Reviewed, UniProtKB/Swiss-Prot P35218 (CAH5A_HUMAN)

Names and origin

Protein names

Recommended name:
    Carbonic anhydrase 5A, mitochondrial
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase VA
      Short name=CA-VA
    Carbonate dehydratase VA

Gene names

Name:	CA5A
Synonyms:	CA5

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Ref.2 Non-traceable author statement. Source: ProtInc
Molecular function	carbonate dehydratase activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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
Sites
	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)
	P35218-1 [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: 8356065] [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: 7490083] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	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.
UniGene	Hs.177446
3D structure databases
SMR	P35218. Positions 61-296.
ModBase	Search...
Protein-protein interaction databases
STRING	P35218.
Proteomic databases
PRIDE	P35218.
Genome annotation databases
Ensembl	ENST00000309893; ENSP00000309649; ENSG00000174990; Homo sapiens. [Genome view]
GeneID	763.
KEGG	hsa:763.
UCSC	uc002fkn.1. human.
Organism-specific databases
CTD	763.
GeneCards	GC16M086479.
H-InvDB	HIX0038659.
HGNC	HGNC:1377. CA5A.
MIM	114761. gene.
PharmGKB	PA25992.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08743.
HOGENOM	HBG717384.
HOVERGEN	P35218.
InParanoid	P35218.
OMA	SYDAASC.
OrthoDB	EOG9GJ27G.
PhylomeDB	P35218.
Enzyme and pathway databases
BRENDA	4.2.1.1. 247.
Gene expression databases
ArrayExpress	P35218.
Bgee	P35218.
CleanEx	HS_CA5A.
Genevestigator	P35218.
GermOnline	ENSG00000174990. Homo sapiens.
Family and domain databases
InterPro	IPR001148. Carbonic_anhydrase_a-class_cat. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018437. Carbonic_anhydrase_CA5_mt. [Graphical view]
Gene3D	G3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHER	PTHR18952:SF25. Carbonic_anhydrase_CA5_mt. 1 hit. PTHR18952. Euk_COanhd. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
PROSITE	PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
BindingDB	P35218.
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:	January 19, 2010
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.