HUMAN:CAH2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CA2
Protein Name(s)	Carbonic anhydrase 2 Carbonate dehydratase II Carbonic anhydrase C CAC Carbonic anhydrase II CA-II
External Links
UniProt	P00918
EMBL	M77181 M77176 M77177 M77178 M77179 M77180 Y00339 X03251 J03037 CR536526 CR541875 AK312978 CH471068 BC011949 M36532
CCDS	CCDS6239.1
PIR	A27175
RefSeq	NP_000058.1
UniGene	Hs.155097
PDB	12CA 1A42 1AM6 1AVN 1BCD 1BIC 1BN1 1BN3 1BN4 1BNM 1BNN 1BNQ 1BNT 1BNU 1BNV 1BNW 1BV3 1CA2 1CA3 1CAH 1CAI 1CAJ 1CAK 1CAL 1CAM 1CAN 1CAO 1CAY 1CAZ 1CCS 1CCT 1CCU 1CIL 1CIM 1CIN 1CNB 1CNC 1CNG 1CNH 1CNI 1CNJ 1CNK 1CNW 1CNX 1CNY 1CRA 1CVA 1CVB 1CVC 1CVD 1CVE 1CVF 1CVH 1DCA 1DCB 1EOU 1F2W 1FQL 1FQM 1FQN 1FQR 1FR4 1FR7 1FSN 1FSQ 1FSR 1G0E 1G0F 1G1D 1G3Z 1G45 1G46 1G48 1G4J 1G4O 1G52 1G53 1G54 1H4N 1H9N 1H9Q 1HCA 1HEA 1HEB 1HEC 1HED 1HVA 1I8Z 1I90 1I91 1I9L 1I9M 1I9N 1I9O 1I9P 1I9Q 1IF4 1IF5 1IF6 1IF7 1IF8 1IF9 1KWQ 1KWR 1LG5 1LG6 1LGD 1LUG 1LZV 1MOO 1MUA 1OKL 1OKM 1OKN 1OQ5 1RAY 1RAZ 1RZA 1RZB 1RZC 1RZD 1RZE 1T9N 1TB0 1TBT 1TE3 1TEQ 1TEU 1TG3 1TG9 1TH9 1THK 1TTM 1UGA 1UGB 1UGC 1UGD 1UGE 1UGF 1UGG 1XEG 1XEV 1XPZ 1XQ0 1YDA 1YDB 1YDC 1YDD 1YO0 1YO1 1YO2 1Z9Y 1ZE8 1ZFK 1ZFQ 1ZGE 1ZGF 1ZH9 1ZSA 1ZSB 1ZSC 2ABE 2AW1 2AX2 2CA2 2CBA 2CBB 2CBC 2CBD 2CBE 2EU2 2EU3 2EZ7 2F14 2FMG 2FMZ 2FNK 2FNM 2FNN 2FOQ 2FOS 2FOU 2FOV 2GD8 2GEH 2H15 2H4N 2HD6 2HKK 2HL4 2HNC 2HOC 2ILI 2NNG 2NNO 2NNS 2NNV 2NWO 2NWP 2NWY 2NWZ 2NXR 2NXS 2NXT 2O4Z 2OSF 2OSM 2POU 2POV 2POW 2Q1B 2Q1Q 2Q38 2QO8 2QOA 2QP6 2VVA 2VVB 2WD2 2WD3 2WEG 2WEH 2WEJ 2WEO 2X7S 2X7T 2X7U 3B4F 3BET 3BL0 3BL1 3C7P 3CA2 3CAJ 3CYU 3D8W 3D92 3D93 3D9Z 3DAZ 3DBU 3DC3 3DC9 3DCC 3DCS 3DCW 3DD0 3DD8 3DV7 3DVB 3DVC 3DVD 3EFI 3EFT 3F4X 3F8E 3FFP 3GZ0 3HFP 3HKN 3HKQ 3HKT 3HKU 3HLJ 3HS4 3IBI 3IBL 3IBN 3IBU 3IEO 3IGP 3K2F 3K34 3K7K 3KIG 3KKX 3KNE 3KOI 3KOK 3KON 3KS3 3KWA 3L14 3M04 3M14 3M1J 3M1K 3M1Q 3M1W 3M2N 3M2X 3M2Y 3M2Z 3M3X 3M40 3M5E 3M5S 3M5T 3M67 3M96 3M98 3MHC 3MHI 3MHL 3MHM 3MHO 3ML2 3MMF 3MNA 3MNH 3MNI 3MNJ 3MNK 3MNU 3MWO 3MYQ 3MZC 3N0N 3N2P 3N3J 3N4B 3NB5 3NI5 3NJ9 3OIK 3OIL 3OIM 3OKU 3OKV 3OY0 3OYQ 3OYS 3P3H 3P3J 3P44 3P4V 3P55 3P58 3P5A 3P5L 3PJJ 3PO6 3PYK 3QYK 3R16 3R17 3RG3 3RG4 3RGE 3RJ7 3RLD 3RYJ 3RYV 3RYX 3RYY 3RYZ 3RZ0 3RZ1 3RZ5 3RZ7 3RZ8 3S71 3S72 3S73 3S74 3S75 3S76 3S77 3S78 3S8X 3S9T 3SAP 3SAX 3SBH 3SBI 3T5U 3T5Z 3T82 3T83 3T84 3T85 3TMJ 3TVN 3TVO 3U3A 3U45 3U47 3U7C 3V2J 3V2M 3V3F 3V3G 3V3H 3V3I 3V3J 3V5G 3V7X 3VBD 3ZP9 4BCW 4BF1 4BF6 4CA2 4CAC 4CQ0 4DZ7 4DZ9 4E3D 4E3F 4E3G 4E3H 4E49 4E4A 4E5Q 4FIK 4FL7 4FPT 4FRC 4FU5 4FVN 4FVO 4G0C 4GL1 4HBA 4HEW 4HEY 4HEZ 4HF3 4HT0 4IDR 4ILX 4ITO 4ITP 4IWZ 4JS6 4JSA 4JSS 4JSW 4JSZ 4K0S 4K0T 4K0Z 4K13 4K1Q 4KAP 4KNI 4KNJ 4KUV 4KUW 4KUY 4KV0 4L5U 4L5V 4L5W 4LHI 4LP6 4M2R 4M2U 4M2V 4M2W 4MDG 4MDL 4MDM 4MLT 4MLX 4MO8 4MTY 4N0X 4N16 4PQ7 4QEF 4R59 4R5A 4R5B 5CA2 5CAC 6CA2 7CA2 8CA2 9CA2
PDBsum	12CA 1A42 1AM6 1AVN 1BCD 1BIC 1BN1 1BN3 1BN4 1BNM 1BNN 1BNQ 1BNT 1BNU 1BNV 1BNW 1BV3 1CA2 1CA3 1CAH 1CAI 1CAJ 1CAK 1CAL 1CAM 1CAN 1CAO 1CAY 1CAZ 1CCS 1CCT 1CCU 1CIL 1CIM 1CIN 1CNB 1CNC 1CNG 1CNH 1CNI 1CNJ 1CNK 1CNW 1CNX 1CNY 1CRA 1CVA 1CVB 1CVC 1CVD 1CVE 1CVF 1CVH 1DCA 1DCB 1EOU 1F2W 1FQL 1FQM 1FQN 1FQR 1FR4 1FR7 1FSN 1FSQ 1FSR 1G0E 1G0F 1G1D 1G3Z 1G45 1G46 1G48 1G4J 1G4O 1G52 1G53 1G54 1H4N 1H9N 1H9Q 1HCA 1HEA 1HEB 1HEC 1HED 1HVA 1I8Z 1I90 1I91 1I9L 1I9M 1I9N 1I9O 1I9P 1I9Q 1IF4 1IF5 1IF6 1IF7 1IF8 1IF9 1KWQ 1KWR 1LG5 1LG6 1LGD 1LUG 1LZV 1MOO 1MUA 1OKL 1OKM 1OKN 1OQ5 1RAY 1RAZ 1RZA 1RZB 1RZC 1RZD 1RZE 1T9N 1TB0 1TBT 1TE3 1TEQ 1TEU 1TG3 1TG9 1TH9 1THK 1TTM 1UGA 1UGB 1UGC 1UGD 1UGE 1UGF 1UGG 1XEG 1XEV 1XPZ 1XQ0 1YDA 1YDB 1YDC 1YDD 1YO0 1YO1 1YO2 1Z9Y 1ZE8 1ZFK 1ZFQ 1ZGE 1ZGF 1ZH9 1ZSA 1ZSB 1ZSC 2ABE 2AW1 2AX2 2CA2 2CBA 2CBB 2CBC 2CBD 2CBE 2EU2 2EU3 2EZ7 2F14 2FMG 2FMZ 2FNK 2FNM 2FNN 2FOQ 2FOS 2FOU 2FOV 2GD8 2GEH 2H15 2H4N 2HD6 2HKK 2HL4 2HNC 2HOC 2ILI 2NNG 2NNO 2NNS 2NNV 2NWO 2NWP 2NWY 2NWZ 2NXR 2NXS 2NXT 2O4Z 2OSF 2OSM 2POU 2POV 2POW 2Q1B 2Q1Q 2Q38 2QO8 2QOA 2QP6 2VVA 2VVB 2WD2 2WD3 2WEG 2WEH 2WEJ 2WEO 2X7S 2X7T 2X7U 3B4F 3BET 3BL0 3BL1 3C7P 3CA2 3CAJ 3CYU 3D8W 3D92 3D93 3D9Z 3DAZ 3DBU 3DC3 3DC9 3DCC 3DCS 3DCW 3DD0 3DD8 3DV7 3DVB 3DVC 3DVD 3EFI 3EFT 3F4X 3F8E 3FFP 3GZ0 3HFP 3HKN 3HKQ 3HKT 3HKU 3HLJ 3HS4 3IBI 3IBL 3IBN 3IBU 3IEO 3IGP 3K2F 3K34 3K7K 3KIG 3KKX 3KNE 3KOI 3KOK 3KON 3KS3 3KWA 3L14 3M04 3M14 3M1J 3M1K 3M1Q 3M1W 3M2N 3M2X 3M2Y 3M2Z 3M3X 3M40 3M5E 3M5S 3M5T 3M67 3M96 3M98 3MHC 3MHI 3MHL 3MHM 3MHO 3ML2 3MMF 3MNA 3MNH 3MNI 3MNJ 3MNK 3MNU 3MWO 3MYQ 3MZC 3N0N 3N2P 3N3J 3N4B 3NB5 3NI5 3NJ9 3OIK 3OIL 3OIM 3OKU 3OKV 3OY0 3OYQ 3OYS 3P3H 3P3J 3P44 3P4V 3P55 3P58 3P5A 3P5L 3PJJ 3PO6 3PYK 3QYK 3R16 3R17 3RG3 3RG4 3RGE 