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Q9WVT6 (CAH14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 14

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase XIV
Carbonic anhydrase XIV
Short name=CA-XIV
Gene names
Name:Ca14
Synonyms:Car14, Catm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length337 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.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Inhibited by acetazolamide. Ref.3

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Most abundant in the kidney and heart, followed by the skeletal muscle, brain, lung and liver.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 337322Carbonic anhydrase 14
PRO_0000004252

Regions

Topological domain16 – 290275Extracellular Potential
Transmembrane291 – 31121Helical; Potential
Topological domain312 – 33726Cytoplasmic Potential
Region217 – 2182Substrate binding By similarity

Sites

Active site841Proton acceptor By similarity
Active site1441 By similarity
Metal binding1091Zinc; catalytic
Metal binding1111Zinc; catalytic
Metal binding1351Zinc; catalytic

Amino acid modifications

Modified residue3251Phosphoserine By similarity
Glycosylation2131N-linked (GlcNAc...) Ref.3
Disulfide bond40 ↔ 221 Ref.3

Secondary structure

............................................... 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WVT6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 32F02F4DB78AC0C9

FASTA33737,505
        10         20         30         40         50         60 
MLFFALLLKV TWILAADGGH HWTYEGPHGQ DHWPTSYPEC GGDAQSPINI QTDSVIFDPD 

        70         80         90        100        110        120 
LPAVQPHGYD QLGTEPLDLH NNGHTVQLSL PPTLHLGGLP RKYTAAQLHL HWGQRGSLEG 

       130        140        150        160        170        180 
SEHQINSEAT AAELHVVHYD SQSYSSLSEA AQKPQGLAVL GILIEVGETE NPAYDHILSR 

       190        200        210        220        230        240 
LHEIRYKDQK TSVPPFSVRE LFPQQLEQFF RYNGSLTTPP CYQSVLWTVF NRRAQISMGQ 

       250        260        270        280        290        300 
LEKLQETLSS TEEDPSEPLV QNYRVPQPLN QRTIFASFIQ AGPLYTTGEM LGLGVGILAG 

       310        320        330 
CLCLLLAVYF IAQKIRKKRL GNRKSVVFTS ARATTEA 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of CA XIV, a novel membrane-bound carbonic anhydrase from mouse kidney."
Mori K., Ogawa Y., Ebihara K., Tamura N., Tashiro K., Kuwahara T., Mukoyama M., Sugawara A., Ozaki S., Tanaka I., Nakao K.
J. Biol. Chem. 274:15701-15705(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Retina.
[3]"Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes."
Whittington D.A., Grubb J.H., Waheed A., Shah G.N., Sly W.S., Christianson D.W.
J. Biol. Chem. 279:7223-7228(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 18-278 ALONE AND IN COMPLEX WITH ACETAZOLAMIDE, DISULFIDE BOND, ZINC-BINDING SITES, ENZYME REGULATION, GLYCOSYLATION AT ASN-213.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005450 mRNA. Translation: BAA78709.1.
BC046995 mRNA. Translation: AAH46995.1.
RefSeqNP_035927.1. NM_011797.2.
UniGeneMm.489647.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJ5X-ray2.81A/B18-278[»]
1RJ6X-ray2.90A/B18-278[»]
ProteinModelPortalQ9WVT6.
SMRQ9WVT6. Positions 20-278.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00819. Acetazolamide.

PTM databases

PhosphoSiteQ9WVT6.

Proteomic databases

PaxDbQ9WVT6.
PRIDEQ9WVT6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036181; ENSMUSP00000036983; ENSMUSG00000038526.
GeneID23831.
KEGGmmu:23831.
UCSCuc008qls.1. mouse.

Organism-specific databases

CTD23831.
MGIMGI:1344341. Car14.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00660000095420.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidQ9WVT6.
KOK01672.
OMAGPHGQDH.
OrthoDBEOG7WMCK7.
PhylomeDBQ9WVT6.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 2605.

Gene expression databases

ArrayExpressQ9WVT6.
BgeeQ9WVT6.
CleanExMM_CAR14.
GenevestigatorQ9WVT6.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018429. CA9/14.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WVT6.
NextBio303497.
PROQ9WVT6.
SOURCESearch...

Entry information

Entry nameCAH14_MOUSE
AccessionPrimary (citable) accession number: Q9WVT6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 113 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot