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Q64444

- CAH4_MOUSE

UniProt

Q64444 - CAH4_MOUSE

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Protein

Carbonic anhydrase 4

Gene
Ca4, Car4
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Inhibited by acetazolamide By similarity.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. bicarbonate transport Source: Ensembl
  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_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199096. Reversible hydration of carbon dioxide.
REACT_199098. Erythrocytes take up oxygen and release 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: Chromosome 11

Organism-specific databases

MGIiMGI:1096574. Car4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
BLAST
Chaini18 – 277260Carbonic anhydrase 4PRO_0000004228Add
BLAST
Propeptidei278 – 30528Removed in mature form Reviewed predictionPRO_0000004229Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ64444.
PaxDbiQ64444.
PRIDEiQ64444.

PTM databases

PhosphoSiteiQ64444.

Expressioni

Gene expression databases

BgeeiQ64444.
CleanExiMM_CAR4.
GenevestigatoriQ64444.

Interactioni

Subunit structurei

Interacts with SLC4A4.1 Publication

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 – 295
Beta strandi30 – 334
Helixi38 – 403
Helixi43 – 464
Beta strandi47 – 493
Helixi57 – 593
Beta strandi70 – 734
Beta strandi78 – 847
Beta strandi86 – 927
Beta strandi96 – 1005
Beta strandi108 – 11710
Beta strandi119 – 1235
Beta strandi125 – 1295
Beta strandi135 – 14410
Beta strandi156 – 16813
Helixi171 – 1733
Helixi174 – 1796
Helixi180 – 1823
Beta strandi189 – 1957
Helixi198 – 2003
Helixi204 – 2063
Beta strandi210 – 2156
Beta strandi226 – 2338
Beta strandi235 – 2384
Helixi239 – 24810
Beta strandi250 – 2523
Beta strandi275 – 2773

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNCX-ray2.80A22-279[»]
3ZNCX-ray2.80A22-279[»]
ProteinModelPortaliQ64444.
SMRiQ64444. Positions 22-279.

Miscellaneous databases

EvolutionaryTraceiQ64444.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00750000117527.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ64444.
KOiK18246.
OMAiKGTSRNV.
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

MQLLLALLAL AYVAPSTEDS GWCYEIQTKD PRSSCLGPEK WPGACKENQQ    50
SPINIVTART KVNPRLTPFI LVGYDQKQQW PIKNNQHTVE MTLGGGACII 100
GGDLPARYEA VQLHLHWSNG NDNGSEHSID GRHFAMEMHI VHKKLTSSKE 150
DSKDKFAVLA FMIEVGDKVN KGFQPLVEAL PSISKPHSTS TVRESSLQDM 200
LPPSTKMYTY FRYNGSLTTP NCDETVIWTV YKQPIKIHKN QFLEFSKNLY 250
YDEDQKLNMK DNVRPLQPLG KRQVFKSHAP GQLLSLPLPT LLVPTLTCLV 300
ANFLQ 305
Length:305
Mass (Da):34,351
Last modified:November 1, 1997 - v1
Checksum:iEEE988FF52732884
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U37091 Genomic DNA. Translation: AAC52569.1 .
BC012704 mRNA. Translation: AAH12704.1 .
CCDSi CCDS25190.1.
RefSeqi NP_031633.1. NM_007607.2.
UniGenei Mm.1641.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZNC X-ray 2.80 A 22-279 [» ]
3ZNC X-ray 2.80 A 22-279 [» ]
ProteinModelPortali Q64444.
SMRi Q64444. Positions 22-279.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q64444. 2 interactions.
MINTi MINT-4089751.

PTM databases

PhosphoSitei Q64444.

Proteomic databases

MaxQBi Q64444.
PaxDbi Q64444.
PRIDEi Q64444.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000103194 ; ENSMUSP00000099483 ; ENSMUSG00000000805 .
GeneIDi 12351.
KEGGi mmu:12351.
UCSCi uc007krg.2. mouse.

Organism-specific databases

CTDi 12351.
MGIi MGI:1096574. Car4.

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00750000117527.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi Q64444.
KOi K18246.
OMAi KGTSRNV.
OrthoDBi EOG7MD4QN.
TreeFami TF316425.

Enzyme and pathway databases

Reactomei REACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199096. Reversible hydration of carbon dioxide.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

Miscellaneous databases

EvolutionaryTracei Q64444.
NextBioi 281004.
PROi Q64444.
SOURCEi Search...

Gene expression databases

Bgeei Q64444.
CleanExi MM_CAR4.
Genevestigatori Q64444.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1996) [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(2004) [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(2003) [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(1998) [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: September 3, 2014
This is version 125 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

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