFLKLGKHH KELQKLVDTL PSIKHKDTLV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS 250 260 270 280 290 300 ESVTWIIKKQ PVEVDRDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY 310 VLNIQVKPKP TASEVTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mitochondrial carbonic anhydrase CA VB: differences in tissue distribution and pattern of evolution from those of CA VA suggest distinct physiological roles." Shah G.N., Hewett-Emmett D., Grubb J.H., Migas M.C., Fleming R.E., Waheed A., Sly W.S. Proc. Natl. Acad. Sci. U.S.A. 97:1677-1682(2000) [PubMed: 10677517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary gland.
[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: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF192978 mRNA. Translation: AAF08291.1. AK085670 mRNA. Translation: BAC39501.1. BC034413 mRNA. Translation: AAH34413.1.
IPI	IPI00317025.
RefSeq	NP_851832.2.
UniGene	Mm.180953
3D structure databases
SMR	Q9QZA0. Positions 61-297.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QZA0.
Proteomic databases
PRIDE	Q9QZA0.
Genome annotation databases
Ensembl	ENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373; Mus musculus. [Genome view]
GeneID	56078.
KEGG	mmu:56078.
UCSC	uc009uvc.1. mouse.
Organism-specific databases
CTD	56078.
MGI	MGI:1926249. Car5b.
Phylogenomic databases
HOGENOM	HBG717384.
HOVERGEN	Q9QZA0.
InParanoid	Q9QZA0.
OMA	SVIEGGP.
OrthoDB	EOG9GJ27G.
PhylomeDB	Q9QZA0.
Enzyme and pathway databases
BRENDA	4.2.1.1. 244.
Gene expression databases
ArrayExpress	Q9QZA0.
Bgee	Q9QZA0.
CleanEx	MM_CAR5B.
Genevestigator	Q9QZA0.
GermOnline	ENSMUSG00000031373. Mus musculus.
Family and domain databases
InterPro	IPR001148. Carbonic_anhydrase_a-class_cat. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018437. Carbonic_anhydrase_CA5_mt. [Graphical view]
Gene3D	G3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHER	PTHR18952:SF25. Carbonic_anhydrase_CA5_mt. 1 hit. PTHR18952. Euk_COanhd. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
PROSITE	PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	311872.
SOURCE	Search...

Entry information

Entry name

CAH5B_MOUSE

Accession

Primary (citable) accession number: Q9QZA0
Secondary accession number(s): Q8C3J9, Q8K014

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 9, 2003
Last modified:	January 19, 2010
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)