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Protein

Carbonic anhydrase 5A, mitochondrial

Gene

Ca5a

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

Functioni

Reversible hydration of carbon dioxide. Low activity.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+3 Publications

Enzyme regulationi

Inhibited by acetazolamide.By similarity

pH dependencei

Optimum pH is 7-8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei94Curated1
Metal bindingi124Zinc; catalytic3 Publications1
Metal bindingi126Zinc; catalytic3 Publications1
Metal bindingi149Zinc; catalytic3 Publications1
Active sitei158By similarity1
Active sitei161Curated1

GO - Molecular functioni

  • carbonate dehydratase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • gluconeogenesis Source: MGI

Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1475029 Reversible hydration of carbon dioxide

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 5A, mitochondrial (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase VA
Short name:
CA Y
Carbonic anhydrase VA
Short name:
CA-VA
Gene namesi
Name:Ca5a
Synonyms:Ca5, Car5, Car5a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:101946 Car5a

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94Y → A: Normal activity. 2 Publications1
Mutagenesisi94Y → H: Normal activity. Enhanced proton transfer due to removal of the steric hindrance of F-95; when associated with A-95. 2 Publications1
Mutagenesisi95F → A: Normal activity. Enhanced proton transfer; when associated with H-94 or C-161. 3 Publications1
Mutagenesisi121K → C: Normal activity. 1 Publication1
Mutagenesisi161Y → A: Normal activity. 3 Publications1
Mutagenesisi161Y → C: Normal activity. Enhanced proton transfer; when associated with A-95. 3 Publications1
Mutagenesisi161Y → H: Normal activity. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29Mitochondrion1 PublicationAdd BLAST29
ChainiPRO_000000423530 – 299Carbonic anhydrase 5A, mitochondrialAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-succinyllysineCombined sources1

Proteomic databases

MaxQBiP23589
PaxDbiP23589
PeptideAtlasiP23589
PRIDEiP23589

PTM databases

iPTMnetiP23589
PhosphoSitePlusiP23589

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSMUSG00000025317
CleanExiMM_CAR5A
GenevisibleiP23589 MM

Interactioni

Protein-protein interaction databases

IntActiP23589, 1 interactor
MINTiP23589

Chemistry databases

BindingDBiP23589

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi65 – 67Combined sources3
Beta strandi68 – 70Combined sources3
Beta strandi75 – 80Combined sources6
Helixi83 – 85Combined sources3
Beta strandi86 – 91Combined sources6
Beta strandi93 – 100Combined sources8
Beta strandi104 – 112Combined sources9
Beta strandi118 – 127Combined sources10
Beta strandi136 – 139Combined sources4
Beta strandi145 – 154Combined sources10
Turni155 – 157Combined sources3
Helixi161 – 164Combined sources4
Beta strandi171 – 182Combined sources12
Helixi185 – 191Combined sources7
Helixi192 – 196Combined sources5
Beta strandi203 – 205Combined sources3
Helixi211 – 214Combined sources4
Beta strandi221 – 226Combined sources6
Beta strandi237 – 244Combined sources8
Beta strandi246 – 248Combined sources3
Helixi250 – 256Combined sources7
Beta strandi260 – 262Combined sources3
Beta strandi264 – 266Combined sources3
Beta strandi286 – 290Combined sources5

3D structure databases

ProteinModelPortaliP23589
SMRiP23589
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23589

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 290Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST261

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni229 – 230Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0382 Eukaryota
COG3338 LUCA
GeneTreeiENSGT00760000118915
HOGENOMiHOG000112637
HOVERGENiHBG002837
InParanoidiP23589
KOiK01672
OMAiNNFRPPM
OrthoDBiEOG091G0XFM
PhylomeDBiP23589
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
IPR018338 Carbonic_anhydrase_a-class_CS
PANTHERiPTHR18952 PTHR18952, 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
PS00162 ALPHA_CA_1, 1 hit
PS51144 ALPHA_CA_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P23589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRRDPRKPL AILRHVGLLC ATGPQRWRFQ HSCAEEHSNC ARHPLWTGPV
60 70 80 90 100
SSAEGTRQSP INIQWKDSVY DPQLAPLRVS YDAASCRYLW NTGYFFQVEF
110 120 130 140 150
DDSCEDSGIS GGPLGNHYRL KQFHFHWGAT DEWGSEHAVD GHTYPAELHL
160 170 180 190 200
VHWNSTKYEN YKKASVGENG LAVIGVFLKL GAHHQALQKL VDVLPEVRHK
210 220 230 240 250
DTQVAMGPFD PSCLLPACRD YWTYPGSLTT PPLAESVTWI VQKTPVEVSP
260 270 280 290
SQLSTFRTLL FSGRGEEEDV MVNNYRPLQP LRDRKLRSSF RLDRTKMRS
Length:299
Mass (Da):34,072
Last modified:November 1, 1995 - v2
Checksum:i2698CABA00686151
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti151 – 153VHW → FM in strain: BIO-HTT. 3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51971 mRNA Translation: CAA36233.1
BC030174 mRNA Translation: AAH30174.1
CCDSiCCDS22731.1
PIRiS12579
RefSeqiNP_031634.2, NM_007608.2
UniGeneiMm.116761

Genome annotation databases

EnsembliENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317
GeneIDi12352
KEGGimmu:12352
UCSCiuc009nsf.2 mouse

Similar proteinsi

Entry informationi

Entry nameiCAH5A_MOUSE
AccessioniPrimary (citable) accession number: P23589
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1995
Last modified: June 20, 2018
This is version 163 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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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