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P35218 (CAH5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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 5A, mitochondrial

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase VA
Carbonic anhydrase VA
Short name=CA-VA
Gene names
Name:CA5A
Synonyms:CA5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length305 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. Low activity.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Enzyme regulation

Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt). Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Biophysicochemical properties

Kinetic parameters:

KM=10.0 mM for CO2 Ref.11

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion
Chain39 – 305267Carbonic anhydrase 5A, mitochondrial
PRO_0000004234

Regions

Region235 – 2362Substrate binding By similarity

Sites

Active site1641 By similarity
Active site1671 Probable
Metal binding1301Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity
Metal binding1551Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P35218 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: C4E998D269AB1FE5

FASTA30534,750
        10         20         30         40         50         60 
MLGRNTWKTS AFSFLVEQMW APLWSRSMRP GRWCSQRSCA WQTSNNTLHP LWTVPVSVPG 

        70         80         90        100        110        120 
GTRQSPINIQ WRDSVYDPQL KPLRVSYEAA SCLYIWNTGY LFQVEFDDAT EASGISGGPL 

       130        140        150        160        170        180 
ENHYRLKQFH FHWGAVNEGG SEHTVDGHAY PAELHLVHWN SVKYQNYKEA VVGENGLAVI 

       190        200        210        220        230        240 
GVFLKLGAHH QTLQRLVDIL PEIKHKDARA AMRPFDPSTL LPTCWDYWTY AGSLTTPPLT 

       250        260        270        280        290        300 
ESVTWIIQKE PVEVAPSQLS AFRTLLFSAL GEEEKMMVNN YRPLQPLMNR KVWASFQATN 


EGTRS 

« Hide

References

« Hide 'large scale' references
[1]"Human mitochondrial carbonic anhydrase: cDNA cloning, expression, subcellular localization, and mapping to chromosome 16."
Nagao Y., Platero J.S., Waheed A., Sly W.S.
Proc. Natl. Acad. Sci. U.S.A. 90:7623-7627(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Genomic organization of the human gene (CA5) and pseudogene for mitochondrial carbonic anhydrase V and their localization to chromosomes 16q and 16p."
Nagao Y., Batanian J.R., Clemente M.F., Sly W.S.
Genomics 28:477-484(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Umbilical cord.
[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 (SEP-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].
[5]"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
Temperini C., Scozzafava A., Vullo D., Supuran C.T.
Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[6]"Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
Temperini C., Scozzafava A., Vullo D., Supuran C.T.
J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[7]"Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[8]"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.
[9]"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.
[10]"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.
[11]"Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19297 mRNA. Translation: AAA02890.1.
U25134 Genomic DNA. Translation: AAC99806.1.
S80181 expand/collapse EMBL AC list , S80175, S80176, S80177, S80178, S80240, S80180 Genomic DNA. Translation: AAB47048.1.
CH471114 Genomic DNA. Translation: EAW95372.1.
BC137405 mRNA. Translation: AAI37406.1.
BC137411 mRNA. Translation: AAI37412.1.
CCDSCCDS10965.1.
PIRCRHU5. A47745.
RefSeqNP_001730.1. NM_001739.1.
UniGeneHs.177446.

3D structure databases

ProteinModelPortalP35218.
SMRP35218. Positions 61-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107218. 1 interaction.

Chemistry

BindingDBP35218.
ChEMBLCHEMBL2111457.

PTM databases

PhosphoSiteP35218.

Polymorphism databases

DMDM461680.

Proteomic databases

MaxQBP35218.
PaxDbP35218.
PRIDEP35218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309893; ENSP00000309649; ENSG00000174990.
GeneID763.
KEGGhsa:763.
UCSCuc002fkn.1. human.

Organism-specific databases

CTD763.
GeneCardsGC16M087921.
HGNCHGNC:1377. CA5A.
MIM114761. gene.
neXtProtNX_P35218.
PharmGKBPA25992.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP35218.
KOK01672.
OMAFFQVEFD.
OrthoDBEOG7WMCK7.
PhylomeDBP35218.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP35218.

Gene expression databases

BgeeP35218.
CleanExHS_CA5A.
GenevestigatorP35218.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 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

GenomeRNAi763.
NextBio3086.
PROP35218.
SOURCESearch...

Entry information

Entry nameCAH5A_HUMAN
AccessionPrimary (citable) accession number: P35218
Secondary accession number(s): B2RPF2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 126 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 16

Human chromosome 16: entries, gene names and cross-references to MIM