Carbonic anhydrase 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P00915 (CAH1_HUMAN)

Last modified September 2, 2008. Version 99. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Carbonic anhydrase 1
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase I
      Short name=CA-I
    Carbonate dehydratase I
    Carbonic anhydrase B
      Short name=CAB

Gene names

Name:

CA1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H(2)CO(3) = CO(2) + H(2)O.
Cofactor	Zinc.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	carbonate dehydratase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

Removed

Chain

2 – 261

260

Carbonic anhydrase 1

Sites

Metal binding

Zinc; catalytic

Metal binding

Zinc; catalytic

Metal binding

120

Zinc; catalytic

Amino acid modifications

Modified residue

N-acetylalanine

Natural variations

Natural variant

H → R in Michigan-1.

Natural variant

254

G → R in Guam.

Experimental info

Sequence conflict

75 – 76

DN → ND AA sequence Ref.4

Sequence conflict

75 – 76

DN → ND AA sequence Ref.5

Secondary structure

261

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00915-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4959E5FA25E374F8
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FASTA

261

28,870

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human carbonic anhydrase I cDNA." Barlow J.H., Lowe N., Edwards Y.H., Butterworth P.H.W. Nucleic Acids Res. 15:2386-2386(1987) [PubMed: 3104879] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and methylation patterns of the gene encoding human carbonic anhydrase I." Lowe N., Brady H.J.M., Barlow J.H., Sowden J.C., Edwards M., Butterworth P.H.W. Gene 93:277-283(1990) [PubMed: 2121614] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Spleen.
[4]	"Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)." Giraud N., Marriq C., Laurent-Tabusse G. Biochimie 56:1031-1043(1974) [PubMed: 4217196] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-261.
[5]	"Amino acid sequence of human erythrocyte carbonic anhydrase B." Andersson B., Nyman P.O., Strid L. Biochem. Biophys. Res. Commun. 48:670-677(1972) [PubMed: 4625868] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-261.
[6]	"Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B." Lin K.-T.D., Deutsch H.F. J. Biol. Chem. 248:1885-1893(1973) [PubMed: 4632246] [Abstract] Cited for: PROTEIN SEQUENCE OF 12-261.
[7]	"Human carbonic anhydrases. XII. The complete primary structure of the C isozyme." Lin K.-T.D., Deutsch H.F. J. Biol. Chem. 249:2329-2337(1974) [PubMed: 4207120] [Abstract] Cited for: SEQUENCE REVISION.
[8]	"Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution." Kannan K.K., Notstrand B., Fridborg K., Loevgren S., Ohlsson A., Petef M. Proc. Natl. Acad. Sci. U.S.A. 72:51-55(1975) [PubMed: 804171] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[9]	"Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam." Omoto K., Ueda S., Goriki K., Takahashi N., Misawa S., Pagaran I.G. Am. J. Hum. Genet. 33:105-111(1981) [PubMed: 6781336] [Abstract] Cited for: VARIANT GUAM ARG-254.
[10]	"Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I." Chegwidden W.R., Wagner L.E., Venta P.J., Bergenhem N.C.H., Yu Y.-S.L., Tashian R.E. Hum. Mutat. 4:294-296(1994) [PubMed: 7866410] [Abstract] Cited for: VARIANT MICHIGAN-1 ARG-68.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X05014 mRNA. Translation: CAA28663.1.
M33987 mRNA. Translation: AAA51910.1.
BC027890 mRNA. Translation: AAH27890.1.

PIR

CRHU1. JQ0786.

RefSeq

NP_001122301.1.
NP_001122302.1.
NP_001122303.1.
NP_001729.1.

UniGene

Hs.23118

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AZM	X-ray	2.00	A	1-261	[»]
1BZM	X-ray	2.00	A	1-261	[»]
1CRM	X-ray	2.00	A	1-261	[»]
1CZM	X-ray	2.00	A	1-261	[»]
1HCB	X-ray	1.60	A	1-261	[»]
1HUG	X-ray	2.00	A	1-261	[»]
1HUH	X-ray	2.20	A	1-261	[»]
1J9W	X-ray	2.60	A/B	1-261	[»]
1JV0	X-ray	2.00	A/B	1-261	[»]
2CAB	X-ray	2.00	A	1-261	[»]
2FOY	X-ray	1.55	A/B	1-261	[»]
2FW4	X-ray	2.00	A/B	2-261	[»]
2IT4	X-ray	2.00	A/B	6-261	[»]
2NMX	X-ray	1.55	A/B	2-261	[»]
2NN1	X-ray	1.65	A/B	2-261	[»]
2NN7	X-ray	1.85	A/B	2-261	[»]

ModBase

Search...

2-D gel databases

DOSAC-COBS-2DPAGE

P00915.

PMMA-2DPAGE

P00915.

REPRODUCTION-2DPAGE

IPI00215983.
P00915.

Proteomic databases

PeptideAtlas

P00915.

Genome annotation databases

Ensembl

ENSG00000133742. Homo sapiens. [Contig view]

GeneID

759.

KEGG

hsa:759.

Organism-specific databases

H-InvDB

HIX0007626.

HGNC

HGNC:1368. CA1.

HPA

HPA006558.

MIM

114800. gene.

PharmGKB

PA24373.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P00915.

HOVERGEN

P00915.

Gene expression databases

ArrayExpress

P00915.

CleanEx

HS_CA1.

GermOnline

ENSG00000133742. Homo sapiens.

Family and domain databases

InterPro

IPR001148. Euk_COanhd.
[Graphical view]

Gene3D

G3DSA:3.10.200.10. Euk_COanhd. 1 hit.

PANTHER

PTHR18952. Euk_COanhd. 1 hit.

Pfam

PF00194. Carb_anhydrase. 1 hit.
[Graphical view]

ProDom

PD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

BLOCKS

Search...

Other Resources

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.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

CAH1_HUMAN

Accession

Primary (citable) accession number: P00915

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	September 2, 2008
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents