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Protein

Carbonic anhydrase 14

Gene

Ca14

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

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

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

  • carbonate dehydratase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • carbon dioxide transport Source: MGI
  • metabolic process Source: GOC
  • 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. 3474.
ReactomeiREACT_327358. 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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1344341. Car14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 290275ExtracellularSequence AnalysisAdd
BLAST
Transmembranei291 – 31121HelicalSequence AnalysisAdd
BLAST
Topological domaini312 – 33726CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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.
GenevisibleiQ9WVT6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036983.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
OMAiSYPECGS.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB005450 mRNA. Translation: BAA78709.1.
BC046995 mRNA. Translation: AAH46995.1.
CCDSiCCDS17625.1.
RefSeqiNP_035927.1. NM_011797.2.
UniGeneiMm.489647.

3D structure databases

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036983.

PTM databases

PhosphoSiteiQ9WVT6.

Proteomic databases

MaxQBiQ9WVT6.
PaxDbiQ9WVT6.
PRIDEiQ9WVT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23831.
MGIiMGI:1344341. Car14.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi4.2.1.1. 3474.
ReactomeiREACT_327358. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiQ9WVT6.
NextBioi303497.
PROiQ9WVT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVT6.
CleanExiMM_CAR14.
ExpressionAtlasiQ9WVT6. baseline and differential.
GenevisibleiQ9WVT6. MM.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.