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Reviewed, UniProtKB/Swiss-Prot P07452 (CAH1_RABIT)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 1
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase I
      Short name=CA-I
    Carbonate dehydratase I
Gene names
Name: CA1
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length235 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological processone-carbon compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 235›235Carbonic anhydrase 1
PRO_0000077415

Sites

Metal binding691Zinc; catalytic
Metal binding711Zinc; catalytic
Metal binding941Zinc; catalytic

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P07452-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: D731C5B806867FA2

FASTA23525,696
        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 

« Hide

References

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

Cross-references

Sequence databases

M10412 mRNA. Translation: AAA31183.1.
PIRA22962.
UniGeneOcu.1836

3D structure databases

HSSPHSSP built from PDB template 1HCB based on UniProtKB P00915.
SMRP07452. Positions 1-235.
ModBaseSearch...

Phylogenomic databases

HOVERGENP07452.

Enzyme and pathway databases

BRENDA4.2.1.1. 255.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF30. Carbonic_anhydrase_CA1. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH1_RABIT
AccessionPrimary (citable) accession number: P07452
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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