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P18915 (CAH6_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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 6

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase VI
Carbonic anhydrase VI
Short name=CA-VI
Salivary carbonic anhydrase
Secreted carbonic anhydrase
Gene names
Name:CA6
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length319 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. Its role in saliva is unknown.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Subcellular location

Secreted.

Tissue specificity

Major constituent of saliva.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 1414 Ref.2
Chain15 – 319305Carbonic anhydrase 6
PRO_0000004239

Regions

Region215 – 2162Substrate binding By similarity

Sites

Active site801Proton acceptor By similarity
Active site1411 By similarity
Metal binding1061Zinc; catalytic By similarity
Metal binding1081Zinc; catalytic By similarity
Metal binding1331Zinc; catalytic By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...)
Glycosylation2511N-linked (GlcNAc...)
Disulfide bond37 ↔ 219 Potential

Experimental info

Sequence conflict161H → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18915 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 179884A7A9083AED

FASTA31937,007
        10         20         30         40         50         60 
MITLLFLLVV GAQAQHEWTY SEGVLDEKHW RLQYPDCGGT RQSPIDLKMK KVRYNPSLRA 

        70         80         90        100        110        120 
LNLTGYGLRQ GEFPMTNNGH TVQISLPSSM RMTTSDGSQY LAKQMHFHWG GDSSEISGSE 

       130        140        150        160        170        180 
HTVDGMRYII EIHVVHYHSK YGSYEEAQNE PDGLAVLAAL VEVKDYAENT YYSNFISHLE 

       190        200        210        220        230        240 
DIRYAGQSTV LRDLDIQDML PGDLRYYYSY LGSLTTPSCT ENVHWFVVAD TVKLSKTQIE 

       250        260        270        280        290        300 
KLENSLLNHQ NETIQNNYRS TQPLNHRVVE ANFVSHPHQE YTLGSKLHFY LNNIDQNLEY 

       310 
LRRFIEQKIT KRKKEKYWP 

« Hide

References

[1]"Sequence of bovine carbonic anhydrase VI: potential recognition sites for N-acetylgalactosaminyltransferase."
Jiang W., Woitach J.T., Gupta D.
Biochem. J. 318:291-296(1996) [PubMed: 8761494] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Submandibular gland.
[2]"Tissue and species distribution of the secreted carbonic anhydrase isoenzyme."
Fernley R.T., Darling P., Aldred P., Wright R.D., Coghlan J.P.
Biochem. J. 259:91-96(1989) [PubMed: 2497732] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-39.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96503 mRNA. Translation: CAA65357.1.
IPIIPI00688247.
PIRS71877.
RefSeqNP_776323.1. NM_173898.2.
UniGeneBt.47.

3D structure databases

ProteinModelPortalP18915.
ModBaseSearch...

Protein-protein interaction databases

STRINGP18915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID280742.
KEGGbta:280742.

Organism-specific databases

CTD765.

Phylogenomic databases

eggNOGmaNOG16006.
GeneTreeENSGT00570000078862.
HOVERGENHBG002837.
InParanoidP18915.
OrthoDBEOG43FGWZ.

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018428. Carbonic_anhydrase_CA6.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
KOK01672.
PANTHERPTHR18952:SF17. Carbonic_anhydrase_CA6. 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...

Entry information

Entry nameCAH6_BOVIN
AccessionPrimary (citable) accession number: P18915
Secondary accession number(s): Q95322
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 15, 1999
Last modified: January 25, 2012
This is version 90 of the entry and version 2 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