[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION. TISSUE=Renal cell carcinoma; DOI=10.1073/pnas.95.13.7608; PubMed=9636197 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers."; Proc. Natl. Acad. Sci. U.S.A. 95:7608-7613(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Lung; DOI=10.1073/pnas.95.21.12596; PubMed=9770531 [NCBI, ExPASy, EBI, Israel, Japan] Ivanov S.V., Kuzmin I., Wei M.-H., Pack S., Geil L., Johnson B.E., Stanbridge E.J., Lerman M.I.; "Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes."; Proc. Natl. Acad. Sci. U.S.A. 95:12596-12601(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). TISSUE=Eye, and Kidney; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 30-292. DOI=10.1073/pnas.161301298; PubMed=11493685 [NCBI, ExPASy, EBI, Israel, Japan] Whittington D.A., Waheed A., Ulmasov B., Shah G.N., Grubb J.H., Sly W.S., Christianson D.W.; "Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells."; Proc. Natl. Acad. Sci. U.S.A. 98:9545-9550(2001).

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.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	O43570-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	O43570-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_000772.

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.
SIMILARITY: Belongs to the alpha-carbonic anhydrase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF051882; AAC39789.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF037335; AAC63952.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006656; AAP35302.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000278; AAH00278.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011691; AAH11691.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023981; AAH23981.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001209.1; -.
NP_996808.1; -.

UniGene

Hs.210995

3D structure databases

PDB

1JCZ; X-ray; 1.55 A; A/B=30-291.	[ExPASy / RCSB / EBI]
1JD0; X-ray; 1.50 A; A/B=30-291.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JCZ; -.
1JD0; -.

ModBase

O43570.

Protein-protein interaction databases

IntAct

O43570; 7.

PTM databases

PhosphoSite

O43570; -.

Organism-specific databases

GC15M061402; -.

HIX0012325; -.

HGNC:1371; CA12.

HPA008773; -.

603263; gene. [NCBI / EBI]

PharmGKB

PA24376; -.

GeneCards

O43570.

Gene expression databases

ArrayExpress

O43570; -.

CleanEx

HS_CA12; -.

GermOnline

ENSG00000074410; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0016021;	Cellular component: integral to membrane (traceable author statement from ProtInc).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from HPA).
GO:0004089;	Molecular function: carbonate dehydratase activity (traceable author statement from ProtInc).
GO:0008270;	Molecular function: zinc ion binding (traceable author statement from ProtInc).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001148; Euk_COanhd.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.200.10; Euk_COanhd; 1.

PANTHER

PTHR18952; Euk_COanhd; 1.

Pfam

PF00194; Carb_anhydrase; 1.
Pfam graphical view of domain structure.

ProDom

PD000865; Euk_COanhd; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00162; ALPHA_CA_1; 1.
PS51144; ALPHA_CA_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

O43570; -.

Genome annotation databases

Ensembl

ENSG00000074410; Homo sapiens. [Contig view]

GeneID

771; -.

KEGG

hsa:771; -.

Phylogenomic databases

HOGENOM

O43570; -.

HOVERGEN

O43570; -.

Other

DrugBank

DB00819; Acetazolamide.

3114; -.

CA12; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Glycoprotein; Lyase; Membrane; Metal-binding; Signal; Transmembrane; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`CHAIN`	`25 354`	`330`	`Carbonic anhydrase 12.`	`PRO_0000004248`
`TOPO_DOM`	`25 301`	`277`	`Extracellular (Potential).`
`TRANSMEM`	`302 322`	`21`	`Potential.`
`TOPO_DOM`	`323 354`	`32`	`Cytoplasmic (Potential).`
`METAL`	`119 119`		`Zinc; catalytic.`
`METAL`	`121 121`		`Zinc; catalytic.`
`METAL`	`145 145`		`Zinc; catalytic.`
`CARBOHYD`	`28 28`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`80 80`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`162 162`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`50 230`
`VAR_SEQ`	`292 302`		`Missing (in isoform 2).`	`VSP_000772`
`STRAND`	`34 36`	`3`
`HELIX`	`40 42`	`3`
`HELIX`	`43 46`	`4`
`HELIX`	`48 51`	`4`
`STRAND`	`52 54`	`3`
`HELIX`	`62 64`	`3`
`STRAND`	`65 67`	`3`
`STRAND`	`75 78`	`4`
`STRAND`	`85 91`	`7`
`STRAND`	`93 99`	`7`
`STRAND`	`104 111`	`8`
`STRAND`	`113 122`	`10`
`STRAND`	`132 135`	`4`
`STRAND`	`141 150`	`10`
`TURN`	`151 153`	`3`
`HELIX`	`157 160`	`4`
`STRAND`	`167 176`	`10`
`TURN`	`181 183`	`3`
`HELIX`	`184 187`	`4`
`HELIX`	`188 192`	`5`
`STRAND`	`199 203`	`5`
`HELIX`	`207 210`	`4`
`STRAND`	`218 223`	`6`
`STRAND`	`234 241`	`8`
`STRAND`	`243 245`	`3`
`HELIX`	`247 255`	`9`
`STRAND`	`258 260`	`3`
`STRAND`	`285 288`	`4`

Sequence information

Length: 354 AA [This is the length of the unprocessed precursor]

Molecular weight: 39451 Da [This is the MW of the unprocessed precursor]

CRC64: 9016216BF2CA6C0C [This is a checksum on the sequence]

        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

O43570 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools