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P35218

- CAH5A_HUMAN

UniProt

P35218 - CAH5A_HUMAN

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Protein
Carbonic anhydrase 5A, mitochondrial
Gene
CA5A, CA5
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Zinc 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; catalytic By similarity
Metal bindingi132 – 1321Zinc; catalytic By similarity
Metal bindingi155 – 1551Zinc; catalytic By similarity
Active sitei164 – 1641 By similarity
Active sitei167 – 1671 Inferred

GO - Molecular functioni

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

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-RKiP35218.

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: 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

Organism-specific databases

PharmGKBiPA25992.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838Mitochondrion
Add
BLAST
Chaini39 – 305267Carbonic anhydrase 5A, mitochondrial
PRO_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.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP35218.
KOiK01672.
OMAiFFQVEFD.
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

MLGRNTWKTS AFSFLVEQMW APLWSRSMRP GRWCSQRSCA WQTSNNTLHP    50
LWTVPVSVPG GTRQSPINIQ WRDSVYDPQL KPLRVSYEAA SCLYIWNTGY 100
LFQVEFDDAT EASGISGGPL ENHYRLKQFH FHWGAVNEGG SEHTVDGHAY 150
PAELHLVHWN SVKYQNYKEA VVGENGLAVI GVFLKLGAHH QTLQRLVDIL 200
PEIKHKDARA AMRPFDPSTL LPTCWDYWTY AGSLTTPPLT ESVTWIIQKE 250
PVEVAPSQLS AFRTLLFSAL GEEEKMMVNN YRPLQPLMNR KVWASFQATN 300
EGTRS 305
Length:305
Mass (Da):34,750
Last modified:February 1, 1994 - v1
Checksum:iC4E998D269AB1FE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10965.1.
PIRi A47745. CRHU5.
RefSeqi NP_001730.1. NM_001739.1.
UniGenei Hs.177446.

3D structure databases

ProteinModelPortali P35218.
SMRi P35218. Positions 61-296.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107218. 1 interaction.

Chemistry

BindingDBi P35218.
ChEMBLi CHEMBL2111457.

PTM databases

PhosphoSitei P35218.

Polymorphism databases

DMDMi 461680.

Proteomic databases

MaxQBi P35218.
PaxDbi P35218.
PRIDEi P35218.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309893 ; ENSP00000309649 ; ENSG00000174990 .
GeneIDi 763.
KEGGi hsa:763.
UCSCi uc002fkn.1. human.

Organism-specific databases

CTDi 763.
GeneCardsi GC16M087921.
HGNCi HGNC:1377. CA5A.
MIMi 114761. gene.
neXtProti NX_P35218.
PharmGKBi PA25992.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3338.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P35218.
KOi K01672.
OMAi FFQVEFD.
OrthoDBi EOG7WMCK7.
PhylomeDBi P35218.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 2681.
Reactomei REACT_121123. Reversible hydration of carbon dioxide.
SABIO-RKi P35218.

Miscellaneous databases

GenomeRNAii 763.
NextBioi 3086.
PROi P35218.
SOURCEi Search...

Gene expression databases

Bgeei P35218.
CleanExi HS_CA5A.
Genevestigatori P35218.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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. 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.

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: September 3, 2014
This is version 127 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. 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

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