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Protein

Carbonic anhydrase 5B, mitochondrial

Gene

CA5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Zinc; catalyticBy similarity
Metal bindingi132 – 1321Zinc; catalyticBy similarity
Metal bindingi155 – 1551Zinc; catalyticBy similarity

GO - Molecular functioni

  • carbonate dehydratase activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CA5B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:1378. CA5B.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25993.

Chemistry

DrugBankiDB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiCA5B.
DMDMi8928041.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionAdd
BLAST
Chaini34 – 317284Carbonic anhydrase 5B, mitochondrialPRO_0000004237Add
BLAST

Proteomic databases

PaxDbiQ9Y2D0.
PRIDEiQ9Y2D0.

PTM databases

PhosphoSiteiQ9Y2D0.

Expressioni

Tissue specificityi

Strongest expression in heart, pancreas, kidney, placenta, lung, and skeletal muscle. Not expressed in liver.

Gene expression databases

BgeeiQ9Y2D0.
CleanExiHS_CA5B.
ExpressionAtlasiQ9Y2D0. baseline and differential.
GenevisibleiQ9Y2D0. HS.

Organism-specific databases

HPAiHPA012618.

Interactioni

Protein-protein interaction databases

BioGridi116403. 3 interactions.
STRINGi9606.ENSP00000314099.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2D0.
SMRiQ9Y2D0. Positions 61-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 2362Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9Y2D0.
KOiK01672.
OMAiVMKQHIE.
PhylomeDBiQ9Y2D0.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018437. CA-VB_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y2D0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVMNSLRVI LQASPGKLLW RKFQIPRFMP ARPCSLYTCT YKTRNRALHP
60 70 80 90 100
LWESVDLVPG GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHVWNNGY
110 120 130 140 150
SFLVEFEDST DKSVIKGGPL EHNYRLKQFH FHWGAIDAWG SEHTVDSKCF
160 170 180 190 200
PAELHLVHWN AVRFENFEDA ALEENGLAVI GVFLKLGKHH KELQKLVDTL
210 220 230 240 250
PSIKHKDALV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS ESVTWIIKKQ
260 270 280 290 300
PVEVDHDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY
310
VLNVQAKPKP ATSQATP
Length:317
Mass (Da):36,434
Last modified:November 1, 1999 - v1
Checksum:i7CA11920EFF2588A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021660 mRNA. Translation: BAA76671.1.
AK291050 mRNA. Translation: BAF83739.1.
CH471074 Genomic DNA. Translation: EAW98897.1.
BC028142 mRNA. Translation: AAH28142.1.
CCDSiCCDS14171.1.
RefSeqiNP_009151.1. NM_007220.3.
XP_005274499.1. XM_005274442.3.
UniGeneiHs.653287.

Genome annotation databases

EnsembliENST00000318636; ENSP00000314099; ENSG00000169239.
ENST00000454127; ENSP00000417021; ENSG00000169239.
GeneIDi11238.
KEGGihsa:11238.
UCSCiuc004cxe.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021660 mRNA. Translation: BAA76671.1.
AK291050 mRNA. Translation: BAF83739.1.
CH471074 Genomic DNA. Translation: EAW98897.1.
BC028142 mRNA. Translation: AAH28142.1.
CCDSiCCDS14171.1.
RefSeqiNP_009151.1. NM_007220.3.
XP_005274499.1. XM_005274442.3.
UniGeneiHs.653287.

3D structure databases

ProteinModelPortaliQ9Y2D0.
SMRiQ9Y2D0. Positions 61-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116403. 3 interactions.
STRINGi9606.ENSP00000314099.

Chemistry

BindingDBiQ9Y2D0.
ChEMBLiCHEMBL2095180.
DrugBankiDB00909. Zonisamide.

PTM databases

PhosphoSiteiQ9Y2D0.

Polymorphism and mutation databases

BioMutaiCA5B.
DMDMi8928041.

Proteomic databases

PaxDbiQ9Y2D0.
PRIDEiQ9Y2D0.

Protocols and materials databases

DNASUi11238.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318636; ENSP00000314099; ENSG00000169239.
ENST00000454127; ENSP00000417021; ENSG00000169239.
GeneIDi11238.
KEGGihsa:11238.
UCSCiuc004cxe.3. human.

Organism-specific databases

CTDi11238.
GeneCardsiGC0XP015706.
HGNCiHGNC:1378. CA5B.
HPAiHPA012618.
MIMi300230. gene.
neXtProtiNX_Q9Y2D0.
PharmGKBiPA25993.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9Y2D0.
KOiK01672.
OMAiVMKQHIE.
PhylomeDBiQ9Y2D0.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

Miscellaneous databases

ChiTaRSiCA5B. human.
GeneWikiiCA5B.
GenomeRNAii11238.
NextBioi42774.
PROiQ9Y2D0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2D0.
CleanExiHS_CA5B.
ExpressionAtlasiQ9Y2D0. baseline and differential.
GenevisibleiQ9Y2D0. HS.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018437. CA-VB_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCAH5B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2D0
Secondary accession number(s): A8K4T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.