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P23589

- CAH5A_MOUSE

UniProt

P23589 - CAH5A_MOUSE

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Protein

Carbonic anhydrase 5A, mitochondrial

Gene
Ca5a, Ca5, Car5, Car5a
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Zinc.

Enzyme regulationi

Inhibited by acetazolamide By similarity.

pH dependencei

Optimum pH is 7-8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941 Inferred
Metal bindingi124 – 1241Zinc; catalytic
Metal bindingi126 – 1261Zinc; catalytic
Metal bindingi149 – 1491Zinc; catalytic
Active sitei158 – 1581 By similarity
Active sitei161 – 1611 Inferred

GO - Molecular functioni

  1. carbonate dehydratase activity Source: MGI
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. gluconeogenesis Source: MGI
  2. one-carbon metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199096. 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
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:101946. Car5a.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941Y → A: Normal activity. 2 Publications
Mutagenesisi94 – 941Y → H: Normal activity. Enhanced proton transfer due to removal of the steric hindrance of F-95; when associated with A-95. 2 Publications
Mutagenesisi95 – 951F → A: Normal activity. Enhanced proton transfer; when associated with H-94 or C-161. 3 Publications
Mutagenesisi121 – 1211K → C: Normal activity. 1 Publication
Mutagenesisi161 – 1611Y → A: Normal activity. 3 Publications
Mutagenesisi161 – 1611Y → C: Normal activity. Enhanced proton transfer; when associated with A-95. 3 Publications
Mutagenesisi161 – 1611Y → H: Normal activity. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion1 PublicationAdd
BLAST
Chaini30 – 299270Carbonic anhydrase 5A, mitochondrialPRO_0000004235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-succinyllysine1 Publication

Proteomic databases

MaxQBiP23589.
PaxDbiP23589.
PRIDEiP23589.

PTM databases

PhosphoSiteiP23589.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiP23589.
CleanExiMM_CAR5A.
GenevestigatoriP23589.

Interactioni

Protein-protein interaction databases

IntActiP23589. 1 interaction.
MINTiMINT-4089763.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 673
Beta strandi68 – 703
Beta strandi75 – 806
Helixi83 – 853
Beta strandi86 – 916
Beta strandi93 – 1008
Beta strandi104 – 1129
Beta strandi118 – 12710
Beta strandi136 – 1394
Beta strandi145 – 15410
Turni155 – 1573
Helixi161 – 1644
Beta strandi171 – 18212
Helixi185 – 1917
Helixi192 – 1965
Beta strandi203 – 2053
Helixi211 – 2144
Beta strandi221 – 2266
Beta strandi237 – 2448
Beta strandi246 – 2483
Helixi250 – 2567
Beta strandi260 – 2623
Beta strandi264 – 2663
Beta strandi286 – 2905

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMXX-ray2.45A/B53-299[»]
1DMYX-ray2.45A/B53-299[»]
1KEQX-ray1.88A/B53-299[»]
1URTX-ray2.80A52-299[»]
ProteinModelPortaliP23589.
SMRiP23589. Positions 55-290.

Miscellaneous databases

EvolutionaryTraceiP23589.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 2302Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00750000117305.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP23589.
KOiK01672.
OMAiFFQVEFD.
OrthoDBiEOG7WMCK7.
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

