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Protein

Carbonic anhydrase 5A, mitochondrial

Gene

CA5A

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. Low activity.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

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).7 Publications

Kineticsi

  1. KM=10.0 mM for CO21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Zinc; catalyticBy similarity
Metal bindingi132 – 1321Zinc; catalyticBy similarity
Metal bindingi155 – 1551Zinc; catalyticBy similarity
Active sitei164 – 1641By similarity
Active sitei167 – 1671Curated

GO - Molecular functioni

  1. carbonate dehydratase activity Source: ProtInc
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. bicarbonate transport Source: Reactome
  2. one-carbon metabolic process Source: InterPro
  3. small molecule metabolic process Source: Reactome
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.
SABIO-RKP35218.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 5A, mitochondrial (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase VA
Carbonic anhydrase VA
Short name:
CA-VA
Gene namesi
Name:CA5A
Synonyms:CA5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1377. CA5A.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Hyperammonemia due to carbonic anhydrase VA deficiency (CA5AD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive inborn error of metabolism, clinically characterized by infantile hyperammonemic encephalopathy. Metabolic abnormalities include hypoglycemia, hyperlactatemia, metabolic acidosis and respiratory alkalosis.

See also OMIM:615751
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331S → P in CA5AD; reduced enzymatic activity. 1 Publication
VAR_071188

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615751. phenotype.
Orphaneti401948. Hyperammonemic encephalopathy due to carbonic anhydrase VA deficiency.
PharmGKBiPA25992.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionAdd
BLAST
Chaini39 – 305267Carbonic anhydrase 5A, mitochondrialPRO_0000004234Add
BLAST

Proteomic databases

MaxQBiP35218.
PaxDbiP35218.
PRIDEiP35218.

PTM databases

PhosphoSiteiP35218.

Expressioni

Gene expression databases

BgeeiP35218.
CleanExiHS_CA5A.
GenevestigatoriP35218.

Interactioni

Protein-protein interaction databases

BioGridi107218. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP35218.
SMRiP35218. Positions 61-296.
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.
InParanoidiP35218.
KOiK01672.
OMAiCLLPACR.
OrthoDBiEOG7WMCK7.
PhylomeDBiP35218.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 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.

P35218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGRNTWKTS AFSFLVEQMW APLWSRSMRP GRWCSQRSCA WQTSNNTLHP
60 70 80 90 100
LWTVPVSVPG GTRQSPINIQ WRDSVYDPQL KPLRVSYEAA SCLYIWNTGY
110 120 130 140 150
LFQVEFDDAT EASGISGGPL ENHYRLKQFH FHWGAVNEGG SEHTVDGHAY
160 170 180 190 200
PAELHLVHWN SVKYQNYKEA VVGENGLAVI GVFLKLGAHH QTLQRLVDIL
210 220 230 240 250
PEIKHKDARA AMRPFDPSTL LPTCWDYWTY AGSLTTPPLT ESVTWIIQKE
260 270 280 290 300
PVEVAPSQLS AFRTLLFSAL GEEEKMMVNN YRPLQPLMNR KVWASFQATN

EGTRS
Length:305
Mass (Da):34,750
Last modified:February 1, 1994 - v1
Checksum:iC4E998D269AB1FE5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331S → P in CA5AD; reduced enzymatic activity. 1 Publication
VAR_071188

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19297 mRNA. Translation: AAA02890.1.
U25134 Genomic DNA. Translation: AAC99806.1.
S80181
, 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.
CCDSiCCDS10965.1.
PIRiA47745. CRHU5.
RefSeqiNP_001730.1. NM_001739.1.
UniGeneiHs.177446.

Genome annotation databases

EnsembliENST00000309893; ENSP00000309649; ENSG00000174990.
GeneIDi763.
KEGGihsa:763.
UCSCiuc002fkn.1. human.

Polymorphism databases

DMDMi461680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19297 mRNA. Translation: AAA02890.1.
U25134 Genomic DNA. Translation: AAC99806.1.
S80181
, 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.
CCDSiCCDS10965.1.
PIRiA47745. CRHU5.
RefSeqiNP_001730.1. NM_001739.1.
UniGeneiHs.177446.

3D structure databases

ProteinModelPortaliP35218.
SMRiP35218. Positions 61-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107218. 1 interaction.

Chemistry

BindingDBiP35218.
ChEMBLiCHEMBL2111457.
DrugBankiDB01194. Brinzolamide.
DB00909. Zonisamide.

PTM databases

PhosphoSiteiP35218.

Polymorphism databases

DMDMi461680.

Proteomic databases

MaxQBiP35218.
PaxDbiP35218.
PRIDEiP35218.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309893; ENSP00000309649; ENSG00000174990.
GeneIDi763.
KEGGihsa:763.
UCSCiuc002fkn.1. human.

Organism-specific databases

CTDi763.
GeneCardsiGC16M087921.
HGNCiHGNC:1377. CA5A.
MIMi114761. gene.
615751. phenotype.
neXtProtiNX_P35218.
Orphaneti401948. Hyperammonemic encephalopathy due to carbonic anhydrase VA deficiency.
PharmGKBiPA25992.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP35218.
KOiK01672.
OMAiCLLPACR.
OrthoDBiEOG7WMCK7.
PhylomeDBiP35218.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
SABIO-RKP35218.

Miscellaneous databases

GenomeRNAii763.
NextBioi3086.
PROiP35218.
SOURCEiSearch...

Gene expression databases

BgeeiP35218.
CleanExiHS_CA5A.
GenevestigatoriP35218.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 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: 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(1992) [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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Umbilical cord.
  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(2003) [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(2005) [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(2005) [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(2006) [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(2006) [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(2008) [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(2008) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANT CA5AD PRO-233, CHARACTERIZATION OF VARIANT CA5AD PRO-233.

Entry informationi

Entry nameiCAH5A_HUMAN
AccessioniPrimary (citable) accession number: P35218
Secondary accession number(s): B2RPF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: March 4, 2015
This is version 132 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.