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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

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Proton acceptorBy similarity
Metal bindingi114 – 1141Zinc; catalytic
Metal bindingi116 – 1161Zinc; catalytic
Metal bindingi139 – 1391Zinc; catalytic

GO - Molecular functioni

  1. carbonate dehydratase activity Source: MGI
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. bicarbonate transport Source: MGI
  2. carbon dioxide transport Source: MGI
  3. one-carbon metabolic process Source: InterPro
  4. organ development Source: Ensembl
  5. regulation of pH Source: MGI
  6. response to drug Source: Ensembl
  7. response to steroid hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_309678. Erythrocytes take up oxygen and release carbon dioxide.
REACT_318918. Erythrocytes take up carbon dioxide and release oxygen.
REACT_327358. 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
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1096574. Car4.

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: MGI
  2. anchored component of plasma membrane Source: MGI
  3. apical plasma membrane Source: MGI
  4. brush border membrane Source: MGI
  5. cell surface Source: MGI
  6. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
  7. extracellular vesicular exosome Source: MGI
  8. Golgi apparatus Source: MGI
  9. membrane Source: MGI
  10. perinuclear region of cytoplasm Source: MGI
  11. plasma membrane Source: MGI
  12. rough endoplasmic reticulum Source: MGI
  13. sarcolemma Source: Ensembl
  14. sarcoplasmic reticulum Source: Ensembl
  15. secretory granule membrane Source: MGI
  16. trans-Golgi network Source: MGI
  17. transport vesicle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 277260Carbonic anhydrase 4PRO_0000004228Add
BLAST
Propeptidei278 – 30528Removed in mature formSequence AnalysisPRO_0000004229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 35
Disulfide bondi45 ↔ 222
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
Lipidationi277 – 2771GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ64444.
PaxDbiQ64444.
PRIDEiQ64444.

PTM databases

PhosphoSiteiQ64444.

Expressioni

Gene expression databases

BgeeiQ64444.
CleanExiMM_CAR4.
ExpressionAtlasiQ64444. baseline and differential.
GenevestigatoriQ64444.

Interactioni

Subunit structurei

Interacts with SLC4A4.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

IntActiQ64444. 2 interactions.
MINTiMINT-4089751.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 295Combined sources
Beta strandi30 – 334Combined sources
Helixi38 – 403Combined sources
Helixi43 – 464Combined sources
Beta strandi47 – 493Combined sources
Helixi57 – 593Combined sources
Beta strandi70 – 734Combined sources
Beta strandi78 – 847Combined sources
Beta strandi86 – 927Combined sources
Beta strandi96 – 1005Combined sources
Beta strandi108 – 11710Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi125 – 1295Combined sources
Beta strandi135 – 14410Combined sources
Beta strandi156 – 16813Combined sources
Helixi171 – 1733Combined sources
Helixi174 – 1796Combined sources
Helixi180 – 1823Combined sources
Beta strandi189 – 1957Combined sources
Helixi198 – 2003Combined sources
Helixi204 – 2063Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi226 – 2338Combined sources
Beta strandi235 – 2384Combined sources
Helixi239 – 24810Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi275 – 2773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNCX-ray2.80A22-279[»]
3ZNCX-ray2.80A22-279[»]
ProteinModelPortaliQ64444.
SMRiQ64444. Positions 22-279.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64444.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 2192Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ64444.
KOiK18246.
OMAiQAESSNY.
OrthoDBiEOG7MD4QN.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNCX-ray2.80A22-279[»]
3ZNCX-ray2.80A22-279[»]
ProteinModelPortaliQ64444.
SMRiQ64444. Positions 22-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ64444. 2 interactions.
MINTiMINT-4089751.

PTM databases

PhosphoSiteiQ64444.

Proteomic databases

MaxQBiQ64444.
PaxDbiQ64444.
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

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ64444.
KOiK18246.
OMAiQAESSNY.
OrthoDBiEOG7MD4QN.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_309678. Erythrocytes take up oxygen and release carbon dioxide.
REACT_318918. Erythrocytes take up carbon dioxide and release oxygen.
REACT_327358. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiQ64444.
NextBioi281004.
PROiQ64444.
SOURCEiSearch...

Gene expression databases

BgeeiQ64444.
CleanExiMM_CAR4.
ExpressionAtlasiQ64444. baseline and differential.
GenevestigatoriQ64444.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the mouse gene coding for carbonic anhydrase IV."
    Tamai S., Cody L.B., Sly W.S.
    Biochem. Genet. 34:31-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  3. "Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter."
    Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.
    Biochemistry 42:12321-12329(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC4A4.
  4. "Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination."
    Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A., Dean T., Laipis P., Silverman D.N., Christianson D.W.
    Protein Sci. 7:556-563(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC ION.

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: April 1, 2015
This is version 131 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

External Data

Dasty 3

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 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.