CA12

Functionⁱ

Reversible hydration of carbon dioxide.

Catalytic activityⁱ

H₂CO₃ = CO₂ + H₂O.

Cofactorⁱ

Zn²⁺1 Publication

Activity regulationⁱ

Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA), benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide) and Foscarnet (phosphonoformate trisodium salt).6 Publications

Kineticsⁱ

K_M=
12.0 mM for CO₂
1 Publication
Manual assertion based on experiment inⁱ
- Ref.11
  "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
  Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
  Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	94	Proton acceptorBy similarity	1
Metal bindingⁱ	119	Zinc; catalytic1 Publication	1
Metal bindingⁱ	121	Zinc; catalytic1 Publication	1
Metal bindingⁱ	145	Zinc; catalytic1 Publication	1
Active siteⁱ	154	By similarity	1

GO - Molecular functionⁱ

carbonate dehydratase activity Source: Reactome
zinc ion binding
Source: ProtInc
Traceable author statementⁱ
- 9636197

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

bicarbonate transport Source: Reactome
chloride ion homeostasis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21035102

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	4.2.1.1 2681
Reactomeⁱ	R-HSA-1475029 Reversible hydration of carbon dioxide

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 Tumor antigen HOM-RCC-3.1.3
Gene namesⁱ	Name:CA12
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000074410.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1371 CA12
MIMⁱ	603263 gene
neXtProtⁱ	NX_O43570

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	25 – 301	ExtracellularSequence analysisAdd BLAST	277
Transmembraneⁱ	302 – 322	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	323 – 354	CytoplasmicSequence analysisAdd BLAST	32

Keywords - Cellular componentⁱ

Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Hyperchlorhidrosis, isolated (HCHLH)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by excessive sweating and increased sweat chloride levels. Affected individuals suffer from episodes of hyponatremic dehydration and report increased amounts of visible salt precipitates in sweat.

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	771
MalaCards human disease database More...MalaCardsⁱ	CA12
MIMⁱ	143860 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000074410
PharmGKBⁱ	PA25987

Chemistry databases

ChEMBLⁱ	CHEMBL3242
Drug and drug target database More...DrugBankⁱ	DB00562 Benzthiazide DB08846 Ellagic Acid DB00999 Hydrochlorothiazide DB00774 Hydroflumethiazide DB00909 Zonisamide
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2747

Polymorphism and mutation databases

BioMutaⁱ	CA12

BioMutaⁱ

CA12

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 24	Sequence analysisAdd BLAST		24
ChainⁱPRO_0000004248	25 – 354	Carbonic anhydrase 12Add BLAST		330

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	28	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	50 ↔ 230	1 Publication
Glycosylationⁱ	80	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	162	N-linked (GlcNAc...) asparagineSequence analysis	1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

EPDⁱ	O43570
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O43570
PaxDbⁱ	O43570
PeptideAtlas More...PeptideAtlasⁱ	O43570
PRIDEⁱ	O43570
ProteomicsDBⁱ	49059 49060 [O43570-2]

PTM databases

GlyConnectⁱ	1064
iPTMnetⁱ	O43570
PhosphoSitePlusⁱ	O43570

Expressionⁱ

Tissue specificityⁱ

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.

Gene expression databases

Bgeeⁱ	ENSG00000074410 Expressed in 204 organ(s), highest expression level in cortex of kidney
CleanExⁱ	HS_CA12
ExpressionAtlasⁱ	O43570 baseline and differential
Genevisibleⁱ	O43570 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB025181 CAB062549 CAB068179 HPA008773 HPA073203

HPAⁱ

CAB025181
CAB062549
CAB068179
HPA008773
HPA073203

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Protein-protein interaction databases

BioGridⁱ	107225, 8 interactors
IntActⁱ	O43570, 10 interactors
Molecular INTeraction database More...MINTⁱ	O43570
STRINGⁱ	9606.ENSP00000178638

