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P00917 (CAH1_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbonic anhydrase 1
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase I
Carbonic anhydrase I
Short name=CA-I
Gene names
Name:CA1
OrganismEquus caballus (Horse) [Complete proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subcellular location

Cytoplasm.

Polymorphism

The sequence shown is that of the electrophoretically homogeneous D isozyme.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 261260Carbonic anhydrase 1
PRO_0000077408

Regions

Region200 – 2012Substrate binding By similarity

Sites

Active site651Proton acceptor By similarity
Active site1291 By similarity
Metal binding951Zinc; catalytic
Metal binding971Zinc; catalytic
Metal binding1201Zinc; catalytic
Binding site2001Substrate By similarity

Natural variations

Natural variant551A → D in isozyme T. Ref.1
Natural variant661S → G in homogeneous D isozyme. Ref.1
Natural variant821D → G in isozyme A2. Ref.1
Natural variant841P → F in isozyme A2. Ref.1
Natural variant1161S → H in homogeneous D isozyme. Ref.1
Natural variant1581L → G in homogeneous D isozyme. Ref.1
Natural variant1841S → R in isozyme A1 and isozyme B. Ref.1
Natural variant2131C → Y in homogeneous D isozyme. Ref.1
Natural variant2231Q → R in isozyme B. Ref.1
Natural variant2251S → A in homogeneous D isozyme. Ref.1

Experimental info

Sequence uncertainty121N or D
Sequence uncertainty251N or D
Sequence uncertainty271N or D
Sequence uncertainty281N or D

Sequences

Sequence LengthMass (Da)Tools
P00917 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E2DD4D1BDAE62353

FASTA26129,025
        10         20         30         40         50         60 
MAHSDWGYDS PNGPZEWVKL YPIANGNNQS PIDIKTSETK HDTSLKPFSV SYDPATAKEI 

        70         80         90        100        110        120 
VNVGHSFQVK FEDSDNRSVL KDGPLPGSYR LVQFHFHWGS TDDYGSEHTV DGVKYSAELH 

       130        140        150        160        170        180 
LVHWNSSKYS SFDEASSQAD GLAILGVLMK VGEANPKLQK VLDALNEVKT KGKKAPFKNF 

       190        200        210        220        230        240 
DPSSLLPSSP DYWTYSGSLT HPPLYESVTW IVCKENISIS SQQLSQFRSL LSNVEGGKAV 

       250        260 
PIQHNNRPPQ PLKGRTVRAF F

« Hide

References

[1]"Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms."
Jabusch J.R., Bray R.P., Deutsch H.F.
J. Biol. Chem. 255:9196-9204(1980) [PubMed: 6773961] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-261, VARIANTS ASP-55; GLY-66; GLY-82; PHE-84; HIS-116; GLY-158; ARG-184; TYR-213; ARG-223 AND ALA-225.

Cross-references

Sequence databases

PIRCRHO1D. A01140.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

GeneTreeENSGT00560000076828.
HOVERGENHBG002837.
InParanoidP00917.
OrthoDBEOG4X97HR.

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
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]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH1_HORSE
AccessionPrimary (citable) accession number: P00917
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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