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P48283 (CAH4_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 4

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase IV
Carbonic anhydrase IV
Short name=CA-IV
Gene names
Name:CA4
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 By similarity.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subunit structure

Interacts with SLC4A4. Ref.3

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 280262Carbonic anhydrase 4
PRO_0000004230
Propeptide281 – 30828Removed in mature form By similarity
PRO_0000004231

Regions

Region221 – 2222Substrate binding By similarity

Sites

Active site861Proton acceptor By similarity
Metal binding1131Zinc; catalytic By similarity
Metal binding1151Zinc; catalytic By similarity
Metal binding1381Zinc; catalytic By similarity

Amino acid modifications

Lipidation2801GPI-anchor amidated serine By similarity
Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 34 By similarity
Disulfide bond44 ↔ 225 By similarity

Sequences

Sequence LengthMass (Da)Tools
P48283 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: CDB29AED9D8CDEBC

FASTA30834,394
        10         20         30         40         50         60 
MQLLFALLAL GALRPLAGEE LHWCYEIQAS NYSCLGPDKW QEDCQKSRQS PINIVTTKAE 

        70         80         90        100        110        120 
VDHSLGRFHF SGYDQREARL VENNGHSVMV SLGDEISISG GGLPARYRAT QLHLHWSQEL 

       130        140        150        160        170        180 
DRGSEHSLDG ERSAMEMHIV HQKETGTSGN EVQDSDDSIA VLAFLVEAGP TMNEGFQPLV 

       190        200        210        220        230        240 
TALSAISIPG TNTTMAPSSL WDLLPAEEEL RHYFRYMGSL TTPACSETVV WTVFQEPIRL 

       250        260        270        280        290        300 
HRDQILEFSS KLYYDQERKM NMKDNVRPLQ RLGDRSVFKS QAAGQLLPLP LPTLLVPTLA 


CVMAGLLR 

« Hide

References

[1]"Expression of carbonic anhydrase IV mRNA in rabbit kidney: stimulation by metabolic acidosis."
Winkler C.A., Kittelberger A.M., Schwartz G.J.
Am. J. Physiol. 272:F551-F560(1997) [PubMed: 9140058] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Kidney cortex.
[2]Tamai S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Kidney cortex.
[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: 14567693] [Abstract]
Cited for: INTERACTION WITH SLC4A4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L48928 mRNA. Translation: AAC37337.1.
U58871 mRNA. Translation: AAB09467.1.
RefSeqNP_001075841.1. NM_001082372.1.
UniGeneOcu.2117.

3D structure databases

ProteinModelPortalP48283.
SMRP48283. Positions 23-280.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009226.

Organism-specific databases

CTD762.

Phylogenomic databases

eggNOGmaNOG17562.
GeneTreeENSGT00570000078862.
HOVERGENHBG002837.
OrthoDBEOG4FXR84.

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF5. Carbonic_anhydrase_CA4. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. False negative.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH4_RABIT
AccessionPrimary (citable) accession number: P48283
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 80 of the entry and version 1 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