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Protein

Carbonic anhydrase 14

Gene

Ca14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
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

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...) asparagine1 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

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

Gene3Di3.10.200.10, 1 hit
InterProiView protein in InterPro
IPR001148 CA_dom
IPR036398 CA_dom_sf
IPR023561 Carbonic_anhydrase_a-class
IPR018431 Carbonic_anhydrase_CA14
PANTHERiPTHR18952 PTHR18952, 1 hit
PTHR18952:SF84 PTHR18952:SF84, 1 hit
PfamiView protein in Pfam
PF00194 Carb_anhydrase, 1 hit
SMARTiView protein in SMART
SM01057 Carb_anhydrase, 1 hit
SUPFAMiSSF51069 SSF51069, 1 hit
PROSITEiView protein in PROSITE
PS51144 ALPHA_CA_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCAH14_MOUSE
AccessioniPrimary (citable) accession number: Q9WVT6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: May 23, 2018
This is version 138 of the entry and version 1 of the sequence. See 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

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