Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbonic anhydrase 12

Gene

Ca12

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
Active sitei94Proton acceptorBy similarity1
Metal bindingi120Zinc; catalyticBy similarity1
Metal bindingi122Zinc; catalyticBy similarity1
Metal bindingi146Zinc; catalyticBy similarity1
Active sitei155By similarity1

GO - Molecular functioni

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

GO - Biological processi

  • carbon dioxide transport Source: MGI
  • chloride ion homeostasis Source: MGI
  • one-carbon metabolic process Source: InterPro
  • regulation of pH Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 12 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase XII
Carbonic anhydrase XII
Short name:
CA-XII
Gene namesi
Name:Ca12
Synonyms:Car12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1923709. Car12.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 301ExtracellularSequence analysisAdd BLAST277
Transmembranei302 – 322HelicalSequence analysisAdd BLAST21
Topological domaini323 – 354CytoplasmicSequence analysisAdd BLAST32

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000000424925 – 354Carbonic anhydrase 12Add BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi28N-linked (GlcNAc...)Sequence analysis1
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi50 ↔ 231By similarity
Glycosylationi80N-linked (GlcNAc...)Sequence analysis1
Glycosylationi88N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8CI85.
PaxDbiQ8CI85.
PRIDEiQ8CI85.

PTM databases

iPTMnetiQ8CI85.
PhosphoSitePlusiQ8CI85.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032373.
CleanExiMM_CAR12.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8CI85. 2 interactors.
MINTiMINT-4089721.
STRINGi10090.ENSMUSP00000071786.

Structurei

3D structure databases

ProteinModelPortaliQ8CI85.
SMRiQ8CI85.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni227 – 228Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ8CI85.
KOiK01672.
PhylomeDBiQ8CI85.
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.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF19. PTHR18952:SF19. 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.

Q8CI85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHRSLRATV VLLLVILKKQ PSSSAPLNGS KWTYVGPAGE KNWSKKYPSC
60 70 80 90 100
GGLLQSPIDL HSDILQYDAS LAPLQFQGYN VSVEKLLNLT NDGHSVRLNL
110 120 130 140 150
NSDMYIQGLQ PHHYRAEQLH LHWGNRNDPH GSEHTVSGKH FAAELHIVHY
160 170 180 190 200
NSDLYPDFST ASDKSEGLAV LAVLIEIGSA NPSYDKIFSH LQHVKYKGQQ
210 220 230 240 250
VLIPGFNIEE LLPESPGEYY RYEGSLTTPP CYPTVLWTVF RNPVQISQEQ
260 270 280 290 300
LLALETALYF THMDDPTPRE MINNFRQVQK FDERLVYISF RQGLLTDTGL
310 320 330 340 350
SLGIILSVAL AGVLGISIVL AVSIWLFKRK KSKKGDNKGV IYKPAIKKEA

EVHA
Length:354
Mass (Da):39,695
Last modified:March 1, 2003 - v1
Checksum:i98ED581BF2A16111
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti297D → N in BAC35074 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052639 mRNA. Translation: BAC35074.1.
BC035941 mRNA. Translation: AAH35941.1.
CCDSiCCDS23306.1.
RefSeqiNP_001293077.1. NM_001306148.1.
NP_848483.3. NM_178396.5.
UniGeneiMm.277921.

Genome annotation databases

GeneIDi76459.
KEGGimmu:76459.
UCSCiuc009qfc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052639 mRNA. Translation: BAC35074.1.
BC035941 mRNA. Translation: AAH35941.1.
CCDSiCCDS23306.1.
RefSeqiNP_001293077.1. NM_001306148.1.
NP_848483.3. NM_178396.5.
UniGeneiMm.277921.

3D structure databases

ProteinModelPortaliQ8CI85.
SMRiQ8CI85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CI85. 2 interactors.
MINTiMINT-4089721.
STRINGi10090.ENSMUSP00000071786.

PTM databases

iPTMnetiQ8CI85.
PhosphoSitePlusiQ8CI85.

Proteomic databases

MaxQBiQ8CI85.
PaxDbiQ8CI85.
PRIDEiQ8CI85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi76459.
KEGGimmu:76459.
UCSCiuc009qfc.2. mouse.

Organism-specific databases

CTDi76459.
MGIiMGI:1923709. Car12.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ8CI85.
KOiK01672.
PhylomeDBiQ8CI85.
TreeFamiTF316425.

Miscellaneous databases

PROiQ8CI85.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032373.
CleanExiMM_CAR12.

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.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF19. PTHR18952:SF19. 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 nameiCAH12_MOUSE
AccessioniPrimary (citable) accession number: Q8CI85
Secondary accession number(s): Q8BKG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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.