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P43166

- CAH7_HUMAN

UniProt

P43166 - CAH7_HUMAN

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Protein

Carbonic anhydrase 7

Gene
CA7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited coumarins, sulfonamide derivatives such as acetazolamide (AZA), by saccharin and Foscarnet (phosphonoformate trisodium salt).7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661Proton acceptor By similarity
Metal bindingi96 – 961Zinc; catalytic
Metal bindingi98 – 981Zinc; catalytic
Metal bindingi121 – 1211Zinc; catalytic
Active sitei130 – 1301 By similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: ProtInc
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. bicarbonate transport Source: Reactome
  2. one-carbon metabolic process Source: InterPro
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
SABIO-RKP43166.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 7 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase VII
Carbonic anhydrase VII
Short name:
CA-VII
Gene namesi
Name:CA7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:1381. CA7.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25996.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Carbonic anhydrase 7PRO_0000077431Add
BLAST

Proteomic databases

PaxDbiP43166.
PRIDEiP43166.

PTM databases

PhosphoSiteiP43166.

Expressioni

Gene expression databases

ArrayExpressiP43166.
BgeeiP43166.
CleanExiHS_CA7.
GenevestigatoriP43166.

Organism-specific databases

HPAiHPA047237.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000345659.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 133
Helixi15 – 173
Helixi18 – 214
Helixi23 – 264
Beta strandi27 – 293
Helixi37 – 393
Beta strandi40 – 423
Beta strandi46 – 527
Beta strandi58 – 636
Beta strandi68 – 725
Beta strandi75 – 8410
Beta strandi90 – 9910
Beta strandi108 – 1114
Beta strandi117 – 1259
Turni127 – 1293
Helixi133 – 1364
Beta strandi142 – 15413
Helixi157 – 1648
Turni165 – 1695
Beta strandi174 – 1774
Helixi183 – 1864
Beta strandi193 – 1986
Beta strandi209 – 2168
Beta strandi218 – 2203
Helixi222 – 2298
Beta strandi232 – 2343
Beta strandi259 – 2624

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MDZX-ray2.32A5-262[»]
3ML5X-ray2.05A1-264[»]
ProteinModelPortaliP43166.
SMRiP43166. Positions 5-262.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2022Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP43166.
KOiK01672.
OMAiLVHWNAR.
OrthoDBiEOG7WMCK7.
PhylomeDBiP43166.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018438. Carbonic_anhydrase_CA7.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF26. PTHR18952:SF26. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P43166-1) [UniParc]FASTAAdd 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

MTGHHGWGYG QDDGPSHWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE    50
LSYEACMSLS ITNNGHSVQV DFNDSDDRTV VTGGPLEGPY RLKQFHFHWG 100
KKHDVGSEHT VDGKSFPSEL HLVHWNAKKY STFGEAASAP DGLAVVGVFL 150
ETGDEHPSMN RLTDALYMVR FKGTKAQFSC FNPKCLLPAS RHYWTYPGSL 200
TTPPLSESVT WIVLREPICI SERQMGKFRS LLFTSEDDER IHMVNNFRPP 250
QPLKGRVVKA SFRA 264
Length:264
Mass (Da):29,658
Last modified:November 1, 1995 - v1
Checksum:i7AD559FC6E07EF96
GO
Isoform 2 (identifier: P43166-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.

Show »
Length:208
Mass (Da):23,452
Checksum:iAF3D016A27182D18
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 2. VSP_044254Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76423
, M76420, M76421, M76422 Genomic DNA. Translation: AAA51923.1.
AY075019 mRNA. Translation: AAL78167.1.
AY075020 mRNA. Translation: AAL78168.1.
AC004638 Genomic DNA. Translation: AAC23785.1.
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83047.1.
BC033865 mRNA. Translation: AAH33865.1.
CCDSiCCDS10821.1. [P43166-1]
CCDS42173.1. [P43166-2]
PIRiA55272. CRHU7.
RefSeqiNP_001014435.1. NM_001014435.1. [P43166-2]
NP_005173.1. NM_005182.2. [P43166-1]
XP_005256193.1. XM_005256136.1. [P43166-2]
UniGeneiHs.37014.

