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Reviewed, UniProtKB/Swiss-Prot P23280 (CAH6_HUMAN)

Last modified June 16, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

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Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 6
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase VI
      Short name=CA-VI
    Carbonate dehydratase VI
    Secreted carbonic anhydrase
    Salivary carbonic anhydrase
Gene names
Name: CA6
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.

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Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processone-carbon compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbonate dehydratase activity

Traceable author statement. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 308291Carbonic anhydrase 6
PRO_0000004241

Sites

Metal binding1111Zinc; catalytic By similarity
Metal binding1131Zinc; catalytic By similarity
Metal binding1381Zinc; catalytic By similarity

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 224 Potential

Natural variations

Natural variant371Q → L: dbSNP rs34265054.
VAR_033712
Natural variant551T → M: dbSNP rs2274327.
VAR_028268
Natural variant681M → L: dbSNP rs2274328.
VAR_028269
Natural variant701G → A: dbSNP rs2274329.
VAR_028270
Natural variant901S → G: dbSNP rs2274333. Ref.1 Ref.2
VAR_028271

Experimental info

Sequence conflict1031T → I in AAA51892. Ref.1
Sequence conflict1481S → T in AAA51892. Ref.1
Sequence conflict1481S → T in AAF22565. Ref.2
Sequence conflict2701N → K in AAA51892. Ref.1
Sequence conflict2701N → K in AAF22565. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P23280-1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 6EBFF15085E7112D

FASTA30835,367
        10         20         30         40         50         60 
MRALVLLLSL FLLGGQAQHV SDWTYSEGAL DEAHWPQHYP ACGGQRQSPI NLQRTKVRYN 

        70         80         90        100        110        120 
PSLKGLNMTG YETQAGEFPM VNNGHTVQIS LPSTMRMTVA DGTVYIAQQM HFHWGGASSE 

       130        140        150        160        170        180 
ISGSEHTVDG IRHVIEIHIV HYNSKYKSYD IAQDAPDGLA VLAAFVEVKN YPENTYYSNF 

       190        200        210        220        230        240 
ISHLANIKYP GQRTTLTGLD VQDMLPRNLQ HYYTYHGSLT TPPCTENVHW FVLADFVKLS 

       250        260        270        280        290        300 
RTQVWKLENS LLDHRNKTIH NDYRRTQPLN HRVVESNFPN QEYTLGSEFQ FYLHKIEEIL 


DYLRRALN

« Hide

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References

« Hide 'large scale' references
[1]"Human secreted carbonic anhydrase: cDNA cloning, nucleotide sequence, and hybridization histochemistry."
Aldred P., Fu P., Barrett G., Penschow J.D., Wright R., Coghlan J.P., Fernley R.T.
Biochemistry 30:569-575(1991) [PubMed: 1899030] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-90.
[2]Grubb D.J.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-90.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

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Cross-references

Sequence databases

M57892 mRNA. Translation: AAA51892.1.
AF128418 expand/collapse EMBL AC list , AF128411, AF128412, AF128413, AF128414, AF128415, AF128416, AF128417 Genomic DNA. Translation: AAF22565.1.
AL139415 Genomic DNA. Translation: CAC42429.1.
IPIIPI00295105.
PIRCRHU6. A37917.
RefSeqNP_001206.2.
UniGeneHs.100322

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3FE4X-ray1.90A/B21-290[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSG00000131686. Homo sapiens. [Contig view]
GeneID765.
KEGGhsa:765.

Organism-specific databases

GeneCardsGC01P008940.
H-InvDBHIX0020003.
HIX0028508.
HGNCHGNC:1380. CA6.
MIM114780. gene.
PharmGKBPA24381.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP23280.

Enzyme and pathway databases

BRENDA4.2.1.1. 247.

Gene expression databases

ArrayExpressP23280.
BgeeP23280.
CleanExHS_CA6.
GermOnlineENSG00000131686. Homo sapiens.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018428. Carbonic_anhydrase_CA6.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF17. Carbonic_anhydrase_CA6. 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. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3092.
SOURCESearch...

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Entry information

Entry nameCAH6_HUMAN
AccessionPrimary (citable) accession number: P23280
Secondary accession number(s): Q96QX8, Q9UF03
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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