UniProt ID: A0A8M3ALA9 |
FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000256|RuleBase:RU365081}. CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|RuleBase:RU365081}; SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily. {ECO:0000256|RuleBase:RU365081}. |
UniProt ID: A5PM92 |
FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000256|RuleBase:RU365081}. CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|RuleBase:RU365081}; SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily. {ECO:0000256|RuleBase:RU365081}. |
UniProt ID: A0A8M3B3W8 |
FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. {ECO:0000256|RuleBase:RU365081}. CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|RuleBase:RU365081}; SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4 subfamily. {ECO:0000256|RuleBase:RU365081}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |