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Protein

Carbonic anhydrase 3

Gene

Ca3

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+By similarity

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi94Zinc; catalyticBy similarity1
Metal bindingi96Zinc; catalyticBy similarity1
Metal bindingi119Zinc; catalyticBy similarity1
Active sitei127By similarity1

GO - Molecular functioni

GO - Biological processi

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 3 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase III
Carbonic anhydrase III
Short name:
CA-III
Gene namesi
Name:Ca3
Synonyms:Car3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88270. Car3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000774272 – 260Carbonic anhydrase 3Add BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei29PhosphoserineBy similarity1
Modified residuei43PhosphoserineBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei55PhosphoserineBy similarity1
Modified residuei73PhosphothreonineBy similarity1
Modified residuei127PhosphotyrosineBy similarity1
Modified residuei129PhosphothreonineBy similarity1
Modified residuei176PhosphothreonineCombined sources1
Modified residuei182S-glutathionyl cysteineBy similarity1
Modified residuei187S-glutathionyl cysteineBy similarity1
Modified residuei216PhosphothreonineBy similarity1
Modified residuei219PhosphoserineBy similarity1

Post-translational modificationi

S-glutathionylated in hepatocytes under oxidative stress.By similarity

Keywords - PTMi

Acetylation, Glutathionylation, Phosphoprotein

Proteomic databases

MaxQBiP16015.
PaxDbiP16015.
PeptideAtlasiP16015.
PRIDEiP16015.

2D gel databases

SWISS-2DPAGEiP16015.

PTM databases

iPTMnetiP16015.
PhosphoSitePlusiP16015.

Expressioni

Tissue specificityi

Expressed at lower levels in adipose tissue from animals that were either genetically obese or had experimentally induced obesity.1 Publication

Gene expression databases

BgeeiENSMUSG00000027559.
CleanExiMM_CAR3.
GenevisibleiP16015. MM.

Interactioni

Protein-protein interaction databases

BioGridi198484. 2 interactors.
IntActiP16015. 4 interactors.
MINTiMINT-1869657.
STRINGi10090.ENSMUSP00000029076.

Structurei

3D structure databases

ProteinModelPortaliP16015.
SMRiP16015.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 259Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 67Involved in proton transferBy similarity4
Regioni198 – 199Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP16015.
KOiK01672.
OMAiRDYWTYQ.
OrthoDBiEOG091G0XFM.
PhylomeDBiP16015.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiView protein in InterPro
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018441. Carbonic_anhydrase_CA3.
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF154. PTHR18952:SF154. 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.

P16015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEWGYASH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLQPWSAS
60 70 80 90 100
YDPGSAKTIL NNGKTCRVVF DDTYDRSMLR GGPLSGPYRL RQFHLHWGSS
110 120 130 140 150
DDHGSEHTVD GVKYAAELHL VHWNPKYNTF GEALKQPDGI AVVGIFLKIG
160 170 180 190 200
REKGEFQILL DALDKIKTKG KEAPFTHFDP SCLFPACRDY WTYHGSFTTP
210 220 230 240 250
PCEECIVWLL LKEPMTVSSD QMAKLRSLFS SAENEPPVPL VGNWRPPQPV
260
KGRVVRASFK
Length:260
Mass (Da):29,366
Last modified:January 23, 2007 - v3
Checksum:iF4E9FE69A3C324BB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9S → R in AAA37355 (PubMed:2496681).Curated1
Sequence conflicti86G → R in AAA37355 (PubMed:2496681).Curated1
Sequence conflicti126K → R in AAA37355 (PubMed:2496681).Curated1
Sequence conflicti146F → L in AAA37355 (PubMed:2496681).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27796 mRNA. Translation: AAA37355.1.
AF294988
, AF294983, AF294984, AF294985, AF294986, AF294987 Genomic DNA. Translation: AAG22029.1.
BC011129 mRNA. Translation: AAH11129.1.
CCDSiCCDS17250.1.
PIRiA43641.
RefSeqiNP_031632.2. NM_007606.3.
UniGeneiMm.300.

Genome annotation databases

EnsembliENSMUST00000029076; ENSMUSP00000029076; ENSMUSG00000027559.
GeneIDi12350.
KEGGimmu:12350.
UCSCiuc008oqs.1. mouse.

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.

Entry informationi

Entry nameiCAH3_MOUSE
AccessioniPrimary (citable) accession number: P16015
Secondary accession number(s): Q9ERN8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 139 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families