Q9Y2D0 (CAH5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 5B, mitochondrial
EC=4.2.1.1

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

Gene names

Name:

CA5B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 protein level

General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Enzyme regulation	Inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt). Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Mitochondrion.
Tissue specificity	Strongest expression in heart, pancreas, kidney, placenta, lung, and skeletal muscle. Not expressed in liver.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate transport Traceable author statement. Source: Reactome one-carbon metabolic process Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	carbonate dehydratase activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion
	Chain	34 – 317	284	Carbonic anhydrase 5B, mitochondrial		PRO_0000004237
Regions
	Region	235 – 236	2	Substrate binding By similarity
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

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2D0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7CA11920EFF2588A	FASTA	317	36,434
	10 20 30 40 50 60 MVVMNSLRVI LQASPGKLLW RKFQIPRFMP ARPCSLYTCT YKTRNRALHP LWESVDLVPG 70 80 90 100 110 120 GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHVWNNGY SFLVEFEDST DKSVIKGGPL 130 140 150 160 170 180 EHNYRLKQFH FHWGAIDAWG SEHTVDSKCF PAELHLVHWN AVRFENFEDA ALEENGLAVI 190 200 210 220 230 240 GVFLKLGKHH KELQKLVDTL PSIKHKDALV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS 250 260 270 280 290 300 ESVTWIIKKQ PVEVDHDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY 310 VLNVQAKPKP ATSQATP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human mitochondrial carbonic anhydrase VB: cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome X." Fujikawa-Adachi K., Nishimori I., Taguchi T., Onishi S. J. Biol. Chem. 274:21228-21233(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Pancreas.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]. Tissue: Blood.
[5]	"Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste." Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G. Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[6]	"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I." Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T. Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[7]	"A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases." Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T. Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors." Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T. J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB021660 mRNA. Translation: BAA76671.1. AK291050 mRNA. Translation: BAF83739.1. CH471074 Genomic DNA. Translation: EAW98897.1. BC028142 mRNA. Translation: AAH28142.1.
IPI	IPI00032055.
RefSeq	NP_009151.1. NM_007220.3.
UniGene	Hs.728980.
3D structure databases
ProteinModelPortal	Q9Y2D0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000314099.
PTM databases
PhosphoSite	Q9Y2D0.
Polymorphism databases
DMDM	8928041.
Proteomic databases
PaxDb	Q9Y2D0.
PRIDE	Q9Y2D0.
Protocols and materials databases
DNASU	11238.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000318636; ENSP00000314099; ENSG00000169239. ENST00000454127; ENSP00000417021; ENSG00000169239.
GeneID	11238.
KEGG	hsa:11238.
UCSC	uc004cxe.3. human.
Organism-specific databases
CTD	11238.
GeneCards	GC0XP015706.
HGNC	HGNC:1378. CA5B.
HPA	HPA012618.
MIM	300230. gene.
neXtProt	NX_Q9Y2D0.
PharmGKB	PA25993.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3338.
HOGENOM	HOG000112637.
HOVERGEN	HBG002837.
InParanoid	Q9Y2D0.
KO	K01672.
OMA	IKHKDTL.
OrthoDB	EOG4FR0RX.
PhylomeDB	Q9Y2D0.
Enzyme and pathway databases
BRENDA	4.2.1.1. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9Y2D0.
Bgee	Q9Y2D0.
CleanEx	HS_CA5B.
Genevestigator	Q9Y2D0.
GermOnline	ENSG00000169239. Homo sapiens.
Family and domain databases
Gene3D	3.10.200.10. 1 hit.
InterPro	IPR018437. CA-V_mt. IPR001148. Carbonic_anhydrase_a. IPR023561. Carbonic_anhydrase_a-class. IPR018338. Carbonic_anhydrase_a-class_CS. [Graphical view]
PANTHER	PTHR18952. PTHR18952. 1 hit. PTHR18952:SF25. PTHR18952:SF25. 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
BindingDB	Q9Y2D0.
ChEMBL	CHEMBL3969.
GenomeRNAi	11238.
NextBio	42774.
SOURCE	Search...

Entry information

Entry name

CAH5B_HUMAN

Accession

Primary (citable) accession number: Q9Y2D0
Secondary accession number(s): A8K4T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.