Carbonic anhydrase 7 - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Sites

Natural variations

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Preferred order of sections

Molecule processing

Regions

Sites

Natural variations

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

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P43166 (CAH7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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

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.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome 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	cytosol 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...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 264

264

Carbonic anhydrase 7

PRO_0000077431

Region

201 – 202

Substrate binding By similarity

Active site

Proton acceptor By similarity

Active site

130

By similarity

Metal binding

Zinc; catalytic

Metal binding

Zinc; catalytic

Metal binding

121

Zinc; catalytic

Alternative sequence

1 – 56

Missing in isoform 2.

VSP_044254

264

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7AD559FC6E07EF96 Show »	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 « Hide
Isoform 2 [UniParc]. Checksum: AF3D016A27182D18 Show »	FASTA	208	23,452
10 20 30 40 50 60 MSLSITNNGH SVQVDFNDSD DRTVVTGGPL EGPYRLKQFH FHWGKKHDVG SEHTVDGKSF 70 80 90 100 110 120 PSELHLVHWN AKKYSTFGEA ASAPDGLAVV GVFLETGDEH PSMNRLTDAL YMVRFKGTKA 130 140 150 160 170 180 QFSCFNPKCL LPASRHYWTY PGSLTTPPLS ESVTWIVLRE PICISERQMG KFRSLLFTSE 190 200 DDERIHMVNN FRPPQPLKGR VVKASFRA « Hide

	« 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[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] (ISOFORMS 1 AND 2).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton 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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 1). Tissue: Colon, Kidney and Stomach.
[6]	"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.
[7]	"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.
[8]	"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] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.

EMBL
GenBank
DDBJ

M76423

M76422 Genomic DNA. Translation: AAA51923.1.
AY075019 mRNA. Translation: AAL78167.1.
AY075020 mRNA. Translation: AAL78168.1.
AC004638 Genomic DNA. Translation: AAC23785.1.
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83047.1.
BC033865 mRNA. Translation: AAH33865.1.

IPI

IPI00016493.

PIR

CRHU7. A55272.

RefSeq

NP_001014435.1. NM_001014435.1.
NP_005173.1. NM_005182.2.

UniGene

Hs.37014.

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.

ModBase

Search...

STRING

9606.ENSP00000345659.

PhosphoSite

P43166.

DMDM

1168744.

PaxDb

P43166.

PRIDE

P43166.

DNASU

766.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENST00000338437; ENSP00000345659; ENSG00000168748.
ENST00000394069; ENSP00000377632; ENSG00000168748.

GeneID

766.

KEGG

hsa:766.

UCSC

uc002eqi.3. human.

CTD

766.

GeneCards

GC16P066880.

HGNC

HGNC:1381. CA7.

HPA

HPA047237.

MIM

114770. gene.

neXtProt

NX_P43166.

PharmGKB

PA25996.

GenAtlas

Search...

eggNOG

COG3338.

HOGENOM

HOG000112637.

HOVERGEN

HBG002837.

InParanoid

P43166.

K01672.

OMA

GPSQWHK.

OrthoDB

EOG4H72C6.

PhylomeDB

P43166.

BRENDA

4.2.1.1. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P43166.

ArrayExpress

P43166.

Bgee

P43166.

CleanEx

HS_CA7.

Genevestigator

P43166.

GermOnline

ENSG00000168748. Homo sapiens.

Gene3D

3.10.200.10. 1 hit.

InterPro

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

PANTHER

PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF26. PTHR18952:SF26. 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...

BindingDB

P43166.

ChEMBL

CHEMBL2326.

GenomeRNAi

766.

NextBio

3096.

SOURCE

Search...

Entry name

CAH7_HUMAN

Accession

Primary (citable) accession number: P43166
Secondary accession number(s): Q541F0, Q86YU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 115 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.

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P43166-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P43166-2)

The sequence of this isoform differs from the canonical sequence as follows:
1-56: Missing.