Chemistry databases

BindingDBⁱ

O43570

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	36 – 38	Combined sources	3
Helixⁱ	40 – 45	Combined sources	6
Helixⁱ	48 – 51	Combined sources	4
Beta strandⁱ	52 – 54	Combined sources	3
Helixⁱ	62 – 64	Combined sources	3
Beta strandⁱ	65 – 67	Combined sources	3
Beta strandⁱ	75 – 78	Combined sources	4
Beta strandⁱ	85 – 91	Combined sources	7
Beta strandⁱ	93 – 99	Combined sources	7
Beta strandⁱ	105 – 111	Combined sources	7
Beta strandⁱ	113 – 122	Combined sources	10
Beta strandⁱ	132 – 135	Combined sources	4
Beta strandⁱ	141 – 150	Combined sources	10
Turnⁱ	151 – 153	Combined sources	3
Helixⁱ	157 – 160	Combined sources	4
Beta strandⁱ	167 – 176	Combined sources	10
Helixⁱ	181 – 187	Combined sources	7
Helixⁱ	188 – 192	Combined sources	5
Beta strandⁱ	199 – 203	Combined sources	5
Helixⁱ	207 – 210	Combined sources	4
Turnⁱ	213 – 216	Combined sources	4
Beta strandⁱ	218 – 223	Combined sources	6
Beta strandⁱ	234 – 241	Combined sources	8
Beta strandⁱ	243 – 245	Combined sources	3
Helixⁱ	247 – 255	Combined sources	9
Beta strandⁱ	258 – 260	Combined sources	3
Beta strandⁱ	285 – 288	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	O43570
SMRⁱ	O43570
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O43570

EvolutionaryTraceⁱ

O43570

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	30 – 289	Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST		260

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	226 – 227	Substrate bindingBy similarity		2

Sequence similaritiesⁱ

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG0382 Eukaryota COG3338 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118915
HOGENOMⁱ	HOG000112637
HOVERGENⁱ	HBG002837
InParanoidⁱ	O43570
KEGG Orthology (KO) More...KOⁱ	K01672
OMAⁱ	HTVGGKH
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0XFM
PhylomeDBⁱ	O43570
TreeFamⁱ	TF316425

Family and domain databases

Gene3Dⁱ	3.10.200.10, 1 hit
InterProⁱ	View protein in InterPro IPR001148 CA_dom IPR036398 CA_dom_sf IPR023561 Carbonic_anhydrase_a-class IPR018338 Carbonic_anhydrase_a-class_CS IPR018430 Carbonic_anhydrase_CA12
PANTHERⁱ	PTHR18952 PTHR18952, 1 hit PTHR18952:SF19 PTHR18952:SF19, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00194 Carb_anhydrase, 1 hit
SMARTⁱ	View protein in SMART SM01057 Carb_anhydrase, 1 hit
SUPFAMⁱ	SSF51069 SSF51069, 1 hit
PROSITEⁱ	View protein in PROSITE PS00162 ALPHA_CA_1, 1 hit PS51144 ALPHA_CA_2, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: O43570-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MPRRSLHAAA VLLLVILKEQ PSSPAPVNGS KWTYFGPDGE NSWSKKYPSC 
        60         70         80         90        100
GGLLQSPIDL HSDILQYDAS LTPLEFQGYN LSANKQFLLT NNGHSVKLNL 
       110        120        130        140        150
PSDMHIQGLQ SRYSATQLHL HWGNPNDPHG SEHTVSGQHF AAELHIVHYN 
       160        170        180        190        200
SDLYPDASTA SNKSEGLAVL AVLIEMGSFN PSYDKIFSHL QHVKYKGQEA 
       210        220        230        240        250
FVPGFNIEEL LPERTAEYYR YRGSLTTPPC NPTVLWTVFR NPVQISQEQL 
       260        270        280        290        300
LALETALYCT HMDDPSPREM INNFRQVQKF DERLVYTSFS QVQVCTAAGL 
       310        320        330        340        350
SLGIILSLAL AGILGICIVV VVSIWLFRRK SIKKGDNKGV IYKPATKMET 

EAHA

Length:354

Mass (Da):39,451

Last modified:June 1, 1998 - v1

Checksum:ⁱ9016216BF2CA6C0C

GO

Isoform 2 (identifier: O43570-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
292-302: Missing.

« Hide

        10         20         30         40         50
MPRRSLHAAA VLLLVILKEQ PSSPAPVNGS KWTYFGPDGE NSWSKKYPSC 
        60         70         80         90        100
GGLLQSPIDL HSDILQYDAS LTPLEFQGYN LSANKQFLLT NNGHSVKLNL 
       110        120        130        140        150
PSDMHIQGLQ SRYSATQLHL HWGNPNDPHG SEHTVSGQHF AAELHIVHYN 
       160        170        180        190        200
SDLYPDASTA SNKSEGLAVL AVLIEMGSFN PSYDKIFSHL QHVKYKGQEA 
       210        220        230        240        250
FVPGFNIEEL LPERTAEYYR YRGSLTTPPC NPTVLWTVFR NPVQISQEQL 
       260        270        280        290        300
LALETALYCT HMDDPSPREM INNFRQVQKF DERLVYTSFS QGIILSLALA 
       310        320        330        340 
GILGICIVVV VSIWLFRRKS IKKGDNKGVI YKPATKMETE AHA

