ID G9KGP8_MUSPF Unreviewed; 162 AA.
AC G9KGP8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES04073.1};
RN [1] {ECO:0000313|EMBL:AES04073.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES04073.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU363014};
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DR EMBL; JP015475; AES04073.1; -; mRNA.
DR AlphaFoldDB; G9KGP8; -.
DR HOGENOM; CLU_090028_0_1_1; -.
DR OMA; DEVQCLH; -.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IEA:Ensembl.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050815; F:phosphoserine residue binding; IEA:Ensembl.
DR GO; GO:0050816; F:phosphothreonine residue binding; IEA:Ensembl.
DR GO; GO:1990757; F:ubiquitin ligase activator activity; IEA:Ensembl.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10657; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR10657:SF4; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 2: Evidence at transcript level;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000256|RuleBase:RU363014}.
FT DOMAIN 5..39
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 52..162
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES04073.1"
FT NON_TER 162
FT /evidence="ECO:0000313|EMBL:AES04073.1"
SQ SEQUENCE 162 AA; 18174 MW; A91AF405D7B06FCA CRC64;
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGSKNGQG EPTRVRCSHL
LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG
DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RT
//