3RJ7 3RLD 3RYJ 3RYV 3RYX 3RYY 3RYZ 3RZ0 3RZ1 3RZ5 3RZ7 3RZ8 3S71 3S72 3S73 3S74 3S75 3S76 3S77 3S78 3S8X 3S9T 3SAP 3SAX 3SBH 3SBI 3T5U 3T5Z 3T82 3T83 3T84 3T85 3TMJ 3TVN 3TVO 3U3A 3U45 3U47 3U7C 3V2J 3V2M 3V3F 3V3G 3V3H 3V3I 3V3J 3V5G 3V7X 3VBD 3ZP9 4BCW 4BF1 4BF6 4CA2 4CAC 4CQ0 4DZ7 4DZ9 4E3D 4E3F 4E3G 4E3H 4E49 4E4A 4E5Q 4FIK 4FL7 4FPT 4FRC 4FU5 4FVN 4FVO 4G0C 4GL1 4HBA 4HEW 4HEY 4HEZ 4HF3 4HT0 4IDR 4ILX 4ITO 4ITP 4IWZ 4JS6 4JSA 4JSS 4JSW 4JSZ 4K0S 4K0T 4K0Z 4K13 4K1Q 4KAP 4KNI 4KNJ 4KUV 4KUW 4KUY 4KV0 4L5U 4L5V 4L5W 4LHI 4LP6 4M2R 4M2U 4M2V 4M2W 4MDG 4MDL 4MDM 4MLT 4MLX 4MO8 4MTY 4N0X 4N16 4PQ7 4QEF 4R59 4R5A 4R5B 5CA2 5CAC 6CA2 7CA2 8CA2 9CA2
ProteinModelPortal	P00918
SMR	P00918
BioGrid	107215
IntAct	P00918
MINT	MINT-1367766
STRING	9606.ENSP00000285379
BindingDB	P00918
ChEMBL	CHEMBL205
DrugBank	DB00819 DB00436 DB00562 DB01194 DB00880 DB00606 DB01119 DB01144 DB00869 DB01031 DB00695 DB00999 DB00774 DB00703 DB00232 DB01325 DB00273 DB01021 DB00909
PhosphoSite	P00918
OGP	P00918
REPRODUCTION-2DPAGE	IPI00218414 P00918
UCD-2DPAGE	P00918
MaxQB	P00918
PaxDb	P00918
PeptideAtlas	P00918
PRIDE	P00918
DNASU	760
Ensembl	ENST00000285379
GeneID	760
KEGG	hsa:760
UCSC	uc003ydk.2
CTD	760
GeneCards	GC08P086376
HGNC	HGNC:1373
HPA	CAB010102 HPA001550
MIM	259730 611492
neXtProt	NX_P00918
Orphanet	2785
PharmGKB	PA25989
eggNOG	COG3338
HOGENOM	HOG000112637
HOVERGEN	HBG002837
InParanoid	P00918
KO	K18245
OMA	HFVHADK
OrthoDB	EOG7WMCK7
PhylomeDB	P00918
TreeFam	TF316425
BRENDA	4.2.1.1
Reactome	REACT_121123 REACT_121329 REACT_121380
SABIO-RK	P00918
ChiTaRS	CA2
EvolutionaryTrace	P00918
GeneWiki	Carbonic_anhydrase_II
GenomeRNAi	760
NextBio	3074
PRO	PR:P00918
Proteomes	UP000005640
Bgee	P00918
CleanEx	HS_CA2
ExpressionAtlas	P00918
Genevestigator	P00918
GO	GO:0045177 GO:0030424 GO:0016323 GO:0005737 GO:0005829 GO:0005615 GO:0070062 GO:0005902 GO:0043209 GO:0005886 GO:0004089 GO:0008270 GO:0038166 GO:0015701 GO:0071498 GO:0001822 GO:0002009 GO:0042475 GO:0006730 GO:0045780 GO:0032849 GO:2001150 GO:0045672 GO:0032230 GO:0044070 GO:2001225 GO:0051453 GO:0043627 GO:0009268 GO:0010043 GO:0046903 GO:0044281
Gene3D	3.10.200.10
InterPro	IPR018443 IPR001148 IPR023561 IPR018338
PANTHER	PTHR18952 PTHR18952:SF90
Pfam	PF00194
SMART	SM01057
SUPFAM	SSF51069
PROSITE	PS00162 PS51144

