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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

Zn2+1 Publication

Enzyme regulationi

Inhibited by acetazolamide.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei84Proton acceptorBy similarity1
Metal bindingi109Zinc; catalytic1 Publication1
Metal bindingi111Zinc; catalytic1 Publication1
Metal bindingi135Zinc; catalytic1 Publication1
Active sitei144By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • carbon dioxide transport Source: MGI
  • 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.
ReactomeiR-MMU-1475029. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1344341. Car14.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini16 – 290ExtracellularSequence analysisAdd BLAST275
Transmembranei291 – 311HelicalSequence analysisAdd BLAST21
Topological domaini312 – 337CytoplasmicSequence analysisAdd BLAST26

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Sequence analysisAdd BLAST15
ChainiPRO_000000425216 – 337Carbonic anhydrase 14Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 2211 Publication
Glycosylationi213N-linked (GlcNAc...)1 Publication1
Modified residuei325PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9WVT6.
PaxDbiQ9WVT6.
PeptideAtlasiQ9WVT6.
PRIDEiQ9WVT6.

PTM databases

iPTMnetiQ9WVT6.
PhosphoSitePlusiQ9WVT6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000038526.
CleanExiMM_CAR14.
ExpressionAtlasiQ9WVT6. baseline and differential.
GenevisibleiQ9WVT6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036983.

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 26Combined sources3
Turni30 – 32Combined sources3
Helixi33 – 36Combined sources4
Helixi38 – 41Combined sources4
Turni52 – 54Combined sources3
Beta strandi65 – 67Combined sources3
Turni68 – 70Combined sources3
Beta strandi77 – 81Combined sources5
Beta strandi86 – 89Combined sources4
Beta strandi95 – 101Combined sources7
Beta strandi103 – 112Combined sources10
Beta strandi122 – 125Combined sources4
Beta strandi131 – 140Combined sources10
Turni141 – 143Combined sources3
Helixi147 – 150Combined sources4
Beta strandi157 – 166Combined sources10
Helixi172 – 178Combined sources7
Helixi179 – 184Combined sources6
Beta strandi190 – 193Combined sources4
Helixi198 – 201Combined sources4
Beta strandi209 – 214Combined sources6
Beta strandi225 – 232Combined sources8
Beta strandi234 – 236Combined sources3
Helixi238 – 245Combined sources8
Beta strandi249 – 255Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9WVT6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 278Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni217 – 218Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9WVT6.
KOiK01672.
OMAiSYPECGS.
OrthoDBiEOG091G0XFM.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RJ5X-ray2.81A/B18-278[»]
1RJ6X-ray2.90A/B18-278[»]
ProteinModelPortaliQ9WVT6.
SMRiQ9WVT6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036983.

PTM databases

iPTMnetiQ9WVT6.
PhosphoSitePlusiQ9WVT6.

Proteomic databases

MaxQBiQ9WVT6.
PaxDbiQ9WVT6.
PeptideAtlasiQ9WVT6.
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

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9WVT6.
KOiK01672.
OMAiSYPECGS.
OrthoDBiEOG091G0XFM.
PhylomeDBiQ9WVT6.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 3474.
ReactomeiR-MMU-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiQ9WVT6.
PROiQ9WVT6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038526.
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...

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: November 2, 2016
This is version 131 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

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 one 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.