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Reviewed, UniProtKB/Swiss-Prot O43570 (CAH12_HUMAN)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · 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
    HOM-RCC-3.1.3 tumor antigen
Gene names
Name: CA12
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Enzyme regulation

Inhibited by acetazolamide.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Highly expressed in colon, kidney, prostate, intestine and activated lymphocytes. Expressed at much higher levels in the renal cell cancers than in surrounding normal kidney tissue. Moderately expressed in pancreas, ovary and testis.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processone-carbon compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

integral to membrane Ref.1

Traceable author statement. Source: ProtInc

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular functioncarbonate dehydratase activity Ref.1

Traceable author statement. Source: ProtInc

zinc ion binding Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43570-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43570-2)

The sequence of this isoform differs from the canonical sequence as follows:
     292-302: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 354330Carbonic anhydrase 12
PRO_0000004248

Regions

Topological domain25 – 301277Extracellular Potential
Transmembrane302 – 32221 Potential
Topological domain323 – 35432Cytoplasmic Potential

Sites

Metal binding1191Zinc; catalytic
Metal binding1211Zinc; catalytic
Metal binding1451Zinc; catalytic

Amino acid modifications

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

Natural variations

Alternative sequence292 – 30211Missing in isoform 2.
VSP_000772

Secondary structure

1 ................................................... 354
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 9016216BF2CA6C0C

FASTA35439,451
        10         20         30         40         50         60 
MPRRSLHAAA VLLLVILKEQ PSSPAPVNGS KWTYFGPDGE NSWSKKYPSC GGLLQSPIDL 

        70         80         90        100        110        120 
HSDILQYDAS LTPLEFQGYN LSANKQFLLT NNGHSVKLNL PSDMHIQGLQ SRYSATQLHL 

       130        140        150        160        170        180 
HWGNPNDPHG SEHTVSGQHF AAELHIVHYN SDLYPDASTA SNKSEGLAVL AVLIEMGSFN 

       190        200        210        220        230        240 
PSYDKIFSHL QHVKYKGQEA FVPGFNIEEL LPERTAEYYR YRGSLTTPPC NPTVLWTVFR 

       250        260        270        280        290        300 
NPVQISQEQL LALETALYCT HMDDPSPREM INNFRQVQKF DERLVYTSFS QVQVCTAAGL 

       310        320        330        340        350 
SLGIILSLAL AGILGICIVV VVSIWLFRRK SIKKGDNKGV IYKPATKMET EAHA

« Hide

Isoform 2.

Checksum: 87FD35255B137D18
Show »

FASTA34338,408

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References

« Hide 'large scale' references
[1]"Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers."
Tuereci O., Sahin U., Vollmar E., Siemer S., Goettert E., Seitz G., Parkkila A.-K., Shah G.N., Grubb J.H., Pfreundschuh M., Sly W.S.
Proc. Natl. Acad. Sci. U.S.A. 95:7608-7613(1998) [PubMed: 9636197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
Tissue: Renal cell carcinoma.
[2]"Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes."
Ivanov S.V., Kuzmin I., Wei M.-H., Pack S., Geil L., Johnson B.E., Stanbridge E.J., Lerman M.I.
Proc. Natl. Acad. Sci. U.S.A. 95:12596-12601(1998) [PubMed: 9770531] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Eye and Kidney.
[5]"Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells."
Whittington D.A., Waheed A., Ulmasov B., Shah G.N., Grubb J.H., Sly W.S., Christianson D.W.
Proc. Natl. Acad. Sci. U.S.A. 98:9545-9550(2001) [PubMed: 11493685] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 30-292.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF051882 mRNA. Translation: AAC39789.1.
AF037335 mRNA. Translation: AAC63952.1.
BT006656 mRNA. Translation: AAP35302.1.
BC000278 mRNA. Translation: AAH00278.1.
BC011691 mRNA. Translation: AAH11691.1.
BC023981 mRNA. Translation: AAH23981.1.
IPIIPI00012895.
IPI00221392.
RefSeqNP_001209.1.
NP_996808.1.
UniGeneHs.210995

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JCZX-ray1.55A/B30-291[»]
1JD0X-ray1.50A/B30-291[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO43570. 7 interactions.

PTM databases

PhosphoSiteO43570.

Proteomic databases

PRIDEO43570.

Genome annotation databases

EnsemblENSG00000074410. Homo sapiens. [Contig view]
GeneID771.
KEGGhsa:771.

Organism-specific databases

GeneCardsGC15M061402.
H-InvDBHIX0012325.
HGNCHGNC:1371. CA12.
HPAHPA008773.
MIM603263. gene.
PharmGKBPA24376.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO43570.
HOVERGENO43570.
OMAO43570. AEYYRYR.

Enzyme and pathway databases

BRENDA4.2.1.1. 247.

Gene expression databases

ArrayExpressO43570.
BgeeO43570.
CleanExHS_CA12.
GermOnlineENSG00000074410. Homo sapiens.

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...

Other Resources

DrugBankDB00819. Acetazolamide.
NextBio3114.
SOURCESearch...

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Entry information

Entry nameCAH12_HUMAN
AccessionPrimary (citable) accession number: O43570
Secondary accession number(s): Q53YE5, Q9BWG2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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