PRPF3_PONAB
ID PRPF3_PONAB Reviewed; 683 AA.
AC Q5R5F1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp3;
DE AltName: Full=Pre-mRNA-splicing factor 3;
GN Name=PRPF3;
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=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5
CC 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; CR860910; CAH93015.1; -; mRNA.
DR RefSeq; NP_001126781.1; NM_001133309.1.
DR AlphaFoldDB; Q5R5F1; -.
DR SMR; Q5R5F1; -.
DR STRING; 9601.ENSPPYP00000001054; -.
DR GeneID; 100440626; -.
DR KEGG; pon:100440626; -.
DR CTD; 9129; -.
DR eggNOG; KOG2769; Eukaryota.
DR InParanoid; Q5R5F1; -.
DR OrthoDB; 1322299at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR InterPro; IPR013881; Pre-mRNA_splic_Prp3.
DR InterPro; IPR027104; Prp3.
DR InterPro; IPR010541; Prp3_C.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR PANTHER; PTHR14212; PTHR14212; 1.
DR Pfam; PF06544; DUF1115; 1.
DR Pfam; PF08572; PRP3; 1.
DR Pfam; PF01480; PWI; 1.
DR SMART; SM00311; PWI; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR PROSITE; PS51025; PWI; 1.
PE 2: Evidence at transcript 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_0000312363"
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 153..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 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43395"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43395"
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"
SQ SEQUENCE 683 AA; 77557 MW; 405106CFBF6A29F5 CRC64;
MALSKRELDE LKPWIEKTVK RVLGFSEPTV VTAALNCVGK GMDKKKAADH LKPFLDDSTL
RFVDKLFEAV EEGRSSRHSK SSSDRSRKRE LKEVFGDDSE ISKESSGVKK RRIPRFEEVE
EEPEVIPGPP SESPGMLTKL QIKQMMEAAT RQIEERKKQL SFISPPTPQP KTPSSSQPER
LPIGNTIQPS QAATFMNDAI EKARKAAELQ ARIQAQLALK PGLIGNANMV GLANLHAMGI
APPKVELKDQ TKPTPLILDE QGRTVDATGK EIELTHRMPT LKANIRAVKR EQFRQQLKEK
PSEDMESNTF FDPRVSIAPS QRQRRTFKFH DKGKFEKIAQ RLRTKAQLEK LQAEISQAAR
KTGIHTSTRL ALIAPKKELK EGDIPEIEWW DSYIIPNGFD LTEENPKRED YFGITNLVEH
PAQLNPPVDN DTPVTLGVYL TKKEQKKLRR QTRREAQKEL QEKVRLGLMP PPEPKVRISN
LMRVLGTEAV QDPTKVEAHV RAQMAKRQKA HEEANAARKL TAEQRKVKKI KKLKEDISQG
VHISVYRVRN LSNPAKKFKI EANAGQLYLT GVVVLHKDVN VVVVEGGPKA QKKFKRLMLH
RIKWDEQTSN TKGDDDEESD EEAVKKTNKC VLVWEGTAKD RSFGEMKFKQ CPTENMAREH
FKKHGAEHYW DLALSESVLE STD
