ID   PPWD1_PONAB             Reviewed;         646 AA.
AC   Q5NVL7;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Peptidylprolyl isomerase domain and WD repeat-containing protein 1 {ECO:0000305};
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:Q96BP3};
GN   Name=PPWD1 {ECO:0000250|UniProtKB:Q96BP3};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC       imidic peptide bonds in oligopeptides and may therefore assist protein
CC       folding. May be involved in pre-mRNA splicing.
CC       {ECO:0000250|UniProtKB:Q96BP3}.
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:Q96BP3};
CC   -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC       {ECO:0000250|UniProtKB:Q96BP3}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex.
CC       {ECO:0000250|UniProtKB:Q96BP3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BP3}.
CC       Note=Associated with spliceosomal complexes. {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q96BP3}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR926008; CAI29646.1; -; mRNA.
DR   RefSeq; NP_001127684.1; NM_001134212.1.
DR   AlphaFoldDB; Q5NVL7; -.
DR   SMR; Q5NVL7; -.
DR   STRING; 9601.ENSPPYP00000017328; -.
DR   GeneID; 100174766; -.
DR   KEGG; pon:100174766; -.
DR   CTD; 23398; -.
DR   eggNOG; KOG0882; Eukaryota.
DR   InParanoid; Q5NVL7; -.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 2.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Repeat; Rotamase; Spliceosome; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BP3"
FT   CHAIN           2..646
FT                   /note="Peptidylprolyl isomerase domain and WD repeat-
FT                   containing protein 1"
FT                   /id="PRO_0000240308"
FT   REPEAT          88..126
FT                   /note="WD 1"
FT   REPEAT          131..170
FT                   /note="WD 2"
FT   REPEAT          221..260
FT                   /note="WD 3"
FT   REPEAT          278..319
FT                   /note="WD 4"
FT   DOMAIN          490..645
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96BP3"
SQ   SEQUENCE   646 AA;  73527 MW;  266D3227BF495784 CRC64;
     MAAESGSDFQ QRRRRRRDPE EPEKTELSER ELAVAVAVSQ ENDEENEERW VGPLPVEATL
     AKKRKVLEFE RVYLDNLPSA SMYERSYMHR DVITHVVCTK TDFIITASHD GHVKFWKKIE
     EGIEFVKHFR SHLGVIECIA VSSEGALFCS VGDDKAMKVF DVVNFDMINM LKLGYFPGQC
     EWIYCPGDAI SSVAASEKST GKIFIYDGRG DNQPLHIFDK LHTSPLTQIR LNPVYKAVVS
     SDKSGMIEYW TGPPHEYKFP KNVNWEYKTD TDLYEFAKCK AYPTSICFSP DGKKIATIGS
     DRKVRISKFL TGKLMRVFDE SLSMFTELQQ MRQQLPDMEF GRRMAVEREL EKVDAVRLIN
     IVFDETGHFV LYGTMLGIKV INVETNRCVR ILGKQENIRV MQLALFQGIA KKHRAATTIE
     MKASENPVLQ NIQADPTVVC TPFKKNRFYM FTKREPEDTK SADSDRDVFN EKPSKEEVMA
     ATQAEGPKRV SDSAIIHTSM GDIHTKLFPV ECPKTVENFC VHSRNGYYNG HTFHRIIKGF
     MIQTGDPTGT GMGGESIWGG EFEDEFHSTL RHDRPYTLSM ANAGSNTNGS QFFITVVPTP
     WLDNKHTVFG RVTKGMEVVQ RISNVKVNPK TDKPYEDVSI INITVK