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Reviewed, UniProtKB/Swiss-Prot Q95323 (CAH4_BOVIN)

Last modified November 3, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 4
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase IV
      Short name=CA-IV
    Carbonate dehydratase IV
Gene names
Name: CA4
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subunit structure

Interacts with SLC4A4 By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

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
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 284266Carbonic anhydrase 4
PRO_0000004224
Propeptide285 – 31228Removed in mature form By similarity
PRO_0000004225

Sites

Metal binding1151Zinc; catalytic
Metal binding1171Zinc; catalytic
Metal binding1401Zinc; catalytic

Amino acid modifications

Lipidation2841GPI-anchor amidated serine By similarity
Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 36 By similarity
Disulfide bond46 ↔ 229 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q95323-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: BAEA320C09426351

FASTA31235,151
        10         20         30         40         50         60 
MRLLLALLVL AAAPPQARAA SHWCYQIQVK PSNYTCLEPD EWEGSCQNNR QSPVNIVTAK 

        70         80         90        100        110        120 
TQLDPNLGRF SFSGYNMKHQ WVVQNNGHTV MVLLENKPSI AGGGLSTRYQ ATQLHLHWSR 

       130        140        150        160        170        180 
AMDRGSEHSF DGERFAMEMH IVHEKEKGLS GNASQNQFAE DEIAVLAFMV EDGSKNVNFQ 

       190        200        210        220        230        240 
PLVEALSDIP RPNMNTTMKE GVSLFDLLPE EESLRHYFRY LGSLTTPTCD EKVVWTVFQK 

       250        260        270        280        290        300 
PIQLHRDQIL AFSQKLFYDD QQKVNMTDNV RPVQSLGQRQ VFRSGAPGLL LAQPLPTLLA 

       310 
PVLACLTVGF LR 

« Hide

References

« Hide 'large scale' references
[1]"Bos taurus carbonic anhydrase IV (bovine carbonic anhydrase IV) mRNA, complete cds."
Tamai S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Holstein.
Tissue: Kidney.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

U58870 mRNA. Translation: AAB09466.1.
BC142534 mRNA. Translation: AAI42535.1.
IPIIPI00712612.
RefSeqNP_776322.1.
UniGeneBt.555

3D structure databases

HSSPHSSP built from PDB template 1ZNC based on UniProtKB P22748.
SMRQ95323. Positions 23-284.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ95323.

Genome annotation databases

EnsemblENSBTAT00000023909; ENSBTAP00000023909; ENSBTAG00000017969; Bos taurus. [Genome view]
GeneID280741.
KEGGbta:280741.

Organism-specific databases

CTD280741.

Phylogenomic databases

HOVERGENQ95323.
OMAQNNGHTV.

Enzyme and pathway databases

BRENDA4.2.1.1. 251.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
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]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. False negative.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH4_BOVIN
AccessionPrimary (citable) accession number: Q95323
Secondary accession number(s): A5PKL8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents