位置:首页 > 蛋白库 > CAH7_HUMAN
CAH7_HUMAN
ID   CAH7_HUMAN              Reviewed;         264 AA.
AC   P43166; Q541F0; Q86YU0;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Carbonic anhydrase 7;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase VII;
DE   AltName: Full=Carbonic anhydrase VII;
DE            Short=CA-VII;
GN   Name=CA7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=1783392; DOI=10.1016/0888-7543(91)90006-z;
RA   Montgomery J.C., Venta P.J., Eddy R.L., Fukushima Y.S., Shows T.B.,
RA   Tashian R.E.;
RT   "Characterization of the human gene for a newly discovered carbonic
RT   anhydrase, CA VII, and its localization to chromosome 16.";
RL   Genomics 11:835-848(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Chen Y., Huang C.-H.;
RT   "Molecular identification of carbonic anhydrases (CA) and CA-related (CAR)
RT   genes.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, Kidney, and Stomach;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   ACTIVITY REGULATION.
RX   PubMed=16807956; DOI=10.1002/chem.200600159;
RA   Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT   "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII,
RT   and XIV with l- and d-histidine and crystallographic analysis of their
RT   adducts with isoform II: engineering proton-transfer processes within the
RT   active site of an enzyme.";
RL   Chemistry 12:7057-7066(2006).
RN   [7]
RP   ACTIVITY REGULATION.
RX   PubMed=16686544; DOI=10.1021/jm0603320;
RA   Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT   "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII,
RT   and XIV with L- and D-phenylalanine and crystallographic analysis of their
RT   adducts with isozyme II: stereospecific recognition within the active site
RT   of an enzyme and its consequences for the drug design.";
RL   J. Med. Chem. 49:3019-3027(2006).
RN   [8]
RP   ACTIVITY REGULATION.
RX   PubMed=17705204; DOI=10.1002/anie.200701189;
RA   Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A.,
RA   Supuran C.T., Klebe G.;
RT   "Saccharin inhibits carbonic anhydrases: possible explanation for its
RT   unpleasant metallic aftertaste.";
RL   Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
RN   [9]
RP   ACTIVITY REGULATION.
RX   PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027;
RA   Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.;
RT   "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance
RT   of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.";
RL   Bioorg. Med. Chem. Lett. 17:628-635(2007).
RN   [10]
RP   ACTIVITY REGULATION.
RX   PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
RA   Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
RA   Supuran C.T.;
RT   "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray
RT   crystal structure of the antiviral drug foscarnet complexed to human
RT   carbonic anhydrase I.";
RL   Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
RN   [11]
RP   ACTIVITY REGULATION.
RX   PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA   Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA   Muehlschlegel F.A., Supuran C.T.;
RT   "A thiabendazole sulfonamide shows potent inhibitory activity against
RT   mammalian and nematode alpha-carbonic anhydrases.";
RL   Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN   [12]
RP   ACTIVITY REGULATION.
RX   PubMed=19206230; DOI=10.1021/ja809683v;
RA   Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA   Quinn R.J., Supuran C.T.;
RT   "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT   class of suicide inhibitors.";
RL   J. Am. Chem. Soc. 131:3057-3062(2009).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 5-262 IN COMPLEX WITH ZINC IONS.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human carbonic anhydrase VII [isoform 1], CA7.";
RL   Submitted (JUN-2010) to the PDB data bank.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.13};
CC   -!- ACTIVITY REGULATION: Activated by histamine, L-adrenaline, L- and D-
CC       histidine, and L- and D-phenylalanine. Inhibited by coumarins,
CC       sulfonamide derivatives such as acetazolamide (AZA), by saccharin and
CC       Foscarnet (phosphonoformate trisodium salt).
CC       {ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16807956,
CC       ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17314045,
CC       ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:19186056,
CC       ECO:0000269|PubMed:19206230}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P43166-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P43166-2; Sequence=VSP_044254;
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M76423; AAA51923.1; -; Genomic_DNA.
DR   EMBL; M76420; AAA51923.1; JOINED; Genomic_DNA.
DR   EMBL; M76421; AAA51923.1; JOINED; Genomic_DNA.
DR   EMBL; M76422; AAA51923.1; JOINED; Genomic_DNA.
DR   EMBL; AY075019; AAL78167.1; -; mRNA.
DR   EMBL; AY075020; AAL78168.1; -; mRNA.
DR   EMBL; AC004638; AAC23785.1; -; Genomic_DNA.
DR   EMBL; AC044802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471092; EAW83047.1; -; Genomic_DNA.
DR   EMBL; BC033865; AAH33865.1; -; mRNA.
DR   CCDS; CCDS10821.1; -. [P43166-1]
DR   CCDS; CCDS42173.1; -. [P43166-2]
DR   PIR; A55272; CRHU7.
DR   RefSeq; NP_001014435.1; NM_001014435.1. [P43166-2]
DR   RefSeq; NP_005173.1; NM_005182.2. [P43166-1]
DR   RefSeq; XP_005256193.1; XM_005256136.3.
DR   RefSeq; XP_011521614.1; XM_011523312.1. [P43166-2]
DR   PDB; 3MDZ; X-ray; 2.32 A; A=5-262.
DR   PDB; 3ML5; X-ray; 2.05 A; A=1-264.
DR   PDB; 6G4T; X-ray; 1.91 A; A=1-264.
DR   PDB; 6H36; X-ray; 1.85 A; A=1-264.
DR   PDB; 6H37; X-ray; 1.90 A; A=1-264.
DR   PDB; 6H38; X-ray; 1.70 A; A=1-264.
DR   PDB; 6SDT; X-ray; 1.94 A; A=1-264.