Show »

Length:343

Mass (Da):38,408

Checksum:ⁱ87FD35255B137D18

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	B3KUB4	B3KUB4_HUMAN		Carbonic anhydrase 12 Carbonic anhydrase 12 (Carbonic anhydrase XII, isoform CRA_d) (cDNA FLJ39526 fis, clone PUAEN2003018, highly similar to CARBONIC ANHYDRASE XII)	CA12 hCG_2003428	283	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	305	I → T in BAG38121 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_065292	143	E → K in HCHLH; mild reduction of activity; mutant enzyme is highly inhibited by acetazolamide and shows higher sensitivity to inhibition by anions compared to wild-type; the mutation affects the chloride-mediated negative feedback regulation of the enzyme leading to excessive chloride secretion in sweat. 1 PublicationCorresponds to variant dbSNP:rs267606694EnsemblClinVar.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_000772	292 – 302	Missing in isoform 2. 2 PublicationsAdd BLAST		11

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF051882 mRNA Translation: AAC39789.1 AF037335 mRNA Translation: AAC63952.1 BT006656 mRNA Translation: AAP35302.1 AK315769 mRNA Translation: BAG38121.1 BC000278 mRNA Translation: AAH00278.1 BC011691 mRNA Translation: AAH11691.1 BC023981 mRNA Translation: AAH23981.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10185.1 [O43570-1] CCDS10186.1 [O43570-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001209.1, NM_001218.4 [O43570-1] NP_996808.1, NM_206925.2 [O43570-2]
UniGeneⁱ	Hs.210995 Hs.603780

Genome annotation databases

Ensemblⁱ	ENST00000178638; ENSP00000178638; ENSG00000074410 [O43570-1] ENST00000344366; ENSP00000343088; ENSG00000074410 [O43570-2]
GeneIDⁱ	771
KEGGⁱ	hsa:771
UCSC genome browser More...UCSCⁱ	uc002amc.4 human [O43570-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O43570	Carbonic anhydrase 12 precursor		MACMU		354	UniRef90_O43570
Uncharacterized protein		MACFA		354
Carbonic anhydrase 12 isoform 1		CALJA		354
CA12 isoform 1		PANTR		354
Uncharacterized protein		PANPA		354
+56

Protein	Similar proteins		Species	Score	Length	Source
O43570	Carbonic anhydrase 12		MOUSE		354	UniRef50_O43570
Carbonic anhydrase 12		RABIT		355
Carbonic anhydrase 12		PONAB		354
Carbonic anhydrase 12 isoform 1		CALJA		354
Uncharacterized protein		Cebus capucinus imitator		354
+274

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF051882 mRNA Translation: AAC39789.1 AF037335 mRNA Translation: AAC63952.1 BT006656 mRNA Translation: AAP35302.1 AK315769 mRNA Translation: BAG38121.1 BC000278 mRNA Translation: AAH00278.1 BC011691 mRNA Translation: AAH11691.1 BC023981 mRNA Translation: AAH23981.1
CCDSⁱ	CCDS10185.1 [O43570-1] CCDS10186.1 [O43570-2]
RefSeqⁱ	NP_001209.1, NM_001218.4 [O43570-1] NP_996808.1, NM_206925.2 [O43570-2]
UniGeneⁱ	Hs.210995 Hs.603780

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1JCZ	X-ray	1.55	A/B	30-291	[»]
	1JD0	X-ray	1.50	A/B	30-291	[»]
	4HT2	X-ray	1.45	A/B/C/D	30-291	[»]
	4KP5	X-ray	1.45	A/B/C/D	30-291	[»]
	4KP8	X-ray	1.80	A/B/C/D	30-291	[»]
	4Q0L	X-ray	2.00	A/B/C/D	30-291	[»]
	4QJ0	X-ray	1.55	A/B/C/D	30-291	[»]
	4QJO	X-ray	1.80	A/B/C/D	30-291	[»]
	4QJW	X-ray	1.55	A/B/C/D	30-291	[»]
	4WW8	X-ray	1.42	A/B/C/D	30-291	[»]
	5LL5	X-ray	1.42	A/B/C/D	30-291	[»]
	5LL9	X-ray	1.45	A/B/C/D	30-291	[»]
	5LLO	X-ray	1.60	A/B/C/D	30-291	[»]
	5LLP	X-ray	1.48	A/B/C/D	30-291	[»]
	5MSA	X-ray	1.20	A/B/C/D	30-291	[»]
	5MSB	X-ray	1.30	A/B/C/D	30-291	[»]
ProteinModelPortalⁱ	O43570
SMRⁱ	O43570
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107225, 8 interactors
IntActⁱ	O43570, 10 interactors
MINTⁱ	O43570
STRINGⁱ	9606.ENSP00000178638

