PPWD1_BOVIN
ID PPWD1_BOVIN Reviewed; 644 AA.
AC Q29RZ2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 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].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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; BC113320; AAI13321.1; -; mRNA.
DR RefSeq; NP_001039696.1; NM_001046231.1.
DR AlphaFoldDB; Q29RZ2; -.
DR SMR; Q29RZ2; -.
DR STRING; 9913.ENSBTAP00000012520; -.
DR PaxDb; Q29RZ2; -.
DR PRIDE; Q29RZ2; -.
DR Ensembl; ENSBTAT00000012520; ENSBTAP00000012520; ENSBTAG00000009514.
DR GeneID; 517560; -.
DR KEGG; bta:517560; -.
DR CTD; 23398; -.
DR VEuPathDB; HostDB:ENSBTAG00000009514; -.
DR VGNC; VGNC:33279; PPWD1.
DR eggNOG; KOG0882; Eukaryota.
DR GeneTree; ENSGT00940000158733; -.
DR HOGENOM; CLU_012062_31_2_1; -.
DR InParanoid; Q29RZ2; -.
DR OMA; GGMVEYW; -.
DR OrthoDB; 1392223at2759; -.
DR TreeFam; TF105686; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000009514; Expressed in semen and 108 other tissues.
DR ExpressionAtlas; Q29RZ2; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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; PS50082; WD_REPEATS_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..644
FT /note="Peptidylprolyl isomerase domain and WD repeat-
FT containing protein 1"
FT /id="PRO_0000240305"
FT REPEAT 86..124
FT /note="WD 1"
FT REPEAT 129..168
FT /note="WD 2"
FT REPEAT 219..258
FT /note="WD 3"
FT REPEAT 276..317
FT /note="WD 4"
FT DOMAIN 488..643
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
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 644 AA; 73274 MW; 9EDCC2AEB77BAB18 CRC64;
MAAECGSDSQ PRRRRRRDPE EPGKTELSAR EPVVAVPQEN EEENEERWVG PLPVEATLAK
KRKVLEFEKV YLDNLPSASM YERSYMHRDV ITHVVCTKTD FIITASHDGH VKFWKKIEEG
IEFVKHFRSH LGVIESIAVS SEGALFCSVG DDKAMKVFDV VNFDMINMLK LGYFPGQCEW
IYCPGDAISS VAASEKSTGK IFIYDGRGDN QPLHIFDKLH TSPLTQIRLN PVYKAVVSSD
KSGMIEYWTG PPYEYKFPKN VNWEYKTDTD LYEFAKCKAY PTSICFSPDG KKLATIGSDR
KVRIFRFLTG KLMRVFDESL SMFTELQQMR QQLPDMEFGR RMAVERELEK VDAVRLINIV
FDETGHFVLY GTMLGIKVIN VETNRCVRIL GKQENIRVMQ LALFQGIAKK HRAATTIEMK
ASENPVLQNI QADPTIVCTS FKKNRFYMFT KREPEDTKSA DSDRDVFNEK PSKEEVMAAT
QAEGPKRVSD SAIIHTSMGD IHIKLFPVEC PKTVENFCVH SRNGYYNGHT FHRIIKGFMI
QTGDPTGTGM GGESIWGGEF EDEFHSTLRH DRPYTLSMAN AGSNTNGSQF FITVVPTPWL
DNKHTVFGRV TKGMEVVQRI SNVKVNPKTD KPYEDVSIIN ITVK