Genome annotation databases

EnsembliENST00000338437; ENSP00000345659; ENSG00000168748. [P43166-1]
ENST00000394069; ENSP00000377632; ENSG00000168748. [P43166-2]
GeneIDi766.
KEGGihsa:766.
UCSCiuc002eqi.3. human. [P43166-1]

Polymorphism databases

DMDMi1168744.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M76423
, M76420 , M76421 , M76422 Genomic DNA. Translation: AAA51923.1 .
AY075019 mRNA. Translation: AAL78167.1 .
AY075020 mRNA. Translation: AAL78168.1 .
AC004638 Genomic DNA. Translation: AAC23785.1 .
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83047.1 .
BC033865 mRNA. Translation: AAH33865.1 .
CCDSi CCDS10821.1. [P43166-1 ]
CCDS42173.1. [P43166-2 ]
PIRi A55272. CRHU7.
RefSeqi NP_001014435.1. NM_001014435.1. [P43166-2 ]
NP_005173.1. NM_005182.2. [P43166-1 ]
XP_005256193.1. XM_005256136.1. [P43166-2 ]
UniGenei Hs.37014.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MDZ X-ray 2.32 A 5-262 [» ]
3ML5 X-ray 2.05 A 1-264 [» ]
ProteinModelPortali P43166.
SMRi P43166. Positions 5-262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000345659.

Chemistry

BindingDBi P43166.
ChEMBLi CHEMBL2326.
GuidetoPHARMACOLOGYi 2749.

PTM databases

PhosphoSitei P43166.

Polymorphism databases

DMDMi 1168744.

Proteomic databases

PaxDbi P43166.
PRIDEi P43166.

Protocols and materials databases

DNASUi 766.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338437 ; ENSP00000345659 ; ENSG00000168748 . [P43166-1 ]
ENST00000394069 ; ENSP00000377632 ; ENSG00000168748 . [P43166-2 ]
GeneIDi 766.
KEGGi hsa:766.
UCSCi uc002eqi.3. human. [P43166-1 ]

Organism-specific databases

CTDi 766.
GeneCardsi GC16P066880.
HGNCi HGNC:1381. CA7.
HPAi HPA047237.
MIMi 114770. gene.
neXtProti NX_P43166.
PharmGKBi PA25996.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3338.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P43166.
KOi K01672.
OMAi LVHWNAR.
OrthoDBi EOG7WMCK7.
PhylomeDBi P43166.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 2681.
Reactomei REACT_121123. Reversible hydration of carbon dioxide.
SABIO-RK P43166.

Miscellaneous databases

GeneWikii Carbonic_anhydrase_7.
GenomeRNAii 766.
NextBioi 3096.
PROi P43166.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43166.
Bgeei P43166.
CleanExi HS_CA7.
Genevestigatori P43166.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018438. Carbonic_anhydrase_CA7.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF26. PTHR18952:SF26. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the human gene for a newly discovered carbonic anhydrase, CA VII, and its localization to chromosome 16."
    Montgomery J.C., Venta P.J., Eddy R.L., Fukushima Y.S., Shows T.B., Tashian R.E.
    Genomics 11:835-848(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Molecular identification of carbonic anhydrases (CA) and CA-related (CAR) genes."
    Chen Y., Huang C.-H.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon, Kidney and Stomach.
  6. "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
    Temperini C., Scozzafava A., Vullo D., Supuran C.T.
    Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
    Temperini C., Scozzafava A., Vullo D., Supuran C.T.
    J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  8. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
    Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
    Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
    Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
    Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  11. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
    Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
    Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  12. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
    Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
    J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  13. "Crystal structure of human carbonic anhydrase VII [isoform 1], CA7."
    Structural genomics consortium (SGC)
    Submitted (JUN-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 5-262 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiCAH7_HUMAN
AccessioniPrimary (citable) accession number: P43166
Secondary accession number(s): Q541F0, Q86YU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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