PIN1_BOVIN
ID PIN1_BOVIN Reviewed; 163 AA.
AC Q5BIN5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q13526};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE Short=PPIase Pin1;
DE AltName: Full=Rotamase Pin1;
GN Name=PIN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to
CC and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro)
CC motifs. By inducing conformational changes in a subset of
CC phosphorylated proteins, acts as a molecular switch in multiple
CC cellular processes. Displays a preference for acidic residues located
CC N-terminally to the proline bond to be isomerized. Regulates mitosis
CC presumably by interacting with NIMA and attenuating its mitosis-
CC promoting activity. Down-regulates kinase activity of BTK. Can
CC transactivate multiple oncogenes and induce centrosome amplification,
CC chromosome instability and cell transformation. Required for the
CC efficient dephosphorylation and recycling of RAF1 after mitogen
CC activation. Binds and targets PML and BCL6 for degradation in a
CC phosphorylation-dependent manner. Acts as a regulator of JNK cascade by
CC binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and
CC promoting FBXW7 autoubiquitination and degradation: degradation of
CC FBXW7 leads to subsequent stabilization of JUN. May facilitate the
CC ubiquitination and proteasomal degradation of RBBP8/CtIP through
CC CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA
CC double-strand repair through error-prone non-homologous end joining
CC (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR).
CC Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization
CC of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear
CC translocation and expression of pro-inflammatory genes in dendritic
CC cells. {ECO:0000250|UniProtKB:Q13526}.
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:0000250|UniProtKB:Q13526};
CC -!- SUBUNIT: Interacts with STIL (By similarity). Interacts with KIF20B.
CC Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts
CC with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the
CC phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon
CC NGF stimulation. Interacts with PML (isoform PML-4). Interacts with
CC BCL6. Interacts with FBXW7, disrupting FBXW7 dimerization and promoting
CC FBXW7 autoubiquitination and degradation. Directly interacts with
CC RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation.
CC Interacts (via WW domain) with IRAK3/IRAK-M in response to IL33-
CC mediated (but not TLR4 ligand LPS) dendritic cell stimulation (By
CC similarity). {ECO:0000250|UniProtKB:Q13526,
CC ECO:0000250|UniProtKB:Q9QUR7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13526}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q13526}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13526}. Note=Colocalizes with NEK6 in the
CC nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71
CC by DAPK1 results in inhibition of its nuclear localization.
CC {ECO:0000250|UniProtKB:Q13526}.
CC -!- DOMAIN: The WW domain is required for the interaction with STIL and
CC KIF20B. {ECO:0000250|UniProtKB:Q13526}.
CC -!- PTM: Phosphorylation at Ser-71 by DAPK1 results in inhibition of its
CC catalytic activity, nuclear localization, and its ability to induce
CC centrosome amplification, chromosome instability and cell
CC transformation (By similarity). Ser-71 is dephosphorylated upon IL33-
CC stimulation of dendritic cells (By similarity).
CC {ECO:0000250|UniProtKB:Q13526, ECO:0000250|UniProtKB:Q9QUR7}.
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DR EMBL; BT021189; AAX31371.1; -; mRNA.
DR EMBL; BC112583; AAI12584.1; -; mRNA.
DR RefSeq; NP_001029804.1; NM_001034632.3.
DR AlphaFoldDB; Q5BIN5; -.
DR BMRB; Q5BIN5; -.
DR SMR; Q5BIN5; -.
DR STRING; 9913.ENSBTAP00000022592; -.
DR PaxDb; Q5BIN5; -.
DR PRIDE; Q5BIN5; -.
DR Ensembl; ENSBTAT00000022592; ENSBTAP00000022592; ENSBTAG00000016988.
DR GeneID; 535470; -.
DR KEGG; bta:535470; -.
DR CTD; 5300; -.
DR VEuPathDB; HostDB:ENSBTAG00000016988; -.
DR VGNC; VGNC:97301; PIN1.
DR eggNOG; KOG3259; Eukaryota.
DR GeneTree; ENSGT00640000091578; -.
DR HOGENOM; CLU_090028_0_1_1; -.
DR InParanoid; Q5BIN5; -.
DR OMA; DEVQCLH; -.
DR OrthoDB; 1437969at2759; -.
DR TreeFam; TF101101; -.
DR Reactome; R-BTA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-BTA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-BTA-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-BTA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000016988; Expressed in retina and 108 other tissues.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0016859; F:cis-trans isomerase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0050815; F:phosphoserine residue binding; IEA:Ensembl.
DR GO; GO:0050816; F:phosphothreonine residue binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
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:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; 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:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; 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:0051443; P:positive regulation of ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; IEA:Ensembl.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR CDD; cd00201; WW; 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 Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 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 Acetylation; Cell cycle; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase.
FT CHAIN 1..163
FT /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT 1"
FT /id="PRO_0000236242"
FT DOMAIN 5..39
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 52..163
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13526"
FT MOD_RES 71
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q13526"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13526"
SQ SEQUENCE 163 AA; 18273 MW; 6CED0EF411C3AB0D CRC64;
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSGSGKNGQG EPTRVRCSHL
LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE EDFESLASQF SDCSSAKARG
DLGAFSRGQM QKPFEDASFA LRTGEMSGPV FTDSGIHIIL RTE
