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UniProtKB/Swiss-Prot entry P00915


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAH1_HUMAN
Primary accession number P00915
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 100)
Name and origin of the protein
Protein name Carbonic anhydrase 1
Synonyms EC 4.2.1.1
Carbonic anhydrase I
CA-I
Carbonate dehydratase I
Carbonic anhydrase B
CAB
Gene name
Name: CA1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/15.5.2386; PubMed=3104879 [NCBI, ExPASy, EBI, Israel, Japan]
Barlow J.H., Lowe N., Edwards Y.H., Butterworth P.H.W.;
"Human carbonic anhydrase I cDNA.";
Nucleic Acids Res. 15:2386-2386(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(90)90236-K; PubMed=2121614 [NCBI, ExPASy, EBI, Israel, Japan]
Lowe N., Brady H.J.M., Barlow J.H., Sowden J.C., Edwards M., Butterworth P.H.W.;
"Structure and methylation patterns of the gene encoding human carbonic anhydrase I.";
Gene 93:277-283(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Spleen;
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).
[4]
PROTEIN SEQUENCE OF 2-261.
PubMed=4217196 [NCBI, ExPASy, EBI, Israel, Japan]
Giraud N., Marriq C., Laurent-Tabusse G.;
"Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260).";
Biochimie 56:1031-1043(1974).
[5]
PROTEIN SEQUENCE OF 20-261.
DOI=10.1016/0006-291X(72)90400-7; PubMed=4625868 [NCBI, ExPASy, EBI, Israel, Japan]
Andersson B., Nyman P.O., Strid L.;
"Amino acid sequence of human erythrocyte carbonic anhydrase B.";
Biochem. Biophys. Res. Commun. 48:670-677(1972).
[6]
PROTEIN SEQUENCE OF 12-261.
PubMed=4632246 [NCBI, ExPASy, EBI, Israel, Japan]
Lin K.-T.D., Deutsch H.F.;
"Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B.";
J. Biol. Chem. 248:1885-1893(1973).
[7]
SEQUENCE REVISION.
PubMed=4207120 [NCBI, ExPASy, EBI, Israel, Japan]
Lin K.-T.D., Deutsch H.F.;
"Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.";
J. Biol. Chem. 249:2329-2337(1974).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=804171 [NCBI, ExPASy, EBI, Israel, Japan]
Kannan K.K., Notstrand B., Fridborg K., Loevgren S., Ohlsson A., Petef M.;
"Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 72:51-55(1975).
[9]
VARIANT GUAM ARG-254.
PubMed=6781336 [NCBI, ExPASy, EBI, Israel, Japan]
Omoto K., Ueda S., Goriki K., Takahashi N., Misawa S., Pagaran I.G.;
"Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam.";
Am. J. Hum. Genet. 33:105-111(1981).
[10]
VARIANT MICHIGAN-1 ARG-68.
PubMed=7866410 [NCBI, ExPASy, EBI, Israel, Japan]
Chegwidden W.R., Wagner L.E., Venta P.J., Bergenhem N.C.H., Yu Y.-S.L., Tashian R.E.;
"Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I.";
Hum. Mutat. 4:294-296(1994).
Comments
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
X05014; CAA28663.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33987; AAA51910.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027890; AAH27890.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0786; CRHU1.
RefSeq NP_001122301.1; -.
NP_001122302.1; -.
NP_001122303.1; -.
NP_001729.1; -.
UniGene Hs.23118
3D structure databases
PDB
1AZM; X-ray; 2.00 A; A=1-261.[ExPASy / RCSB / EBI]
1BZM; X-ray; 2.00 A; A=1-261.[ExPASy / RCSB / EBI]
1CRM; X-ray; 2.00 A; A=1-261.[ExPASy / RCSB / EBI]
1CZM; X-ray; 2.00 A; A=1-261.[ExPASy / RCSB / EBI]
1HCB; X-ray; 1.60 A; A=1-261.[ExPASy / RCSB / EBI]
1HUG; X-ray; 2.00 A; A=1-261.[ExPASy / RCSB / EBI]
1HUH; X-ray; 2.20 A; A=1-261.[ExPASy / RCSB / EBI]
1J9W; X-ray; 2.60 A; A/B=1-261.[ExPASy / RCSB / EBI]
1JV0; X-ray; 2.00 A; A/B=1-261.[ExPASy / RCSB / EBI]
2CAB; X-ray; 2.00 A; A=1-261.[ExPASy / RCSB / EBI]
2FOY; X-ray; 1.55 A; A/B=1-261.[ExPASy / RCSB / EBI]
2FW4; X-ray; 2.00 A; A/B=2-261.[ExPASy / RCSB / EBI]
2IT4; X-ray; 2.00 A; A/B=6-261.[ExPASy / RCSB / EBI]
2NMX; X-ray; 1.55 A; A/B=2-261.[ExPASy / RCSB / EBI]
