P35218 (CAH5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CA5A
Synonyms:	CA5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate transport Traceable author statement. Source: Reactome one-carbon metabolic process Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	carbonate dehydratase activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 38	38	Mitochondrion
	Chain	39 – 305	267	Carbonic anhydrase 5A, mitochondrial		PRO_0000004234
Regions
	Region	235 – 236	2	Substrate binding By similarity
Sites
	Active site	164	1	By similarity
	Active site	167	1	Probable
	Metal binding	130	1	Zinc; catalytic By similarity
	Metal binding	132	1	Zinc; catalytic By similarity
	Metal binding	155	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35218 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: C4E998D269AB1FE5	FASTA	305	34,750
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
IPI	IPI00017262.
PIR	CRHU5. A47745.
RefSeq	NP_001730.1. NM_001739.1.
UniGene	Hs.177446.
3D structure databases
ProteinModelPortal	P35218.
ModBase	Search...
PTM databases
PhosphoSite	P35218.
Polymorphism databases
DMDM	461680.
Proteomic databases
PaxDb	P35218.
PRIDE	P35218.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309893; ENSP00000309649; ENSG00000174990.
GeneID	763.
KEGG	hsa:763.
UCSC	uc002fkn.1. human.
Organism-specific databases
CTD	763.
GeneCards	GC16M087921.
HGNC	HGNC:1377. CA5A.
MIM	114761. gene.
neXtProt	NX_P35218.
PharmGKB	PA25992.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3338.
HOGENOM	HOG000112637.
HOVERGEN	HBG002837.
InParanoid	P35218.
KO	K01672.
OMA	FDDSTEG.
OrthoDB	EOG4FR0RX.
PhylomeDB	P35218.
Enzyme and pathway databases
BRENDA	4.2.1.1. 2681.
Reactome	REACT_111217. Metabolism.
SABIO-RK	P35218.
Gene expression databases
Bgee	P35218.
CleanEx	HS_CA5A.
Genevestigator	P35218.
GermOnline	ENSG00000174990. Homo sapiens.
Family and domain databases
Gene3D	3.10.200.10. 1 hit.
InterPro	IPR018437. CA-V_mt. IPR001148. Carbonic_anhydrase_a. IPR023561. Carbonic_anhydrase_a-class. IPR018338. Carbonic_anhydrase_a-class_CS. [Graphical view]
PANTHER	PTHR18952. PTHR18952. 1 hit. PTHR18952:SF25. PTHR18952:SF25. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
SMART	SM01057. Carb_anhydrase. 1 hit. [Graphical view]
SUPFAM	SSF51069. Euk_COanhd. 1 hit.
PROSITE	PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P35218.
ChEMBL	CHEMBL4789.
GenomeRNAi	763.
NextBio	3086.
SOURCE	Search...

Entry information

Entry name

CAH5A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.