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004089	carbonate dehydratase activity	PMID:9336012^[1]	ECO:0000314			F		Figure 10	complete CACAO 5418
	GO:0004064	arylesterase activity	PMID:3126084^[2]	ECO:0000315			F		Table 2 shows the effect of mutations at residue 64 on kinetic constants for hydrolysis of 4-nitrophenyl acetate by purified human CAHII. Because this reaction is the hydrolysis of a phenyl acetate, this protein has arylesterase activity.	complete CACAO 5477
	GO:0004089	carbonate dehydratase activity	PMID:7758465^[3]	ECO:0000315			F		Table 2	complete CACAO 5529
	GO:0004089	carbonate dehydratase activity	PMID:9336012^[1]	ECO:0000314			F		Figure 11	complete CACAO 5779
	GO:0004089	carbonate dehydratase activity	PMID:4994926^[4]	ECO:0000314			F		Figure 5	complete CACAO 5795
	GO:0004089	carbonate dehydratase activity	PMID:1433293^[5]	ECO:0000314			F		Figure 8	complete CACAO 6297
enables	GO:0004089	carbonate dehydratase activity	PMID:7758465^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004064	arylesterase activity	PMID:3126084^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
involved_in	GO:2001150	positive regulation of dipeptide transmembrane transport	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P00920	P		Seeded From UniProt	complete
involved_in	GO:0051453	regulation of intracellular pH	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P00920	P		Seeded From UniProt	complete
part_of	GO:0045177	apical part of cell	PMID:14675051^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0044070	regulation of anion transport	PMID:15990874^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038166	angiotensin-activated signaling pathway	PMID:15990874^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:3151020^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15990874^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15990874^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:114507^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2001225	regulation of chloride transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
involved_in	GO:2001150	positive regulation of dipeptide transmembrane transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
involved_in	GO:0051453	regulation of intracellular pH	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
involved_in	GO:0046903	secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
part_of	GO:0043209	myelin sheath	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	C		Seeded From UniProt	complete
involved_in	GO:0032849	positive regulation of cellular pH reduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
involved_in	GO:0032230	positive regulation of synaptic transmission, GABAergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
involved_in	GO:0015670	carbon dioxide transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	C		Seeded From UniProt	complete
enables	GO:0004089	carbonate dehydratase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	F		Seeded From UniProt	complete
involved_in	GO:0002009	morphogenesis of an epithelium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P00920 ensembl:ENSMUSP00000029078	P		Seeded From UniProt	complete
involved_in	GO:0071498	cellular response to fluid shear stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0048545	response to steroid hormone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0045780	positive regulation of bone resorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0045672	positive regulation of osteoclast differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
part_of	GO:0045177	apical part of cell	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	C		Seeded From UniProt	complete
involved_in	GO:0043627	response to estrogen	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0042475	odontogenesis of dentin-containing tooth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0032849	positive regulation of cellular pH reduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	C		Seeded From UniProt	complete
part_of	GO:0016323	basolateral plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	C		Seeded From UniProt	complete
involved_in	GO:0010043	response to zinc ion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0010033	response to organic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
involved_in	GO:0009268	response to pH	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
part_of	GO:0005902	microvillus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	C		Seeded From UniProt	complete
enables	GO:0004089	carbonate dehydratase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	F		Seeded From UniProt	complete
involved_in	GO:0001822	kidney development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P27139 ensembl:ENSRNOP00000013354	P		Seeded From UniProt	complete
enables	GO:0004089	carbonate dehydratase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018338 InterPro:IPR023561	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018338 InterPro:IPR023561	F		Seeded From UniProt	complete
enables	GO:0004089	carbonate dehydratase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.1.1	F		Seeded From UniProt	complete
enables	GO:0004089	carbonate dehydratase activity	PMID:1928091^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0015701	bicarbonate transport	Reactome:R-HSA-1475029 Reactome:R-HSA-1247673 Reactome:R-HSA-1237044	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-1475436 Reactome:R-HSA-1475435 Reactome:R-HSA-1475026 Reactome:R-HSA-1475022	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Lindskog, S (1997) Structure and mechanism of carbonic anhydrase. Pharmacol. Ther. 74 1-20 PubMed GONUTS page
↑ ^2.0 ^2.1 Forsman, C et al. (1988) Histidine 64 is not required for high CO2 hydration activity of human carbonic anhydrase II. FEBS Lett. 229 360-2 PubMed GONUTS page
↑ ^3.0 ^3.1 Engstrand, C et al. (1995) Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I. Eur. J. Biochem. 229 696-702 PubMed GONUTS page
↑ Khalifah, RG (1971) The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C. J. Biol. Chem. 246 2561-73 PubMed GONUTS page
↑ Håkansson, K et al. (1992) Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J. Mol. Biol. 227 1192-204 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Jouret, F et al. (2004) Comparative ontogeny, processing, and segmental distribution of the renal chloride channel, ClC-5. Kidney Int. 65 198-208 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Alvarez, BV et al. (2005) Metabolon disruption: a mechanism that regulates bicarbonate transport. EMBO J. 24 2499-511 PubMed GONUTS page
↑ Eriksson, AE et al. (1988) Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. Proteins 4 283-93 PubMed GONUTS page
↑ Kumpulainen, T (1979) Immunohistochemical localization of human carbonic anhydrase isoenzyme C. Histochemistry 62 271-80 PubMed GONUTS page
↑ Venta, PJ et al. (1991) Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene. Am. J. Hum. Genet. 49 1082-90 PubMed GONUTS page

