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Protein

Carbonic anhydrase 1

Gene

Ca1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.Curated

Catalytic activityi

H2CO3 = CO2 + H2O.By similarity

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Proton acceptorBy similarity
Metal bindingi95 – 951Zinc 1; catalyticBy similarity
Metal bindingi95 – 951Zinc; catalyticBy similarity
Metal bindingi97 – 971Zinc 1; catalyticBy similarity
Metal bindingi97 – 971Zinc; catalyticBy similarity
Metal bindingi120 – 1201Zinc 1; catalyticBy similarity
Metal bindingi120 – 1201Zinc; catalyticBy similarity
Active sitei129 – 1291By similarity
Binding sitei200 – 2001SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-RNO-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-RNO-1475029. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 1By similarity (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IBy similarity
Carbonic anhydrase IBy similarity
Short name:
CA-IBy similarity
Gene namesi
Name:Ca1By similarity
Synonyms:Car1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1309780. Ca1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 261260Carbonic anhydrase 1By similarityPRO_0000349120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiB0BNN3.
PRIDEiB0BNN3.

PTM databases

iPTMnetiB0BNN3.

Expressioni

Gene expression databases

GenevisibleiB0BNN3. RN.

Interactioni

Protein-protein interaction databases

BioGridi259578. 1 interaction.
IntActiB0BNN3. 1 interaction.
STRINGi10116.ENSRNOP00000014267.

Structurei

3D structure databases

ProteinModelPortaliB0BNN3.
SMRiB0BNN3. Positions 2-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 2012Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Sequence analysis

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiB0BNN3.
KOiK01672.
OMAiVTWIICK.
OrthoDBiEOG7WMCK7.
PhylomeDBiB0BNN3.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF82. PTHR18952:SF82. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B0BNN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASADWGYDS KNGPDQWSKL YPIANGNNQS PIDIKTSEAK HDSSLKPVSV
60 70 80 90 100
SYNPATAKEI VNVGHSFHVV FDDSSNQSVL KGGPLADSYR LTQFHFHWGN
110 120 130 140 150
SNDHGSEHTV DGAKYSGELH LVHWNSAKYS SAAEAISKAD GLAIIGVLMK
160 170 180 190 200
VGPANPNLQK VLDALSSVKT KGKRAPFTNF DPSSLLPSSL DYWTYFGSLT
210 220 230 240 250
HPPLHESVTW VICKESISLS PEQLAQLRGL LSSAEGEPAV PVLSNHRPPQ
260
PLKGRTVRAS F
Length:261
Mass (Da):28,300
Last modified:February 26, 2008 - v1
Checksum:iDEF19D7C46E92171
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473961 Genomic DNA. Translation: EDM00961.1.
BC158888 mRNA. Translation: AAI58889.1.
RefSeqiNP_001101130.1. NM_001107660.1.
XP_006232173.1. XM_006232111.1.
XP_008759064.1. XM_008760842.1.
UniGeneiRn.6854.

Genome annotation databases

EnsembliENSRNOT00000014267; ENSRNOP00000014267; ENSRNOG00000010698.
GeneIDi310218.
KEGGirno:310218.
UCSCiRGD:1309780. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473961 Genomic DNA. Translation: EDM00961.1.
BC158888 mRNA. Translation: AAI58889.1.
RefSeqiNP_001101130.1. NM_001107660.1.
XP_006232173.1. XM_006232111.1.
XP_008759064.1. XM_008760842.1.
UniGeneiRn.6854.

3D structure databases

ProteinModelPortaliB0BNN3.
SMRiB0BNN3. Positions 2-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi259578. 1 interaction.
IntActiB0BNN3. 1 interaction.
STRINGi10116.ENSRNOP00000014267.

PTM databases

iPTMnetiB0BNN3.

Proteomic databases

PaxDbiB0BNN3.
PRIDEiB0BNN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014267; ENSRNOP00000014267; ENSRNOG00000010698.
GeneIDi310218.
KEGGirno:310218.
UCSCiRGD:1309780. rat.

Organism-specific databases

CTDi12346.
RGDi1309780. Ca1.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiB0BNN3.
KOiK01672.
OMAiVTWIICK.
OrthoDBiEOG7WMCK7.
PhylomeDBiB0BNN3.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-RNO-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-RNO-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi661732.
PROiB0BNN3.

Gene expression databases

GenevisibleiB0BNN3. RN.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF82. PTHR18952:SF82. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Brown Norway.
    Tissue: LiverImported.
  3. "Proteome profile of the mature rat olfactory bulb."
    Maurya D.K., Sundaram C.S., Bhargava P.
    Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCAH1_RAT
AccessioniPrimary (citable) accession number: B0BNN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 26, 2008
Last modified: January 20, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.