NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3919381 [NCBI, ExPASy, EBI, Israel, Japan]
Konialis C.P., Barlow J.H., Butterworth P.H.W.;
"Cloned cDNA for rabbit erythrocyte carbonic anhydrase I: a novel erythrocyte-specific probe to study development in erythroid tissues.";
Proc. Natl. Acad. Sci. U.S.A. 82:663-667(1985).

Comments

FUNCTION: Reversible hydration of carbon dioxide.
CATALYTIC ACTIVITY: H₂CO₃ = CO₂ + H₂O.
COFACTOR: Zinc.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the alpha-carbonic anhydrase family.

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

M10412; AAA31183.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A22962; A22962.

UniGene

Ocu.1836

3D structure databases

HSSP

P00915; 1HCB. [HSSP ENTRY / PDB]

SMR

P07452; 1-235.

ModBase

P07452.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004089;	Molecular function: carbonate dehydratase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
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).

Phylogenomic databases

HOVERGEN

P07452; -.

Other

ProtoNet

P07452.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Lyase; Metal-binding; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 235`	`>235`	`Carbonic anhydrase 1.`	`PRO_0000077415`
`METAL`	`69 69`		`Zinc; catalytic.`
`METAL`	`71 71`		`Zinc; catalytic.`
`METAL`	`94 94`		`Zinc; catalytic.`
`NON_TER`	`1 1`

Sequence information

Length: 235 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 25696 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: D731C5B806867FA2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
GNKQSPVDIK SSEVKHDTSL KPFSVSYNPA SAKEIINVGH SFHVNFEDDS QSVLKGGPLS 

        70         80         90        100        110        120 
DNYRLSQFHF HWGKTDDYGS EHTVDGAKFS AELHLVHWNS GKYPNIADSV SKADGLAIVA 

       130        140        150        160        170        180 
VFLKVGQANP KLQKVLDALS AVKTKGKKAS FTNFDPSTLL PPSLDYWTYS GSLTHPPLHE 

       190        200        210        220        230 
SVTWLICKDS ISISSEQLAQ FRSLLSNAEG EAAVPILHNN RPPQPLKGRT VKASF

P07452 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools