SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07630

- CAH2_CHICK

UniProt

P07630 - CAH2_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Carbonic anhydrase 2
Gene
CA2
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Inhibited by acetazolamide By similarity.

Sites

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

GO - Molecular functioni

  1. carbonate dehydratase activity Source: UniProtKB-EC
  2. zinc ion binding Source: Ensembl

GO - Biological processi

  1. angiotensin-activated signaling pathway Source: Ensembl
  2. carbon dioxide transport Source: Ensembl
  3. morphogenesis of an epithelium Source: Ensembl
  4. one-carbon metabolic process Source: InterPro
  5. positive regulation of dipeptide transmembrane transport Source: Ensembl
  6. regulation of anion transport Source: Ensembl
  7. regulation of intracellular pH Source: Ensembl
  8. secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_197145. Erythrocytes take up carbon dioxide and release oxygen.
REACT_197148. Reversible hydration of carbon dioxide.
REACT_197150. Erythrocytes take up oxygen and release carbon dioxide.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 2

Subcellular locationi

Cytoplasm. Cell membrane By similarity

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Ensembl
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiP07630.
PRIDEiP07630.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025525.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103
Turni12 – 143
Helixi15 – 184
Helixi20 – 234
Turni34 – 363
Beta strandi37 – 393
Beta strandi46 – 494
Beta strandi55 – 606
Beta strandi65 – 695
Beta strandi72 – 809
Beta strandi87 – 9610
Beta strandi105 – 1084
Beta strandi114 – 12310
Helixi124 – 1263
Helixi129 – 1324
Beta strandi138 – 15013
Helixi153 – 1553
Helixi156 – 1616
Turni162 – 1654
Beta strandi171 – 1733
Helixi179 – 1824
Beta strandi189 – 1946
Beta strandi205 – 2128
Beta strandi214 – 2163
Helixi218 – 2247
Beta strandi228 – 2303
Beta strandi255 – 2573

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q4Imodel-A1-260[»]
ProteinModelPortaliP07630.
SMRiP07630. Positions 2-260.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00750000117305.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP07630.
KOiK18245.
OMAiNDENESH.
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

MSHHWGYDSH NGPAHWHEHF PIANGERQSP IAISTKAARY DPALKPLSFS    50
YDAGTAKAIV NNGHSFNVEF DDSSDKSVLQ GGALDGVYRL VQFHIHWGSC 100
EGQGSEHTVD GVKYDAELHI VHWNVKYGKF AEALKHPDGL AVVGIFMKVG 150
NAKPEIQKVV DALNSIQTKG KQASFTNFDP TGLLPPCRDY WTYPGSLTTP 200
PLHECVIWHV LKEPITVSSE QMCKLRGLCF SAENEPVCRM VDNWRPCQPL 250
KSREVRASFQ 260
Length:260
Mass (Da):29,008
Last modified:January 23, 2007 - v3
Checksum:i6723309BC77A4950
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51W → L in CAA28501. 1 Publication
Sequence conflicti8 – 81D → G in AAA48646. 1 Publication
Sequence conflicti87 – 871V → S in AAA48646. 1 Publication
Sequence conflicti250 – 2501L → V in CAA31175. 1 Publication
Sequence conflicti250 – 2501L → V in CAA29417. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi JC2580.
RefSeqi NP_990648.1. NM_205317.1.
UniGenei Gga.3986.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q4I model - A 1-260 [» ]
ProteinModelPortali P07630.
SMRi P07630. Positions 2-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000025525.

Proteomic databases

PaxDbi P07630.
PRIDEi P07630.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000025572 ; ENSGALP00000025525 ; ENSGALG00000015862 .
GeneIDi 396257.
KEGGi gga:396257.

Organism-specific databases

CTDi 760.

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00750000117305.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P07630.
KOi K18245.
OMAi NDENESH.
OrthoDBi EOG7WMCK7.
PhylomeDBi P07630.
TreeFami TF316425.

Enzyme and pathway databases

Reactomei REACT_197145. Erythrocytes take up carbon dioxide and release oxygen.
REACT_197148. Reversible hydration of carbon dioxide.
REACT_197150. Erythrocytes take up oxygen and release carbon dioxide.

Miscellaneous databases

NextBioi 20816309.
PROi P07630.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF90. PTHR18952:SF90. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 127 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