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Protein

Carbonic anhydrase 2

Gene

CA2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

Enzyme and pathway databases

ReactomeiREACT_292774. Erythrocytes take up oxygen and release carbon dioxide.
REACT_317819. Reversible hydration of carbon dioxide.
REACT_332034. Erythrocytes take up carbon dioxide and release oxygen.

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 260259Carbonic anhydrase 2PRO_0000077423Add
BLAST

Proteomic databases

PaxDbiP07630.
PRIDEiP07630.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025525.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q4Imodel-A1-260[»]
ProteinModelPortaliP07630.
SMRiP07630. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP07630.
KOiK18245.
OMAiHFVHADK.
OrthoDBiEOG7WMCK7.
PhylomeDBiP07630.
TreeFamiTF316425.

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.

P07630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHHWGYDSH NGPAHWHEHF PIANGERQSP IAISTKAARY DPALKPLSFS
60 70 80 90 100
YDAGTAKAIV NNGHSFNVEF DDSSDKSVLQ GGALDGVYRL VQFHIHWGSC
110 120 130 140 150
EGQGSEHTVD GVKYDAELHI VHWNVKYGKF AEALKHPDGL AVVGIFMKVG
160 170 180 190 200
NAKPEIQKVV DALNSIQTKG KQASFTNFDP TGLLPPCRDY WTYPGSLTTP
210 220 230 240 250
PLHECVIWHV LKEPITVSSE QMCKLRGLCF SAENEPVCRM VDNWRPCQPL
260
KSREVRASFQ
Length:260
Mass (Da):29,008
Last modified:January 23, 2007 - v3
Checksum:i6723309BC77A4950
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51W → L in CAA28501 (PubMed:3102231).Curated
Sequence conflicti8 – 81D → G in AAA48646 (PubMed:6331256).Curated
Sequence conflicti87 – 871V → S in AAA48646 (PubMed:6331256).Curated
Sequence conflicti250 – 2501L → V in CAA31175 (PubMed:3029691).Curated
Sequence conflicti250 – 2501L → V in CAA29417 (PubMed:3029691).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14957 mRNA. Translation: CAA78681.1.
X12639 mRNA. Translation: CAA31175.1.
X06000
, X06001, X06002, X06003, X06004, X06005 Genomic DNA. Translation: CAA29417.1.
X04810 mRNA. Translation: CAA28501.1.
X17378 mRNA. Translation: CAA35250.1.
M25943 mRNA. Translation: AAA48646.1.
PIRiJC2580.
RefSeqiNP_990648.1. NM_205317.1.
UniGeneiGga.3986.

Genome annotation databases

EnsembliENSGALT00000025572; ENSGALP00000025525; ENSGALG00000015862.
GeneIDi396257.
KEGGigga:396257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14957 mRNA. Translation: CAA78681.1.
X12639 mRNA. Translation: CAA31175.1.
X06000
, X06001, X06002, X06003, X06004, X06005 Genomic DNA. Translation: CAA29417.1.
X04810 mRNA. Translation: CAA28501.1.
X17378 mRNA. Translation: CAA35250.1.
M25943 mRNA. Translation: AAA48646.1.
PIRiJC2580.
RefSeqiNP_990648.1. NM_205317.1.
UniGeneiGga.3986.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q4Imodel-A1-260[»]
ProteinModelPortaliP07630.
SMRiP07630. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025525.

Proteomic databases

PaxDbiP07630.
PRIDEiP07630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000025572; ENSGALP00000025525; ENSGALG00000015862.
GeneIDi396257.
KEGGigga:396257.

Organism-specific databases

CTDi760.

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP07630.
KOiK18245.
OMAiHFVHADK.
OrthoDBiEOG7WMCK7.
PhylomeDBiP07630.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_292774. Erythrocytes take up oxygen and release carbon dioxide.
REACT_317819. Reversible hydration of carbon dioxide.
REACT_332034. Erythrocytes take up carbon dioxide and release oxygen.

Miscellaneous databases

NextBioi20816309.
PROiP07630.

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

  1. "A novel carbonic anhydrase II mRNA isolated from mature chicken testis displays a TATA box and other promoter sequences in a leader 5' untranslated region not present in somatic tissues."
    Mezquita J., Pau M., Mezquita C.
    Gene 147:231-235(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Hubbard White Mountain.
    Tissue: Testis.
  2. "The chicken carbonic anhydrase II gene: evidence for a recent shift in intron position."
    Yoshihara C.M., Lee J.-D., Dodgson J.B.
    Nucleic Acids Res. 15:753-770(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: White leghorn.
  3. "Sequence of carbonic anhydrase II cDNA from chick retina."
    Rogers J.H.
    Eur. J. Biochem. 162:119-122(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-260.
    Strain: White leghorn.
    Tissue: Retina.
  4. "Utilization of the second polyadenylation signal at the 3' end of the chicken carbonic anhydrase II gene."
    Godbout R., Andison R., Upton C., Day R.
    Nucleic Acids Res. 18:1049-1049(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 222-260.
    Tissue: Retina.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-87.

Entry informationi

Entry nameiCAH2_CHICK
AccessioniPrimary (citable) accession number: P07630
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.