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Protein

Carbonic anhydrase 4

Gene

Ca4

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. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 (By similarity).By similarity

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+1 Publication

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei87Proton acceptorBy similarity1
Metal bindingi114Zinc; catalytic1 Publication1
Metal bindingi116Zinc; catalytic1 Publication1
Metal bindingi139Zinc; catalytic1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • bicarbonate transport Source: MGI
  • carbon dioxide transport Source: MGI
  • one-carbon metabolic process Source: InterPro
  • regulation of pH Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-MMU-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-MMU-1475029. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 4 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IV
Carbonic anhydrase IV
Short name:
CA-IV
Gene namesi
Name:Ca4
Synonyms:Car4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1096574. Car4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000422818 – 277Carbonic anhydrase 4Add BLAST260
PropeptideiPRO_0000004229278 – 305Removed in mature formSequence analysisAdd BLAST28

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi23 ↔ 351 Publication
Disulfide bondi45 ↔ 2221 Publication
Glycosylationi123N-linked (GlcNAc...)Sequence analysis1
Glycosylationi214N-linked (GlcNAc...)Sequence analysis1
Lipidationi277GPI-anchor amidated serineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ64444.
PaxDbiQ64444.
PeptideAtlasiQ64444.
PRIDEiQ64444.

PTM databases

PhosphoSitePlusiQ64444.

Expressioni

Gene expression databases

BgeeiENSMUSG00000000805.
CleanExiMM_CAR4.
ExpressionAtlasiQ64444. baseline and differential.
GenevisibleiQ64444. MM.

Interactioni

Subunit structurei

Interacts with SLC4A4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Slc4a4O883432EBI-6859308,EBI-771342

Protein-protein interaction databases

IntActiQ64444. 2 interactors.
MINTiMINT-4089751.
STRINGi10090.ENSMUSP00000099483.

Structurei

Secondary structure

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 29Combined sources5
Beta strandi30 – 33Combined sources4
Helixi38 – 40Combined sources3
Helixi43 – 46Combined sources4
Beta strandi47 – 49Combined sources3
Helixi57 – 59Combined sources3
Beta strandi70 – 73Combined sources4
Beta strandi78 – 84Combined sources7
Beta strandi86 – 92Combined sources7
Beta strandi96 – 100Combined sources5
Beta strandi108 – 117Combined sources10
Beta strandi119 – 123Combined sources5
Beta strandi125 – 129Combined sources5
Beta strandi135 – 144Combined sources10
Beta strandi156 – 168Combined sources13
Helixi171 – 173Combined sources3
Helixi174 – 179Combined sources6
Helixi180 – 182Combined sources3
Beta strandi189 – 195Combined sources7
Helixi198 – 200Combined sources3
Helixi204 – 206Combined sources3
Beta strandi210 – 215Combined sources6
Beta strandi226 – 233Combined sources8
Beta strandi235 – 238Combined sources4
Helixi239 – 248Combined sources10
Beta strandi250 – 252Combined sources3
Beta strandi275 – 277Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZNCX-ray2.80A22-279[»]
3ZNCX-ray2.80A22-279[»]
ProteinModelPortaliQ64444.
SMRiQ64444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64444.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 278Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni218 – 219Substrate bindingBy similarity2

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ64444.
KOiK18246.
OMAiSHFENIT.
OrthoDBiEOG091G0XFM.
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.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLLLALLAL AYVAPSTEDS GWCYEIQTKD PRSSCLGPEK WPGACKENQQ
60 70 80 90 100
SPINIVTART KVNPRLTPFI LVGYDQKQQW PIKNNQHTVE MTLGGGACII
110 120 130 140 150
GGDLPARYEA VQLHLHWSNG NDNGSEHSID GRHFAMEMHI VHKKLTSSKE
160 170 180 190 200
DSKDKFAVLA FMIEVGDKVN KGFQPLVEAL PSISKPHSTS TVRESSLQDM
210 220 230 240 250
LPPSTKMYTY FRYNGSLTTP NCDETVIWTV YKQPIKIHKN QFLEFSKNLY
260 270 280 290 300
YDEDQKLNMK DNVRPLQPLG KRQVFKSHAP GQLLSLPLPT LLVPTLTCLV

ANFLQ
Length:305
Mass (Da):34,351
Last modified:November 1, 1997 - v1
Checksum:iEEE988FF52732884
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37091 Genomic DNA. Translation: AAC52569.1.
BC012704 mRNA. Translation: AAH12704.1.
CCDSiCCDS25190.1.
RefSeqiNP_031633.1. NM_007607.2.
UniGeneiMm.1641.

Genome annotation databases

EnsembliENSMUST00000103194; ENSMUSP00000099483; ENSMUSG00000000805.
GeneIDi12351.
KEGGimmu:12351.
UCSCiuc007krg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37091 Genomic DNA. Translation: AAC52569.1.
BC012704 mRNA. Translation: AAH12704.1.
CCDSiCCDS25190.1.
RefSeqiNP_031633.1. NM_007607.2.
UniGeneiMm.1641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZNCX-ray2.80A22-279[»]
3ZNCX-ray2.80A22-279[»]
ProteinModelPortaliQ64444.
SMRiQ64444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64444. 2 interactors.
MINTiMINT-4089751.
STRINGi10090.ENSMUSP00000099483.

PTM databases

PhosphoSitePlusiQ64444.

Proteomic databases

MaxQBiQ64444.
PaxDbiQ64444.
PeptideAtlasiQ64444.
PRIDEiQ64444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103194; ENSMUSP00000099483; ENSMUSG00000000805.
GeneIDi12351.
KEGGimmu:12351.
UCSCiuc007krg.2. mouse.

Organism-specific databases

CTDi12351.
MGIiMGI:1096574. Car4.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ64444.
KOiK18246.
OMAiSHFENIT.
OrthoDBiEOG091G0XFM.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiR-MMU-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-MMU-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-MMU-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiQ64444.
PROiQ64444.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000805.
CleanExiMM_CAR4.
ExpressionAtlasiQ64444. baseline and differential.
GenevisibleiQ64444. 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.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 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 nameiCAH4_MOUSE
AccessioniPrimary (citable) accession number: Q64444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.