MLRRDPRKPL AILRHVGLLC ATGPQRWRFQ HSCAEEHSNC ARHPLWTGPV    50
SSAEGTRQSP INIQWKDSVY DPQLAPLRVS YDAASCRYLW NTGYFFQVEF 100
DDSCEDSGIS GGPLGNHYRL KQFHFHWGAT DEWGSEHAVD GHTYPAELHL 150
VHWNSTKYEN YKKASVGENG LAVIGVFLKL GAHHQALQKL VDVLPEVRHK 200
DTQVAMGPFD PSCLLPACRD YWTYPGSLTT PPLAESVTWI VQKTPVEVSP 250
SQLSTFRTLL FSGRGEEEDV MVNNYRPLQP LRDRKLRSSF RLDRTKMRS 299
Length:299
Mass (Da):34,072
Last modified:November 1, 1995 - v2
Checksum:i2698CABA00686151
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1533VHW → FM in strain: BIO-HTT.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X51971 mRNA. Translation: CAA36233.1 .
BC030174 mRNA. Translation: AAH30174.1 .
CCDSi CCDS22731.1.
PIRi S12579.
RefSeqi NP_031634.2. NM_007608.2.
UniGenei Mm.116761.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DMX X-ray 2.45 A/B 53-299 [» ]
1DMY X-ray 2.45 A/B 53-299 [» ]
1KEQ X-ray 1.88 A/B 53-299 [» ]
1URT X-ray 2.80 A 52-299 [» ]
ProteinModelPortali P23589.
SMRi P23589. Positions 55-290.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P23589. 1 interaction.
MINTi MINT-4089763.

Chemistry

BindingDBi P23589.

PTM databases

PhosphoSitei P23589.

Proteomic databases

MaxQBi P23589.
PaxDbi P23589.
PRIDEi P23589.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000057653 ; ENSMUSP00000060457 ; ENSMUSG00000025317 .
GeneIDi 12352.
KEGGi mmu:12352.
UCSCi uc009nsf.2. mouse.

Organism-specific databases

CTDi 12352.
MGIi MGI:101946. Car5a.

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00750000117305.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P23589.
KOi K01672.
OMAi FFQVEFD.
OrthoDBi EOG7WMCK7.
PhylomeDBi P23589.
TreeFami TF316425.

Enzyme and pathway databases

Reactomei REACT_199096. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTracei P23589.
NextBioi 281008.
PROi P23589.
SOURCEi Search...

Gene expression databases

Bgeei P23589.
CleanExi MM_CAR5A.
Genevestigatori P23589.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and derived amino-acid sequence of a cDNA encoding a new mouse carbonic anhydrase."
    Amor-Gueret M., Levi-Strauss M.
    Nucleic Acids Res. 18:1646-1646(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BIO-HTT.
    Tissue: Liver.
  2. "Mitochondrial carbonic anhydrase (isozyme V) in mouse and rat: cDNA cloning, expression, subcellular localization, processing, and tissue distribution."
    Nagao Y., Srinivasan M., Platero J.S., Svendrowski M., Waheed A., Sly W.S.
    Proc. Natl. Acad. Sci. U.S.A. 91:10330-10334(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-41.
    Tissue: Liver.
  3. "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].
    Strain: FVB/N.
    Tissue: Liver.
  4. "Introduction of histidine analogs leads to enhanced proton transfer in carbonic anhydrase V."
    Earnhardt J.N., Wright S.K., Qian M., Tu C., Laipis P.J., Viola R.E., Silverman D.N.
    Arch. Biochem. Biophys. 361:264-270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-95; LYS-121 AND TYR-161.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design."
    Boriack-Sjodin P.A., Heck R.W., Laipis P.J., Silverman D.N., Christianson D.W.
    Proc. Natl. Acad. Sci. U.S.A. 92:10949-10953(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 55-299 IN COMPLEX WITH INHIBITORS AND ZINC ION, MUTAGENESIS OF TYR-94.
  7. "Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V."
    Heck R.W., Boriack-Sjodin P.A., Qian M., Tu C., Christianson D.W., Laipis P.J., Silverman D.N.
    Biochemistry 35:11605-11611(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 52-299 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF TYR-94; PHE-95 AND TYR-161.
  8. "Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle."
    Jude K.M., Wright S.K., Tu C., Silverman D.N., Viola R.E., Christianson D.W.
    Biochemistry 41:2485-2491(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 55-299 IN COMPLEX WITH INHIBITORS AND ZINC ION, MUTAGENESIS OF PHE-95 AND TYR-161.

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: September 3, 2014
This is version 140 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

External Data

Dasty 3

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