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Reviewed, UniProtKB/Swiss-Prot Q9MZ30 (CAH12_RABIT)

Last modified October 13, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 12
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase XII
      Short name=CA-XII
    Carbonate dehydratase XII
Gene names
Name: CA12
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Reversible hydration of carbon dioxide By similarity.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 355331Carbonic anhydrase 12
PRO_0000004250

Regions

Topological domain25 – 303279Extracellular Potential
Transmembrane304 – 32421 Potential
Topological domain325 – 35531Cytoplasmic Potential

Sites

Metal binding1191Zinc; catalytic By similarity
Metal binding1211Zinc; catalytic By similarity
Metal binding1451Zinc; catalytic By similarity

Amino acid modifications

Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 230 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9MZ30-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 5B468580EBA437D5

FASTA35539,591
        10         20         30         40         50         60 
MPVGSLRAAA VLLLGIAQLP PSSAAPRNGS KWTYVGADGE RSWFKKYPSC GGRLQSPIDL 

        70         80         90        100        110        120 
HGDTLQYDAS LTPLEFQGYN VSADKQFNLT NDGHSVRLNL PPDMYLQGLP SRYTATQLHL 

       130        140        150        160        170        180 
HWGNRNDPYG SEHTVGGKQF AAELHIVHYN SDSYPDISTA SNKSEGLAVL AVLIEKGYFN 

       190        200        210        220        230        240 
PYYDRIFSFL RYVKYKGQNV RIPTFNIEEL LPEKPAEYYR YRGSLTTPPC YPSVLWTVFR 

       250        260        270        280        290        300 
NPVTISQEQL LALQTALYFT RADDPAPREM INNFRPIQNF GVRLVHASFQ EVQILPGTGL 

       310        320        330        340        350 
SVGIILSVAL AGVLGICIVL AVCIWFFRRK KGSKKGDNKG VIYNPAIKME TEAHA

« Hide

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References

[1]"Carbonic anhydrase XII mRNA encodes a hydratase that is differentially expressed along the rabbit nephron."
Schwartz G.J., Kittelberger A.M., Watkins R.H., O'Reilly M.A.
Am. J. Physiol. 284:F399-F410(2003) [PubMed: 12388401] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney cortex.

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Cross-references

Sequence databases

AF263367 mRNA. Translation: AAF91392.2.
RefSeqNP_001075555.1.
UniGeneOcu.3061

3D structure databases

HSSPHSSP built from PDB template 1JD0 based on UniProtKB O43570.
SMRQ9MZ30. Positions 31-289.
ModBaseSearch...

Genome annotation databases

GeneID100008777.

Organism-specific databases

CTD100008777.

Phylogenomic databases

HOVERGENQ9MZ30.

Enzyme and pathway databases

BRENDA4.2.1.1. 255.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF19. Carbonic_anhydrase_CA12. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCAH12_RABIT
AccessionPrimary (citable) accession number: Q9MZ30
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 6, 2002
Last modified: October 13, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents