PPWD1_MOUSE
ID PPWD1_MOUSE Reviewed; 646 AA.
AC Q8CEC6; Q0VEA0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
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:0000312|MGI:MGI:2443069};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK028532; BAC25996.1; -; mRNA.
DR EMBL; BC119282; AAI19283.1; -; mRNA.
DR EMBL; BC119310; AAI19311.1; -; mRNA.
DR CCDS; CCDS26748.1; -.
DR RefSeq; NP_766395.2; NM_172807.4.
DR AlphaFoldDB; Q8CEC6; -.
DR SMR; Q8CEC6; -.
DR BioGRID; 232021; 53.
DR STRING; 10090.ENSMUSP00000022226; -.
DR iPTMnet; Q8CEC6; -.
DR PhosphoSitePlus; Q8CEC6; -.
DR EPD; Q8CEC6; -.
DR MaxQB; Q8CEC6; -.
DR PaxDb; Q8CEC6; -.
DR PeptideAtlas; Q8CEC6; -.
DR PRIDE; Q8CEC6; -.
DR ProteomicsDB; 289820; -.
DR Antibodypedia; 11576; 215 antibodies from 22 providers.
DR DNASU; 238831; -.
DR Ensembl; ENSMUST00000022226; ENSMUSP00000022226; ENSMUSG00000021713.
DR GeneID; 238831; -.
DR KEGG; mmu:238831; -.
DR UCSC; uc007rsz.2; mouse.
DR CTD; 23398; -.
DR MGI; MGI:2443069; Ppwd1.
DR VEuPathDB; HostDB:ENSMUSG00000021713; -.
DR eggNOG; KOG0882; Eukaryota.
DR GeneTree; ENSGT00940000158733; -.
DR HOGENOM; CLU_012062_31_2_1; -.
DR InParanoid; Q8CEC6; -.
DR OMA; GGMVEYW; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q8CEC6; -.
DR TreeFam; TF105686; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 238831; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Ppwd1; mouse.
DR PRO; PR:Q8CEC6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CEC6; protein.
DR Bgee; ENSMUSG00000021713; Expressed in animal zygote and 217 other tissues.
DR Genevisible; Q8CEC6; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
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 1: Evidence at protein 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_0000240307"
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..50
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96BP3"
FT CONFLICT 385
FT /note="T -> P (in Ref. 1; BAC25996)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="P -> T (in Ref. 1; BAC25996)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="T -> S (in Ref. 1; BAC25996)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="S -> F (in Ref. 1; BAC25996)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="K -> Q (in Ref. 1; BAC25996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 73385 MW; FEF78325D862560A CRC64;
MATESGSDSQ LRRRRRRDPE GSEKTELSER EPALAVAGSE ENDDENEERW VGPLPVEATL
AKKRKVLEFE RVYLDNLPSA SMYERSYMHR DVITHVVCTK TDFIITASHD GHVKFWKKIE
EGIEFVKHFR SHLGVIESIA VSSEGALFCS VGDDKAMKVF DVVNFDMINM LKLGYFPGQC
EWIYCPGDAI SSVAASEKST GKIFIYDGRG DNQPLHIFDK LHVSPLTQIR LNPVYKAVVS
SDKSGMIEYW TGPPHEYKFP KNVNWEYKTD TDLYEFAKCK AYPTSICFSP DGKKIATIGS
DRKVRIFRFL TGKLMRVFDE SLSMFTELQQ MRQQLPDMEF GRRMAVEREL EKVDAVRLVN
IVFDETGHFV LYGTMLGIKV INVETNRCVR ILGKQENIRV MQLALFQGIA KKHRAAATIE
MKASENPVLQ NIQADPTIVC TSFKKNRFYM FTKREPEDTK TADSDRDVFN EKPSKEEVMA
ATQAEGPKRV SDSAIVHTSM GDIHIKLFPV ECPKTVENFC VHSRNGYYNG HTFHRIIKGF
MIQTGDPTGT GMGGESIWGG EFEDEFHSTL RHDRPYTLSM ANAGSNTNGS QFFITVVPTP
WLDNKHTVFG RVTKGMEVVQ RISNVKVNPK TDKPYEDVSI INITVK
