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Q9WVT6

- CAH14_MOUSE

UniProt

Q9WVT6 - CAH14_MOUSE

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Protein

Carbonic anhydrase 14

Gene

Ca14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Inhibited by acetazolamide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei84 – 841Proton acceptorBy similarity
Metal bindingi109 – 1091Zinc; catalytic
Metal bindingi111 – 1111Zinc; catalytic
Metal bindingi135 – 1351Zinc; catalytic
Active sitei144 – 1441By similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: MGI
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbon dioxide transport Source: MGI
  2. metabolic process Source: GOC
  3. regulation of pH Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2605.
ReactomeiREACT_199096. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 14 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase XIV
Carbonic anhydrase XIV
Short name:
CA-XIV
Gene namesi
Name:Ca14
Synonyms:Car14, Catm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1344341. Car14.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 337322Carbonic anhydrase 14PRO_0000004252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 2211 Publication
Glycosylationi213 – 2131N-linked (GlcNAc...)1 Publication
Modified residuei325 – 3251PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9WVT6.
PaxDbiQ9WVT6.
PRIDEiQ9WVT6.

PTM databases

PhosphoSiteiQ9WVT6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9WVT6.
CleanExiMM_CAR14.
ExpressionAtlasiQ9WVT6. baseline and differential.
GenevestigatoriQ9WVT6.

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 263
Turni30 – 323
Helixi33 – 364
Helixi38 – 414
Turni52 – 543
Beta strandi65 – 673
Turni68 – 703
Beta strandi77 – 815
Beta strandi86 – 894
Beta strandi95 – 1017
Beta strandi103 – 11210
Beta strandi122 – 1254
Beta strandi131 – 14010
Turni141 – 1433
Helixi147 – 1504
Beta strandi157 – 16610
Helixi172 – 1787
Helixi179 – 1846
Beta strandi190 – 1934
Helixi198 – 2014
Beta strandi209 – 2146
Beta strandi225 – 2328
Beta strandi234 – 2363
Helixi238 – 2458
Beta strandi249 – 2557

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJ5X-ray2.81A/B18-278[»]
1RJ6X-ray2.90A/B18-278[»]
ProteinModelPortaliQ9WVT6.
SMRiQ9WVT6. Positions 20-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WVT6.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 290275ExtracellularSequence AnalysisAdd
BLAST
Topological domaini312 – 33726CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei291 – 31121HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni217 – 2182Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9WVT6.
KOiK01672.
OMAiHWPASYP.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ9WVT6.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018431. Carbonic_anhydrase_CA14.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF84. PTHR18952:SF84. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WVT6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLFFALLLKV TWILAADGGH HWTYEGPHGQ DHWPTSYPEC GGDAQSPINI
60 70 80 90 100
QTDSVIFDPD LPAVQPHGYD QLGTEPLDLH NNGHTVQLSL PPTLHLGGLP
110 120 130 140 150
RKYTAAQLHL HWGQRGSLEG SEHQINSEAT AAELHVVHYD SQSYSSLSEA
160 170 180 190 200
AQKPQGLAVL GILIEVGETE NPAYDHILSR LHEIRYKDQK TSVPPFSVRE
210 220 230 240 250
LFPQQLEQFF RYNGSLTTPP CYQSVLWTVF NRRAQISMGQ LEKLQETLSS
260 270 280 290 300
TEEDPSEPLV QNYRVPQPLN QRTIFASFIQ AGPLYTTGEM LGLGVGILAG
310 320 330
CLCLLLAVYF IAQKIRKKRL GNRKSVVFTS ARATTEA
Length:337
Mass (Da):37,505
Last modified:November 1, 1999 - v1
Checksum:i32F02F4DB78AC0C9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB005450 mRNA. Translation: BAA78709.1.
BC046995 mRNA. Translation: AAH46995.1.
CCDSiCCDS17625.1.
RefSeqiNP_035927.1. NM_011797.2.
UniGeneiMm.489647.

Genome annotation databases

EnsembliENSMUST00000036181; ENSMUSP00000036983; ENSMUSG00000038526.
GeneIDi23831.
KEGGimmu:23831.
UCSCiuc008qls.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB005450 mRNA. Translation: BAA78709.1 .
BC046995 mRNA. Translation: AAH46995.1 .
CCDSi CCDS17625.1.
RefSeqi NP_035927.1. NM_011797.2.
UniGenei Mm.489647.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RJ5 X-ray 2.81 A/B 18-278 [» ]
1RJ6 X-ray 2.90 A/B 18-278 [» ]
ProteinModelPortali Q9WVT6.
SMRi Q9WVT6. Positions 20-278.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9WVT6.

Proteomic databases

MaxQBi Q9WVT6.
PaxDbi Q9WVT6.
PRIDEi Q9WVT6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000036181 ; ENSMUSP00000036983 ; ENSMUSG00000038526 .
GeneIDi 23831.
KEGGi mmu:23831.
UCSCi uc008qls.1. mouse.

Organism-specific databases

CTDi 23831.
MGIi MGI:1344341. Car14.

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00760000118915.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi Q9WVT6.
KOi K01672.
OMAi HWPASYP.
OrthoDBi EOG7WMCK7.
PhylomeDBi Q9WVT6.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 2605.
Reactomei REACT_199096. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTracei Q9WVT6.
NextBioi 303497.
PROi Q9WVT6.
SOURCEi Search...

Gene expression databases

Bgeei Q9WVT6.
CleanExi MM_CAR14.
ExpressionAtlasi Q9WVT6. baseline and differential.
Genevestigatori Q9WVT6.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018431. Carbonic_anhydrase_CA14.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF84. PTHR18952:SF84. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCAH14_MOUSE
AccessioniPrimary (citable) accession number: Q9WVT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3