Chemistry databases

BindingDBⁱ	O43570
ChEMBLⁱ	CHEMBL3242
DrugBankⁱ	DB00562 Benzthiazide DB08846 Ellagic Acid DB00999 Hydrochlorothiazide DB00774 Hydroflumethiazide DB00909 Zonisamide
GuidetoPHARMACOLOGYⁱ	2747

PTM databases

GlyConnectⁱ	1064
iPTMnetⁱ	O43570
PhosphoSitePlusⁱ	O43570

Polymorphism and mutation databases

BioMutaⁱ	CA12

BioMutaⁱ

CA12

Proteomic databases

EPDⁱ	O43570
MaxQBⁱ	O43570
PaxDbⁱ	O43570
PeptideAtlasⁱ	O43570
PRIDEⁱ	O43570
ProteomicsDBⁱ	49059 49060 [O43570-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	771
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000178638; ENSP00000178638; ENSG00000074410 [O43570-1] ENST00000344366; ENSP00000343088; ENSG00000074410 [O43570-2]
GeneIDⁱ	771
KEGGⁱ	hsa:771
UCSCⁱ	uc002amc.4 human [O43570-1]

Organism-specific databases

CTDⁱ	771
DisGeNETⁱ	771
EuPathDBⁱ	HostDB:ENSG00000074410.13
GeneCardsⁱ	CA12
HGNCⁱ	HGNC:1371 CA12
HPAⁱ	CAB025181 CAB062549 CAB068179 HPA008773 HPA073203
MalaCardsⁱ	CA12
MIMⁱ	143860 phenotype 603263 gene
neXtProtⁱ	NX_O43570
OpenTargetsⁱ	ENSG00000074410
PharmGKBⁱ	PA25987
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0382 Eukaryota COG3338 LUCA
GeneTreeⁱ	ENSGT00760000118915
HOGENOMⁱ	HOG000112637
HOVERGENⁱ	HBG002837
InParanoidⁱ	O43570
KOⁱ	K01672
OMAⁱ	HTVGGKH
OrthoDBⁱ	EOG091G0XFM
PhylomeDBⁱ	O43570
TreeFamⁱ	TF316425

Enzyme and pathway databases

BRENDAⁱ	4.2.1.1 2681
Reactomeⁱ	R-HSA-1475029 Reversible hydration of carbon dioxide

Miscellaneous databases

ChiTaRSⁱ	CA12 human
EvolutionaryTraceⁱ	O43570
GeneWikiⁱ	CA12
GenomeRNAiⁱ	771
Protein Ontology More...PROⁱ	PR:O43570
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000074410 Expressed in 204 organ(s), highest expression level in cortex of kidney
CleanExⁱ	HS_CA12
ExpressionAtlasⁱ	O43570 baseline and differential
Genevisibleⁱ	O43570 HS

Family and domain databases

Gene3Dⁱ	3.10.200.10, 1 hit
InterProⁱ	View protein in InterPro IPR001148 CA_dom IPR036398 CA_dom_sf IPR023561 Carbonic_anhydrase_a-class IPR018338 Carbonic_anhydrase_a-class_CS IPR018430 Carbonic_anhydrase_CA12
PANTHERⁱ	PTHR18952 PTHR18952, 1 hit PTHR18952:SF19 PTHR18952:SF19, 1 hit
Pfamⁱ	View protein in Pfam PF00194 Carb_anhydrase, 1 hit
SMARTⁱ	View protein in SMART SM01057 Carb_anhydrase, 1 hit
SUPFAMⁱ	SSF51069 SSF51069, 1 hit
PROSITEⁱ	View protein in PROSITE PS00162 ALPHA_CA_1, 1 hit PS51144 ALPHA_CA_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CAH12_HUMAN
Accessionⁱ	O43570Primary (citable) accession number: O43570 Secondary accession number(s): B2RE24, Q53YE5, Q9BWG2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
	Last sequence update:	June 1, 1998
	Last modified:	November 7, 2018
	This is version 178 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
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
Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM

UniProtKB

UniParc

Help

UniRef

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Annotation systems

Supporting data

UniProtKB - O43570 (CAH12_HUMAN)

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Carbonic anhydrase 12

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Other locations

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