DR   PDB; 6ZR9; X-ray; 2.05 A; A=1-264.
DR   PDB; 7NC4; X-ray; 1.60 A; A=1-264.
DR   PDB; 7P1A; X-ray; 1.58 A; A=1-264.
DR   PDBsum; 3MDZ; -.
DR   PDBsum; 3ML5; -.
DR   PDBsum; 6G4T; -.
DR   PDBsum; 6H36; -.
DR   PDBsum; 6H37; -.
DR   PDBsum; 6H38; -.
DR   PDBsum; 6SDT; -.
DR   PDBsum; 6ZR9; -.
DR   PDBsum; 7NC4; -.
DR   PDBsum; 7P1A; -.
DR   AlphaFoldDB; P43166; -.
DR   SMR; P43166; -.
DR   STRING; 9606.ENSP00000345659; -.
DR   BindingDB; P43166; -.
DR   ChEMBL; CHEMBL2326; -.
DR   DrugBank; DB00819; Acetazolamide.
DR   DrugBank; DB00562; Benzthiazide.
DR   DrugBank; DB00606; Cyclothiazide.
DR   DrugBank; DB01144; Diclofenamide.
DR   DrugBank; DB08846; Ellagic acid.
DR   DrugBank; DB00311; Ethoxzolamide.
DR   DrugBank; DB00774; Hydroflumethiazide.
DR   DrugBank; DB00703; Methazolamide.
DR   DrugBank; DB00909; Zonisamide.
DR   DrugCentral; P43166; -.
DR   GuidetoPHARMACOLOGY; 2749; -.
DR   iPTMnet; P43166; -.
DR   PhosphoSitePlus; P43166; -.
DR   BioMuta; CA7; -.
DR   DMDM; 1168744; -.
DR   MassIVE; P43166; -.
DR   PaxDb; P43166; -.
DR   PeptideAtlas; P43166; -.
DR   PRIDE; P43166; -.
DR   ProteomicsDB; 55595; -. [P43166-1]
DR   ProteomicsDB; 70472; -.
DR   Antibodypedia; 29327; 135 antibodies from 27 providers.
DR   DNASU; 766; -.
DR   Ensembl; ENST00000338437.7; ENSP00000345659.2; ENSG00000168748.14. [P43166-1]
DR   Ensembl; ENST00000394069.3; ENSP00000377632.3; ENSG00000168748.14. [P43166-2]
DR   GeneID; 766; -.
DR   KEGG; hsa:766; -.
DR   MANE-Select; ENST00000338437.7; ENSP00000345659.2; NM_005182.3; NP_005173.1.
DR   UCSC; uc002eqi.4; human. [P43166-1]
DR   CTD; 766; -.
DR   DisGeNET; 766; -.
DR   GeneCards; CA7; -.
DR   HGNC; HGNC:1381; CA7.
DR   HPA; ENSG00000168748; Tissue enriched (intestine).
DR   MIM; 114770; gene.
DR   neXtProt; NX_P43166; -.
DR   OpenTargets; ENSG00000168748; -.
DR   PharmGKB; PA25996; -.
DR   VEuPathDB; HostDB:ENSG00000168748; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000159757; -.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; P43166; -.
DR   OMA; RMRMENN; -.
DR   OrthoDB; 1377476at2759; -.
DR   PhylomeDB; P43166; -.
DR   TreeFam; TF316425; -.
DR   BRENDA; 4.2.1.1; 2681.
DR   PathwayCommons; P43166; -.
DR   Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR   SABIO-RK; P43166; -.
DR   BioGRID-ORCS; 766; 20 hits in 1069 CRISPR screens.
DR   ChiTaRS; CA7; human.
DR   GeneWiki; Carbonic_anhydrase_7; -.
DR   GenomeRNAi; 766; -.
DR   Pharos; P43166; Tclin.
DR   PRO; PR:P43166; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P43166; protein.
DR   Bgee; ENSG00000168748; Expressed in mucosa of transverse colon and 72 other tissues.
DR   ExpressionAtlas; P43166; baseline and differential.
DR   Genevisible; P43166; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0004089; F:carbonate dehydratase activity; TAS:ProtInc.
DR   GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR   GO; GO:0032849; P:positive regulation of cellular pH reduction; IEA:Ensembl.
DR   GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR   GO; GO:2001225; P:regulation of chloride transport; IEA:Ensembl.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   CDD; cd03149; alpha_CA_VII; 1.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR041890; Alpha_CA_VII.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Lyase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..264
FT                   /note="Carbonic anhydrase 7"
FT                   /id="PRO_0000077431"
FT   DOMAIN          5..262
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        66
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|Ref.13"
FT   BINDING         201..202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   VAR_SEQ         1..56
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_044254"
FT   TURN            11..13
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           15..20
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          90..99
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          117..125
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   TURN            127..129
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           133..136
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          142..154
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           159..165
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          193..198
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          209..216
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   HELIX           222..228
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:7P1A"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:7P1A"
SQ   SEQUENCE   264 AA;  29658 MW;  7AD559FC6E07EF96 CRC64;
     MTGHHGWGYG QDDGPSHWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE LSYEACMSLS
     ITNNGHSVQV DFNDSDDRTV VTGGPLEGPY RLKQFHFHWG KKHDVGSEHT VDGKSFPSEL
     HLVHWNAKKY STFGEAASAP DGLAVVGVFL ETGDEHPSMN RLTDALYMVR FKGTKAQFSC
     FNPKCLLPAS RHYWTYPGSL TTPPLSESVT WIVLREPICI SERQMGKFRS LLFTSEDDER
     IHMVNNFRPP QPLKGRVVKA SFRA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024