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CAH3_PIG
ID   CAH3_PIG                Reviewed;         260 AA.
AC   Q5S1S4; Q0Z809;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Carbonic anhydrase 3;
DE            EC=4.2.1.1 {ECO:0000250|UniProtKB:P07451};
DE   AltName: Full=Carbonate dehydratase III;
DE   AltName: Full=Carbonic anhydrase III;
DE            Short=CA-III;
GN   Name=CA3 {ECO:0000303|PubMed:17065793};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17065793; DOI=10.1159/000095232;
RA   Wang H.L., Zhu Z.M., Wang H., Yang S.L., Zhao S.H., Li K.;
RT   "Molecular characterization and association analysis of porcine CA3.";
RL   Cytogenet. Genome Res. 115:129-133(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liu G.Y., Xiong Z.Y.;
RT   "Isolation, prediction of one novel swine gene that is differentially
RT   expressed in the longissimus dorsi muscle tissues from landrace large white
RT   cross combination.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Wu J., Deng C.Y., Xiong Y.Z.;
RT   "Characterization of the porcine carbonic anhydrase III (CA3) mRNA.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wu J., Deng C.Y., Xiong Y.Z., Zhou D.H.;
RT   "Characterization of the porcine carbonic anhydrase III (CA3) gene.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000250|UniProtKB:P07451}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P07451};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P07451};
CC   -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC       {ECO:0000250|UniProtKB:P07451}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07451}.
CC   -!- PTM: S-thiolated both by thiol-disulfide exchange with glutathione
CC       disulfide and by oxyradical-initiated S-thiolation with reduced
CC       glutathione. {ECO:0000250|UniProtKB:P14141}.
CC   -!- PTM: S-glutathionylated in hepatocytes under oxidative stress.
CC       {ECO:0000250|UniProtKB:P14141}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ157048; ABA41599.1; -; Genomic_DNA.
DR   EMBL; AY789645; AAV65838.1; -; mRNA.
DR   EMBL; AY789514; AAV83540.1; -; mRNA.
DR   EMBL; DQ675018; ABG49150.1; -; Genomic_DNA.
DR   RefSeq; NP_001008688.1; NM_001008688.1.
DR   AlphaFoldDB; Q5S1S4; -.
DR   SMR; Q5S1S4; -.
DR   STRING; 9823.ENSSSCP00000006551; -.
DR   PaxDb; Q5S1S4; -.
DR   PeptideAtlas; Q5S1S4; -.
DR   PRIDE; Q5S1S4; -.
DR   Ensembl; ENSSSCT00005052521; ENSSSCP00005032438; ENSSSCG00005032882.
DR   Ensembl; ENSSSCT00070032097; ENSSSCP00070026771; ENSSSCG00070016319.
DR   Ensembl; ENSSSCT00070032110; ENSSSCP00070026784; ENSSSCG00070016319.
DR   GeneID; 494016; -.
DR   KEGG; ssc:494016; -.
DR   CTD; 761; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; Q5S1S4; -.
DR   OMA; ERWHENY; -.
DR   OrthoDB; 1377476at2759; -.
DR   TreeFam; TF316425; -.
DR   Reactome; R-SSC-1475029; Reversible hydration of carbon dioxide.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 4.
DR   Genevisible; Q5S1S4; SS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR   GO; GO:0016151; F:nickel cation binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   InterPro; IPR018441; Carbonic_anhydrase_CA3.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   PANTHER; PTHR18952:SF127; PTHR18952:SF127; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Glutathionylation; Lyase; Metal-binding;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P07450"
FT   CHAIN           2..260
FT                   /note="Carbonic anhydrase 3"
FT                   /id="PRO_0000077428"
FT   DOMAIN          3..259
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          64..67
FT                   /note="Involved in proton transfer"
FT                   /evidence="ECO:0000250|UniProtKB:P07451"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07451"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07451"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P07451"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P07450"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         73
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         127
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         176
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16015"
FT   MOD_RES         182
FT                   /note="S-glutathionyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         187
FT                   /note="S-glutathionyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         216
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14141"
SQ   SEQUENCE   260 AA;  29411 MW;  3256EF36BF48FC2F CRC64;
     MAKEWGYADH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLLPWTAS YDPGSAKTIL
     NNGKTCRVVF DDTYDRSMLR GGPLTAAYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL
     VHWNSKYNSF ATALKHPDGV AVVGIFLKIG REKGEFQLVL DALDKIKTKG KEAPFTNFNP
     SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPITVSSD QMAKLRSLYS SAENEPPVPL
     VRNWRPPQPI KGRIVKASFK
 
 
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