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Q9Y2D0 (CAH5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion
Chain34 – 317284Carbonic anhydrase 5B, mitochondrial
PRO_0000004237

Regions

Region235 – 2362Substrate binding By similarity

Sites

Metal binding1301Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity
Metal binding1551Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y2D0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 7CA11920EFF2588A

FASTA31736,434
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_009151.1. NM_007220.3.
XP_005274499.1. XM_005274442.2.
UniGeneHs.653287.

3D structure databases

ProteinModelPortalQ9Y2D0.
SMRQ9Y2D0. Positions 61-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116403. 1 interaction.
STRING9606.ENSP00000314099.

Chemistry

BindingDBQ9Y2D0.
ChEMBLCHEMBL2095180.

PTM databases

PhosphoSiteQ9Y2D0.

Polymorphism databases

DMDM8928041.

Proteomic databases

PaxDbQ9Y2D0.
PRIDEQ9Y2D0.

Protocols and materials databases

DNASU11238.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318636; ENSP00000314099; ENSG00000169239.
ENST00000454127; ENSP00000417021; ENSG00000169239.
GeneID11238.
KEGGhsa:11238.
UCSCuc004cxe.3. human.

Organism-specific databases

CTD11238.
GeneCardsGC0XP015706.
HGNCHGNC:1378. CA5B.
HPAHPA012618.
MIM300230. gene.
neXtProtNX_Q9Y2D0.
PharmGKBPA25993.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidQ9Y2D0.
KOK01672.
OMAIKHKDTL.
PhylomeDBQ9Y2D0.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9Y2D0.
BgeeQ9Y2D0.
CleanExHS_CA5B.
GenevestigatorQ9Y2D0.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018437. CA-VB_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF68. PTHR18952:SF68. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCA5B.
GenomeRNAi11238.
NextBio42774.
PROQ9Y2D0.
SOURCESearch...

Entry information

Entry nameCAH5B_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM