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P48284 (CAH4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length309 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 By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor By similarity.

Tissue specificity

Present in kidney and lung. Also particularly abundant in brain, muscle, heart and liver. Not detected in skin or spleen. Ref.3

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 281264Carbonic anhydrase 4
PRO_0000004232
Propeptide282 – 30928Removed in mature form By similarity
PRO_0000004233

Regions

Region222 – 2232Substrate binding By similarity

Sites

Active site871Proton acceptor By similarity
Metal binding1141Zinc; catalytic By similarity
Metal binding1161Zinc; catalytic By similarity
Metal binding1391Zinc; catalytic By similarity

Amino acid modifications

Lipidation2811GPI-anchor amidated serine By similarity
Glycosylation1931N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 35 By similarity
Disulfide bond45 ↔ 226 By similarity

Sequences

Sequence LengthMass (Da)Tools
P48284 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9EBD1315348CFC8C

FASTA30935,076
        10         20         30         40         50         60 
MQLLLALLAL AYVAPSTEDS HWCYEIQAKE PNSHCSGPEQ WTGDCKKNQQ SPINIVTSKT 

        70         80         90        100        110        120 
KLNPSLTPFT FVGYDQKKKW EVKNNQHSVE MSLGEDIYIF GGDLPTQYKA IQLHLHWSEE 

       130        140        150        160        170        180 
SNKGSEHSID GKHFAMEMHV VHKKMTTGDK VQDSDSKDKI AVLAFMVEVG NEVNEGFQPL 

       190        200        210        220        230        240 
VEALSRLSKP FTNSTVSESC LQDMLPEKKK LSAYFRYQGS LTTPGCDETV IWTVFEEPIK 

       250        260        270        280        290        300 
IHKDQFLEFS KKLYYDQEQK LNMKDNVRPL QPLGNRQVFR SHASGRLLSL PLPTLLVPTL 


TCLVASFLH 

« Hide

References

« Hide 'large scale' references
[1]"Pulmonary carbonic anhydrase IV: developmental regulation and cell-specific expression in the capillary endothelium."
Fleming R.E., Crouch E.C., Ruzicka C.A., Sly W.S.
Am. J. Physiol. 265:L627-L635(1993) [PubMed: 8279579] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Lung.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]"Membrane-associated carbonic anhydrase from rat lung. Purification, characterization, tissue distribution, and comparison with carbonic anhydrase IVs of other mammals."
Waheed A., Zhu X.L., Sly W.S.
J. Biol. Chem. 267:3308-3311(1992) [PubMed: 1737787] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-22; 24-33 AND 36-38, CHARACTERIZATION, TISSUE SPECIFICITY.
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S68245 mRNA. Translation: AAB29505.1.
BC097329 mRNA. Translation: AAH97329.1.
IPIIPI00189083.
PIRI51900.
RefSeqNP_062047.1. NM_019174.1.
UniGeneRn.51389.

3D structure databases

ProteinModelPortalP48284.
SMRP48284. Positions 22-283.
ModBaseSearch...

Protein-protein interaction databases

STRINGP48284.

Proteomic databases

PRIDEP48284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003908; ENSRNOP00000003908; ENSRNOG00000002916.
GeneID29242.
KEGGrno:29242.
UCSCNM_019174. rat.

Organism-specific databases

CTD12351.
RGD2242. Ca4.

Phylogenomic databases

eggNOGroNOG16065.
GeneTreeENSGT00570000078862.
HOVERGENHBG002837.
OrthoDBEOG4FXR84.
PhylomeDBP48284.

Gene expression databases

ArrayExpressP48284.
GenevestigatorP48284.
GermOnlineENSRNOG00000002916. Rattus norvegicus.

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
KOK01672.
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. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608518.

Entry information

Entry nameCAH4_RAT
AccessionPrimary (citable) accession number: P48284
Secondary accession number(s): Q4QR97
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 89 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