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Protein

Carbonic anhydrase 2

Gene

CA2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide.By similarity

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Proton acceptorBy similarity
Active sitei67 – 671By similarity
Metal bindingi94 – 941Zinc; catalytic
Metal bindingi96 – 961Zinc; catalytic
Metal bindingi119 – 1191Zinc; catalytic
Active sitei127 – 1271By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 2 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase II
Short name:
CA-II
Gene namesi
Name:CA2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 260259Carbonic anhydrase 2PRO_0000077417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00921.
PRIDEiP00921.

Interactioni

Subunit structurei

Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity (By similarity).By similarity

Protein-protein interaction databases

IntActiP00921. 1 interaction.
STRINGi9913.ENSBTAP00000023581.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 113Combined sources
Helixi13 – 153Combined sources
Turni16 – 194Combined sources
Helixi21 – 244Combined sources
Beta strandi25 – 273Combined sources
Beta strandi31 – 333Combined sources
Helixi35 – 373Combined sources
Beta strandi47 – 504Combined sources
Beta strandi56 – 616Combined sources
Beta strandi63 – 708Combined sources
Beta strandi73 – 819Combined sources
Beta strandi88 – 9710Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi115 – 12410Combined sources
Helixi125 – 1273Combined sources
Helixi130 – 1334Combined sources
Beta strandi139 – 15113Combined sources
Helixi154 – 1607Combined sources
Helixi161 – 1666Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi172 – 1743Combined sources
Helixi180 – 1834Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi206 – 2138Combined sources
Beta strandi215 – 2173Combined sources
Helixi219 – 2257Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi256 – 2583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6VX-ray3.50A1-254[»]
1V9EX-ray1.95A/B2-260[»]
1V9IX-ray2.95C2-260[»]
4CNRX-ray2.29A/B/C/D1-260[»]
4CNVX-ray1.62A1-260[»]
4CNWX-ray2.03A/B1-260[»]
4CNXX-ray1.23A1-260[»]
5A25X-ray1.90A/B1-260[»]
ProteinModelPortaliP00921.
SMRiP00921. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00921.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 1992Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP00921.
KOiK18245.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF90. PTHR18952:SF90. 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.

P00921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHHWGYGKH NGPEHWHKDF PIANGERQSP VDIDTKAVVQ DPALKPLALV
60 70 80 90 100
YGEATSRRMV NNGHSFNVEY DDSQDKAVLK DGPLTGTYRL VQFHFHWGSS
110 120 130 140 150
DDQGSEHTVD RKKYAAELHL VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG
160 170 180 190 200
DANPALQKVL DALDSIKTKG KSTDFPNFDP GSLLPNVLDY WTYPGSLTTP
210 220 230 240 250
PLLESVTWIV LKEPISVSSQ QMLKFRTLNF NAEGEPELLM LANWRPAQPL
260
KNRQVRGFPK
Length:260
Mass (Da):29,114
Last modified:January 23, 2007 - v3
Checksum:iA89412C23FFD19A7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571R → Q in one of the major forms.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY240020 mRNA. Translation: AAO85140.1.
BC103260 mRNA. Translation: AAI03261.1.
PIRiA01144. CRBO2.
RefSeqiNP_848667.1. NM_178572.2.
UniGeneiBt.49731.

Genome annotation databases

GeneIDi280740.
KEGGibta:280740.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY240020 mRNA. Translation: AAO85140.1.
BC103260 mRNA. Translation: AAI03261.1.
PIRiA01144. CRBO2.
RefSeqiNP_848667.1. NM_178572.2.
UniGeneiBt.49731.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6VX-ray3.50A1-254[»]
1V9EX-ray1.95A/B2-260[»]
1V9IX-ray2.95C2-260[»]
4CNRX-ray2.29A/B/C/D1-260[»]
4CNVX-ray1.62A1-260[»]
4CNWX-ray2.03A/B1-260[»]
4CNXX-ray1.23A1-260[»]
5A25X-ray1.90A/B1-260[»]
ProteinModelPortaliP00921.
SMRiP00921. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00921. 1 interaction.
STRINGi9913.ENSBTAP00000023581.

Chemistry

BindingDBiP00921.
ChEMBLiCHEMBL2096971.

Proteomic databases

PaxDbiP00921.
PRIDEiP00921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280740.
KEGGibta:280740.

Organism-specific databases

CTDi760.

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP00921.
KOiK18245.

Miscellaneous databases

EvolutionaryTraceiP00921.
NextBioi20804911.
PROiP00921.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF90. PTHR18952:SF90. 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. "Full length cDNA of bovine carbonic anhydrase II."
    Daigle R., Castro I., Desrochers M., Charest P.-M.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone marrow.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.
  3. "Primary structure of bovine erythrocyte carbonic carbonic anhydrase CI. II. Complete sequence."
    Sciaky M., Limozin N., Filippi-Foveau D., Gulian J.M., Laurent-Tabusse G.
    Biochimie 58:1071-1082(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-260.
    Tissue: Erythrocyte.
  4. "Genetic independence of two forms of carbonic anhydrase from bovine erythrocytes."
    Gulian J.M., Limozin N., Mallet B., di Costanzo J., Charrel M.
    Biochimie 59:293-302(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "Structure of bovine carbonic anhydrase II at 1.95 A resolution."
    Saito R., Sato T., Ikai A., Tanaka N.
    Acta Crystallogr. D 60:792-795(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION.
  6. "Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody."
    Desmyter A., Decanniere K., Muyldermans S., Wyns L.
    J. Biol. Chem. 276:26285-26290(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-254 IN COMPLEX WITH ANTIBODY.

Entry informationi

Entry nameiCAH2_BOVIN
AccessioniPrimary (citable) accession number: P00921
Secondary accession number(s): Q3ZBJ5, Q865Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

One minor and two major forms were isolated chromatographically.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.