2NN1; X-ray; 1.65 A; A/B=2-261.[ExPASy / RCSB / EBI]
2NN7; X-ray; 1.85 A; A/B=2-261.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AZM; -.
1BZM; -.
1CRM; -.
1CZM; -.
1HCB; -.
1HUG; -.
1HUH; -.
1J9W; -.
1JV0; -.
2CAB; -.
2FOY; -.
2FW4; -.
2IT4; -.
2NMX; -.
2NN1; -.
2NN7; -.
ModBase P00915.
2D gel databases
DOSAC-COBS-2DPAGE P00915; -.
PMMA-2DPAGE P00915; -.
REPRODUCTION-2DPAGE IPI00215983; -.
P00915; -.
Organism-specific databases
H-InvDB HIX0007626; -.
HGNC HGNC:1368; CA1.
GenAtlas CA1.
HPA HPA006558; -.
MIM 114800; gene. [NCBI / EBI]
PharmGKB PA24373; -.
GeneCards P00915.
Gene expression databases
ArrayExpress P00915; -.
CleanEx HS_CA1; -.
GermOnline ENSG00000133742; Homo sapiens.
Ontologies
GO
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from HPA).
GO:0004089; Molecular function: carbonate dehydratase activity (traceable author statement from ProtInc).
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).
BLOCKS P00915.
ProtoNet P00915.
Proteomic databases
PeptideAtlas P00915; -.
Genome annotation databases
Ensembl ENSG00000133742; Homo sapiens. [Contig view]
GeneID 759; -.
KEGG hsa:759; -.
Phylogenomic databases
HOGENOM P00915; -.
HOVERGEN P00915; -.
Other
BindingDB P00915; -.
DrugBank DB00819; Acetazolamide.
DB00381; Amlodipine.
DB00436; Bendroflumethiazide.
DB00562; Benzthiazide.
DB01194; Brinzolamide.
DB00880; Chlorothiazide.
DB00606; Cyclothiazide.
DB01119; Diazoxide.
DB01144; Dichlorphenamide.
DB01031; Ethinamate.
DB00311; Ethoxzolamide.
DB00999; Hydrochlorothiazide.
DB00774; Hydroflumethiazide.
DB01202; Levetiracetam.
DB00703; Methazolamide.
DB00232; Methyclothiazide.
DB01325; Quinethazone.
DB01021; Trichlormethiazide.
DB00661; Verapamil.
DB00909; Zonisamide.
LinkHub P00915; -.
NextBio 3070; -.
SOURCE CA1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lyase; Metal-binding; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   261  260     Carbonic anhydrase 1. PRO_0000077409
METAL   95    95        Zinc; catalytic. 
METAL   97    97        Zinc; catalytic. 
METAL   120   120        Zinc; catalytic. 
MOD_RES   2     2        N-acetylalanine. 
VARIANT   68    68  1     H -> R (in Michigan-1). VAR_001378 [3D]
VARIANT   254   254  1     G -> R (in Guam). VAR_001379 [3D]
CONFLICT   75    76        DN -> ND (in Ref. 4; AA sequence and 5; AA sequence). 
TURN   10    12  3      
TURN   14    16  3      
HELIX   17    19  3      
HELIX   22    25  4      
HELIX   36    38  3      
STRAND   48    51  4      
HELIX   54    56  3      
STRAND   57    62  6      
STRAND   64    71  8      
STRAND   74    82  9      
STRAND   89    98  10      
STRAND   100   104  5      
STRAND   107   110  4      
STRAND   116   125  10      
TURN   126   128  3      
HELIX   132   135  4      
STRAND   141   153  13      
HELIX   156   158  3      
HELIX   159   164  6      
HELIX   165   168  4      
STRAND   174   176  3      
HELIX   182   185  4      
STRAND   192   197  6      
STRAND   208   215  8      
STRAND   217   219  3      
HELIX   221   227  7      
STRAND   230   233  4      
Sequence information
Length: 261 AA [This is the length of the unprocessed precursor] Molecular weight: 28870 Da [This is the MW of the unprocessed precursor] CRC64: 4959E5FA25E374F8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI 

        70         80         90        100        110        120 
INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH 

       130        140        150        160        170        180 
VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF 

       190        200        210        220        230        240 
DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV 

       250        260 
PMQHNNRPTQ PLKGRTVRAS F 

P00915 in FASTA format

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