P43166 (CAH7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 7
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase VII
Carbonic anhydrase VII
Short name=CA-VII

Gene names

Name:

CA7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc.
Enzyme regulation	Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited coumarins, sulfonamide derivatives such as acetazolamide (AZA), by saccharin and Foscarnet (phosphonoformate trisodium salt). Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carbonate dehydratase activity Traceable author statement. 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

Chain

1 – 264

264

Carbonic anhydrase 7

PRO_0000077431

Regions

Region

201 – 202

2

Substrate binding By similarity

Sites

Active site

66

1

Proton acceptor By similarity

Active site

130

1

By similarity

Metal binding

96

1

Zinc; catalytic

Metal binding

98

1

Zinc; catalytic

Metal binding

121

1

Zinc; catalytic

Secondary structure

1

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264

Helix Strand Turn

Details...

Helix

18 – 20

3

Helix

23 – 25

3

Turn

37 – 39

3

Beta strand

40 – 42

3

Beta strand

58 – 63

6

Beta strand

68 – 72

5

Beta strand

75 – 82

8

Beta strand

90 – 98

9

Beta strand

109 – 111

3

Beta strand

117 – 125

9

Turn

127 – 129

3

Helix

136 – 138

3

Beta strand

144 – 146

3

Beta strand

148 – 151

4

Helix

158 – 160

3

Helix

161 – 165

5

Turn

166 – 169

4

Beta strand

175 – 177

3

Helix

183 – 186

4

Beta strand

193 – 196

4

Beta strand

210 – 216

7

Turn

222 – 224

3

Helix

228 – 230

3

Beta strand

232 – 234

3

Sequences

	Sequence		Length	Mass (Da)
	P43166 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7AD559FC6E07EF96	FASTA	264	29,658
	10 20 30 40 50 60 MTGHHGWGYG QDDGPSHWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE LSYEACMSLS 70 80 90 100 110 120 ITNNGHSVQV DFNDSDDRTV VTGGPLEGPY RLKQFHFHWG KKHDVGSEHT VDGKSFPSEL 130 140 150 160 170 180 HLVHWNAKKY STFGEAASAP DGLAVVGVFL ETGDEHPSMN RLTDALYMVR FKGTKAQFSC 190 200 210 220 230 240 FNPKCLLPAS RHYWTYPGSL TTPPLSESVT WIVLREPICI SERQMGKFRS LLFTSEDDER 250 260 IHMVNNFRPP QPLKGRVVKA SFRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the human gene for a newly discovered carbonic anhydrase, CA VII, and its localization to chromosome 16." Montgomery J.C., Venta P.J., Eddy R.L., Fukushima Y.S., Shows T.B., Tashian R.E. Genomics 11:835-848(1991) [PubMed: 1783392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular identification of carbonic anhydrases (CA) and CA-related (CAR) genes." Chen Y., Huang C.-H. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q." Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D. Genomics 60:295-308(1999) [PubMed: 10493829] [Abstract] 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]. Tissue: Colon, Kidney and Stomach.
[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: 16807956] [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: 16686544] [Abstract] Cited for: ENZYME REGULATION.
[7]	"Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste." Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G. Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed: 17705204] [Abstract] Cited for: ENZYME REGULATION.
[8]	"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: 17127057] [Abstract] Cited for: ENZYME REGULATION.
[9]	"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: 17314045] [Abstract] Cited for: ENZYME REGULATION.
[10]	"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: 19186056] [Abstract] Cited for: ENZYME REGULATION.
[11]	"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: 19206230] [Abstract] Cited for: ENZYME REGULATION.
[12]	"Crystal structure of human carbonic anhydrase VII [isoform 1], CA7." Structural genomics consortium (SGC) Submitted (JUN-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 5-262 IN COMPLEX WITH ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M76423 , M76420, M76421, M76422 Genomic DNA. Translation: AAA51923.1.
AY075019 mRNA. Translation: AAL78167.1.
AC004638 Genomic DNA. Translation: AAC23785.1.
BC033865 mRNA. Translation: AAH33865.1.

IPI

IPI00016493.

PIR

CRHU7. A55272.

RefSeq

NP_005173.1. NM_005182.2.

UniGene

Hs.37014.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MDZ	X-ray	2.32	A	5-262	[»]
3ML5	X-ray	2.05	A	1-264	[»]

ProteinModelPortal

P43166.

SMR

P43166. Positions 5-262.

ModBase

Search...

Protein-protein interaction databases

STRING

P43166.

Polymorphism databases

DMDM

1168744.

Proteomic databases

PRIDE

P43166.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338437; ENSP00000345659; ENSG00000168748.

GeneID

766.

KEGG

hsa:766.

UCSC

uc002eqi.1. human.

Organism-specific databases

CTD

766.

GeneCards

GC16P066880.

H-InvDB

HIX0013122.

HGNC

HGNC:1381. CA7.

MIM

114770. gene.

neXtProt

NX_P43166.

PharmGKB

PA25996.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06740.

HOGENOM

HBG717384.

HOVERGEN

HBG002837.

InParanoid

P43166.

OMA

HWGKKHS.

OrthoDB

EOG4H72C6.

PhylomeDB

P43166.

Enzyme and pathway databases

BRENDA

4.2.1.1. 2681.

Gene expression databases

ArrayExpress

P43166.

Bgee

P43166.

CleanEx

HS_CA7.

Genevestigator

P43166.

GermOnline

ENSG00000168748. Homo sapiens.

Family and domain databases

InterPro

IPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018438. Carbonic_anhydrase_CA7.
[Graphical view]

Gene3D

G3DSA:3.10.200.10. Euk_COanhd. 1 hit.

KO

K01672.

PANTHER

PTHR18952:SF26. Carbonic_anhydrase_CA7. 1 hit.
PTHR18952. Euk_COanhd. 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

P43166.

NextBio

3096.

SOURCE

Search...

Entry information

Entry name

CAH7_HUMAN

Accession

Primary (citable) accession number: P43166
Secondary accession number(s): Q541F0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 101 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.