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Protein

Carbonic anhydrase 5A, mitochondrial

Gene

Ca5a

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. 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
  • one-carbon metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:101946. Car5a.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

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.
MINTiMINT-4089763.
STRINGi10090.ENSMUSP00000060457.

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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DMXX-ray2.45A/B53-299[»]
1DMYX-ray2.45A/B53-299[»]
1KEQX-ray1.88A/B53-299[»]
1URTX-ray2.80A52-299[»]
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
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP23589.
KOiK01672.
OMAiPFQPSCL.
OrthoDBiEOG091G0XFM.
PhylomeDBiP23589.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DMXX-ray2.45A/B53-299[»]
1DMYX-ray2.45A/B53-299[»]
1KEQX-ray1.88A/B53-299[»]
1URTX-ray2.80A52-299[»]
ProteinModelPortaliP23589.
SMRiP23589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP23589. 1 interactor.
MINTiMINT-4089763.
STRINGi10090.ENSMUSP00000060457.

Chemistry databases

BindingDBiP23589.

PTM databases

iPTMnetiP23589.
PhosphoSitePlusiP23589.

Proteomic databases

MaxQBiP23589.
PaxDbiP23589.
PeptideAtlasiP23589.
PRIDEiP23589.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi12352.
MGIiMGI:101946. Car5a.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP23589.
KOiK01672.
OMAiPFQPSCL.
OrthoDBiEOG091G0XFM.
PhylomeDBiP23589.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiR-MMU-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiP23589.
PROiP23589.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025317.
CleanExiMM_CAR5A.
GenevisibleiP23589. MM.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAH5A_MOUSE
AccessioniPrimary (citable) accession number: P23589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 154 of the entry and version 2 of the sequence. [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

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.