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Q9ERQ8 (CAH7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Synonyms:Car7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Carbonic anhydrase 7
PRO_0000077432

Regions

Region201 – 2022Substrate binding By similarity

Sites

Active site661Proton acceptor By similarity
Active site1301 By similarity
Metal binding961Zinc; catalytic By similarity
Metal binding981Zinc; catalytic By similarity
Metal binding1211Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ERQ8 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: B58E0E20CB840FA5

FASTA26429,915
        10         20         30         40         50         60 
MTGHHCWGYG QDDGPSNWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE LFYEACMSLS 

        70         80         90        100        110        120 
ITNNGHSVQV DFNDSDDRTV VSGGPLEGPY RLKQLHFHWG KKRDMGSEHT VDGKSFPSEL 

       130        140        150        160        170        180 
HLVHWNAKKY STFGEAAAAP DGLAVVGVFL ETGDEHPSMN RLTDALYMVR FKDTKAQFSC 

       190        200        210        220        230        240 
FNPKCLLPTS RHYWTYPGSL TTPPLSESVT WIVLREPIRI SERQMEKFRS LLFTSEDDER 

       250        260 
IHMVDNFRPP QPLKGRVVKA SFQA 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Conservation of the deduced amino acid sequences of human and mouse carbonic anhydrase VII cDNAs."
Ling B., Bergenhem N.C.H., Tashian R.E.
Isozyme Bull. 28:32-32(1995)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-264.
Strain: C57BL/6.
Tissue: Brain.
[4]"The catalytic properties of murine carbonic anhydrase VII."
Earnhardt J.N., Qian M., Tu C., Lakkis M.M., Bergenhem N.C., Laipis P.J., Tashian R.E., Silverman D.N.
Biochemistry 37:10837-10845(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY075021 mRNA. Translation: AAL78169.1.
BC094913 mRNA. Translation: AAH94913.1.
AF291660 mRNA. Translation: AAG16230.1.
RefSeqNP_444300.1. NM_053070.3.
UniGeneMm.129265.

3D structure databases

ProteinModelPortalQ9ERQ8.
SMRQ9ERQ8. Positions 5-262.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ9ERQ8.
ChEMBLCHEMBL2216.

PTM databases

PhosphoSiteQ9ERQ8.

Proteomic databases

PRIDEQ9ERQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056051; ENSMUSP00000052136; ENSMUSG00000031883.
GeneID12354.
KEGGmmu:12354.
UCSCuc009nat.1. mouse.

Organism-specific databases

CTD12354.
MGIMGI:103100. Car7.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00750000117305.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidQ9ERQ8.
KOK01672.
OMAHWGKKHS.
OrthoDBEOG7WMCK7.
PhylomeDBQ9ERQ8.
TreeFamTF316425.

Gene expression databases

BgeeQ9ERQ8.
CleanExMM_CAR7.
GenevestigatorQ9ERQ8.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018438. Carbonic_anhydrase_CA7.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF26. PTHR18952:SF26. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281016.
PROQ9ERQ8.
SOURCESearch...

Entry information

Entry nameCAH7_MOUSE
AccessionPrimary (citable) accession number: Q9ERQ8
Secondary accession number(s): Q811X4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: August 16, 2005
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot