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Protein

Carbonic anhydrase 7

Gene

Ca7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661Proton acceptorBy similarity
Metal bindingi96 – 961Zinc; catalyticBy similarity
Metal bindingi98 – 981Zinc; catalyticBy similarity
Metal bindingi121 – 1211Zinc; catalyticBy similarity
Active sitei130 – 1301By similarity

GO - Molecular functioni

  • carbonate dehydratase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • mitophagy in response to mitochondrial depolarization Source: MGI
  • one-carbon metabolic process Source: InterPro
  • positive regulation of cellular pH reduction Source: MGI
  • positive regulation of defense response to virus by host Source: MGI
  • positive regulation of synaptic transmission, GABAergic Source: MGI
  • regulation of chloride transport Source: MGI
  • xenophagy Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1475029. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 7 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase VII
Carbonic anhydrase VII
Short name:
CA-VII
Gene namesi
Name:Ca7
Synonyms:Car7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:103100. Car7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Carbonic anhydrase 7PRO_0000077432Add
BLAST

Proteomic databases

MaxQBiQ9ERQ8.
PaxDbiQ9ERQ8.
PRIDEiQ9ERQ8.

PTM databases

PhosphoSiteiQ9ERQ8.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031883.
CleanExiMM_CAR7.
ExpressionAtlasiQ9ERQ8. baseline and differential.
GenevisibleiQ9ERQ8. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052136.

Chemistry

BindingDBiQ9ERQ8.

Structurei

3D structure databases

ProteinModelPortaliQ9ERQ8.
SMRiQ9ERQ8. Positions 5-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 262258Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2022Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9ERQ8.
KOiK01672.
OMAiLVHWNAR.
OrthoDBiEOG091G0XFM.
PhylomeDBiQ9ERQ8.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018438. Carbonic_anhydrase_CA7.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF124. PTHR18952:SF124. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ERQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGHHCWGYG QDDGPSNWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE
60 70 80 90 100
LFYEACMSLS ITNNGHSVQV DFNDSDDRTV VSGGPLEGPY RLKQLHFHWG
110 120 130 140 150
KKRDMGSEHT VDGKSFPSEL HLVHWNAKKY STFGEAAAAP DGLAVVGVFL
160 170 180 190 200
ETGDEHPSMN RLTDALYMVR FKDTKAQFSC FNPKCLLPTS RHYWTYPGSL
210 220 230 240 250
TTPPLSESVT WIVLREPIRI SERQMEKFRS LLFTSEDDER IHMVDNFRPP
260
QPLKGRVVKA SFQA
Length:264
Mass (Da):29,915
Last modified:August 16, 2005 - v2
Checksum:iB58E0E20CB840FA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY075021 mRNA. Translation: AAL78169.1.
BC094913 mRNA. Translation: AAH94913.1.
AF291660 mRNA. Translation: AAG16230.1.
CCDSiCCDS22581.1.
RefSeqiNP_001288093.1. NM_001301164.1.
NP_001288094.1. NM_001301165.1.
NP_444300.1. NM_053070.3.
UniGeneiMm.129265.

Genome annotation databases

EnsembliENSMUST00000056051; ENSMUSP00000052136; ENSMUSG00000031883.
GeneIDi12354.
KEGGimmu:12354.
UCSCiuc009nat.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY075021 mRNA. Translation: AAL78169.1.
BC094913 mRNA. Translation: AAH94913.1.
AF291660 mRNA. Translation: AAG16230.1.
CCDSiCCDS22581.1.
RefSeqiNP_001288093.1. NM_001301164.1.
NP_001288094.1. NM_001301165.1.
NP_444300.1. NM_053070.3.
UniGeneiMm.129265.

3D structure databases

ProteinModelPortaliQ9ERQ8.
SMRiQ9ERQ8. Positions 5-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052136.

Chemistry

BindingDBiQ9ERQ8.
ChEMBLiCHEMBL2216.

PTM databases

PhosphoSiteiQ9ERQ8.

Proteomic databases

MaxQBiQ9ERQ8.
PaxDbiQ9ERQ8.
PRIDEiQ9ERQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056051; ENSMUSP00000052136; ENSMUSG00000031883.
GeneIDi12354.
KEGGimmu:12354.
UCSCiuc009nat.2. mouse.

Organism-specific databases

CTDi12354.
MGIiMGI:103100. Car7.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9ERQ8.
KOiK01672.
OMAiLVHWNAR.
OrthoDBiEOG091G0XFM.
PhylomeDBiQ9ERQ8.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiR-MMU-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

PROiQ9ERQ8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031883.
CleanExiMM_CAR7.
ExpressionAtlasiQ9ERQ8. baseline and differential.
GenevisibleiQ9ERQ8. MM.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018438. Carbonic_anhydrase_CA7.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF124. PTHR18952:SF124. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAH7_MOUSE
AccessioniPrimary (citable) accession number: Q9ERQ8
Secondary accession number(s): Q811X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: August 16, 2005
Last modified: September 7, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.