[PMID:9336012-1] 1.0 ^1.1 Lindskog, S (1997) Structure and mechanism of carbonic anhydrase. Pharmacol. Ther. 74 1-20 PubMed GONUTS page

[PMID:3126084-2] 2.0 ^2.1 Forsman, C et al. (1988) Histidine 64 is not required for high CO2 hydration activity of human carbonic anhydrase II. FEBS Lett. 229 360-2 PubMed GONUTS page

[PMID:7758465-3] 3.0 ^3.1 Engstrand, C et al. (1995) Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I. Eur. J. Biochem. 229 696-702 PubMed GONUTS page

[PMID:4994926-4] Khalifah, RG (1971) The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C. J. Biol. Chem. 246 2561-73 PubMed GONUTS page

[PMID:1433293-5] Håkansson, K et al. (1992) Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J. Mol. Biol. 227 1192-204 PubMed GONUTS page

[PMID:19056867-6] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:14675051-7] Jouret, F et al. (2004) Comparative ontogeny, processing, and segmental distribution of the renal chloride channel, ClC-5. Kidney Int. 65 198-208 PubMed GONUTS page

[PMID:15990874-8] 8.0 ^8.1 ^8.2 ^8.3 Alvarez, BV et al. (2005) Metabolon disruption: a mechanism that regulates bicarbonate transport. EMBO J. 24 2499-511 PubMed GONUTS page

[PMID:3151020-9] Eriksson, AE et al. (1988) Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. Proteins 4 283-93 PubMed GONUTS page

[PMID:114507-10] Kumpulainen, T (1979) Immunohistochemical localization of human carbonic anhydrase isoenzyme C. Histochemistry 62 271-80 PubMed GONUTS page

[PMID:1928091-11] Venta, PJ et al. (1991) Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene. Am. J. Hum. Genet. 49 1082-90 PubMed GONUTS page

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HUMAN:CAH2

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