ID   PRPF3_MOUSE             Reviewed;         683 AA.
AC   Q922U1; Q3TJH4; Q9D6C6;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp3;
DE   AltName: Full=Pre-mRNA-splicing factor 3;
GN   Name=Prpf3;
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, and NOD; TISSUE=Placenta, and Thymus;
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=Mammary tumor;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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: Plays a role in pre-mRNA splicing as component of the U4/U6-
CC       U5 tri-snRNP complex that is involved in spliceosome assembly, and as
CC       component of the precatalytic spliceosome (spliceosome B complex).
CC       {ECO:0000250|UniProtKB:O43395}.
CC   -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC       complex) (By similarity). Component of the U4/U6-U5 tri-snRNP complex,
CC       a building block of the precatalytic spliceosome (spliceosome B
CC       complex) (By similarity). The U4/U6-U5 tri-snRNP complex is composed of
CC       the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8,
CC       PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC       SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and
CC       USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 (By
CC       similarity). Interacts directly with PRPF4 (By similarity). Part of a
CC       heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in
CC       the absence of RNA (By similarity). Interacts with SART3; the
CC       interaction is direct and recruits the deubiquitinase USP4 to PRPF3 (By
CC       similarity). Interacts with PRPF19 (By similarity). Interacts ('Lys-
CC       63'-linked polyubiquitinated) with PRPF8 (via the MPN (JAB/Mov34)
CC       domain); may stabilize the U4/U6-U5 tri-snRNP complex (By similarity).
CC       Interacts with ERCC6 (By similarity). {ECO:0000250|UniProtKB:O43395}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43395}. Nucleus
CC       speckle {ECO:0000255|PROSITE-ProRule:PRU00627}.
CC   -!- PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination by
CC       PRPF19 and deubiquitination by USP4. 'Lys-63'-linked ubiquitination
CC       increases the affinity for PRPF8 and may regulate the assembly of the
CC       U4/U6-U5 tri-snRNP complex. {ECO:0000250|UniProtKB:O43395}.
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DR   EMBL; AK014398; BAB29324.1; -; mRNA.
DR   EMBL; AK088194; BAC40202.1; -; mRNA.
DR   EMBL; AK167435; BAE39521.1; -; mRNA.
DR   EMBL; BC006782; AAH06782.1; -; mRNA.
DR   CCDS; CCDS17621.1; -.
DR   RefSeq; NP_001303680.1; NM_001316751.1.
DR   RefSeq; NP_081817.2; NM_027541.4.
DR   AlphaFoldDB; Q922U1; -.
DR   SMR; Q922U1; -.
DR   BioGRID; 214242; 70.
DR   IntAct; Q922U1; 21.
DR   STRING; 10090.ENSMUSP00000015892; -.
DR   iPTMnet; Q922U1; -.
DR   PhosphoSitePlus; Q922U1; -.
DR   EPD; Q922U1; -.
DR   jPOST; Q922U1; -.
DR   MaxQB; Q922U1; -.
DR   PaxDb; 10090-ENSMUSP00000015892; -.
DR   PeptideAtlas; Q922U1; -.
DR   ProteomicsDB; 291564; -.
DR   Pumba; Q922U1; -.
DR   Antibodypedia; 20281; 211 antibodies from 31 providers.
DR   DNASU; 70767; -.
DR   Ensembl; ENSMUST00000015892.14; ENSMUSP00000015892.8; ENSMUSG00000015748.14.
DR   Ensembl; ENSMUST00000161476.8; ENSMUSP00000124950.2; ENSMUSG00000015748.14.
DR   GeneID; 70767; -.
DR   KEGG; mmu:70767; -.
DR   UCSC; uc008qlf.1; mouse.
DR   AGR; MGI:1918017; -.
DR   CTD; 9129; -.
DR   MGI; MGI:1918017; Prpf3.
DR   VEuPathDB; HostDB:ENSMUSG00000015748; -.
DR   eggNOG; KOG2769; Eukaryota.
DR   GeneTree; ENSGT00390000011497; -.
DR   HOGENOM; CLU_015750_3_0_1; -.
DR   InParanoid; Q922U1; -.
DR   OMA; KNHEMRN; -.
DR   OrthoDB; 5489218at2759; -.
DR   PhylomeDB; Q922U1; -.
DR   TreeFam; TF313082; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 70767; 17 hits in 81 CRISPR screens.
DR   ChiTaRS; Prpf3; mouse.
DR   PRO; PR:Q922U1; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q922U1; Protein.
DR   Bgee; ENSMUSG00000015748; Expressed in embryonic post-anal tail and 226 other cell types or tissues.
DR   ExpressionAtlas; Q922U1; baseline and differential.
DR   GO; GO:0015030; C:Cajal body; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISO:MGI.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR   Gene3D; 1.20.1390.10; PWI domain; 1.
DR   InterPro; IPR013881; Pre-mRNA_splic_Prp3_dom.
DR   InterPro; IPR027104; Prp3.
DR   InterPro; IPR010541; Prp3_C.
DR   InterPro; IPR002483; PWI_dom.
DR   InterPro; IPR036483; PWI_dom_sf.
DR   PANTHER; PTHR14212; U4/U6-ASSOCIATED RNA SPLICING FACTOR-RELATED; 1.
DR   PANTHER; PTHR14212:SF0; U4_U6 SMALL NUCLEAR RIBONUCLEOPROTEIN PRP3; 1.
DR   Pfam; PF08572; PRP3; 1.
DR   Pfam; PF06544; Prp3_C; 1.
DR   Pfam; PF01480; PWI; 1.
DR   SMART; SM00311; PWI; 1.
DR   SUPFAM; SSF101233; PWI domain; 1.
DR   PROSITE; PS51025; PWI; 1.
DR   Genevisible; Q922U1; MM.
PE   1: Evidence at protein level;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Spliceosome; Ubl conjugation.
FT   CHAIN           1..683
FT                   /note="U4/U6 small nuclear ribonucleoprotein Prp3"
FT                   /id="PRO_0000097045"
FT   DOMAIN          1..87
FT                   /note="PWI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT   REGION          73..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..550
FT                   /note="Mediates interaction with SART3"
FT                   /evidence="ECO:0000250|UniProtKB:O43395"
FT   COMPBIAS        73..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43395"
FT   MOD_RES         619
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        139
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43395"
FT   CROSSLNK        244
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43395"
FT   CROSSLNK        252
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O43395"
FT   CONFLICT        78
FT                   /note="H -> L (in Ref. 1; BAB29324)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   683 AA;  77455 MW;  988219CF88E0EC4A CRC64;
     MALSKRELDE LKPWIEKTVK RVLGFSEPTV VTAALNCVGK GMDKKKAADH LKPFLDDSTL
     RFVDKLFEAV EEGRSSRHSK SSSDRSRKRE LKEVFGDDSE ISKESSGVKK RRIPRFEEVE
     EEPEVIPGPP SESPGMLTKL QIKQMMEAAT RQIEERKKQL SFISPPAPQP KTPSSSQPER
     LPIGNTIQPS QAATFMNDAI EKARKAAELQ ARIQAQLALK PGLIGNANMV GLANLHAMGI
     APPKVELKDQ TKPTPLILDE QGRTVDATGK EVELTHRMPT LKANIRAVKR EQFKQQLKEK
     PSEDMESNTF FDPRVSIAPS QRQRRTFKFH DKGKFEKIAQ RLRTKAQLEK LQAEISQAAR
     KTGIHTSTRL ALIAPKKELK EGDIPEIEWW DSYIIPNGFD LTEENPKRED YFGITNLVEH
     PAQLNPPVDN DTPVTLGVYL TKKEQKKLRR QTRREAQKEL QEKVRLGLTP PPEPKVRISN
     LMRVLGTEAV QDPTKVEAHV RAQMAKRQKA HEEANAARKL TAEQRKVKKI KKLKEDISQG
     VHISVYRVRN LSNPAKKFKI EANAGQLYLT GVVVLHKDVN VVVVEGGPKA QKKFKRLMLH
     RIKWDEQTSN TKGDDDEESD EEAVKKTNKC VLVWEGTAKD RSFGEMKFKQ CPTENMAREH
     FKKHGAEHYW DLALSESVLE STD
//