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Database: UniProt
Entry: A0A2K6FE07_PROCO
LinkDB: A0A2K6FE07_PROCO
Original site: A0A2K6FE07_PROCO 
ID   A0A2K6FE07_PROCO        Unreviewed;       163 AA.
AC   A0A2K6FE07;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363014};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363014};
GN   Name=PIN1 {ECO:0000313|Ensembl:ENSPCOP00000012221.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000012221.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000012221.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_012496928.1; XM_012641474.1.
DR   AlphaFoldDB; A0A2K6FE07; -.
DR   STRING; 379532.ENSPCOP00000012221; -.
DR   Ensembl; ENSPCOT00000022815.1; ENSPCOP00000012221.1; ENSPCOG00000017665.1.
DR   GeneID; 105807944; -.
DR   KEGG; pcoq:105807944; -.
DR   CTD; 5300; -.
DR   GeneTree; ENSGT00640000091578; -.
DR   OMA; DEVQCLH; -.
DR   OrthoDB; 417859at2759; -.
DR   Proteomes; UP000233160; Unplaced.
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   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|RuleBase:RU363014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
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..163
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          33..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   163 AA;  18257 MW;  353A0AF30B7D1E14 CRC64;
     MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN STSGGKNGQG EPARVRCSHL
     LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG
     DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE
//
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