ID   PRP31_XENLA             Reviewed;         498 AA.
AC   Q5U5C5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp31;
DE   AltName: Full=Pre-mRNA-processing factor 31;
GN   Name=prpf31;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC       spliceosome. Required for the assembly of the U4/U5/U6 tri-snRNP
CC       complex, one of the building blocks of the spliceosome.
CC       {ECO:0000250|UniProtKB:Q8WWY3}.
CC   -!- SUBUNIT: Identified in the spliceosome B complex. Component of the
CC       U4/U6-U5 tri-snRNP complex. Component of some MLL1/MLL complex.
CC       {ECO:0000250|UniProtKB:Q8WWY3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WWY3}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q8WWY3}. Nucleus, Cajal body
CC       {ECO:0000250|UniProtKB:Q8WWY3}. Note=Predominantly found in speckles
CC       and in Cajal bodies. {ECO:0000250|UniProtKB:Q8WWY3}.
CC   -!- DOMAIN: Interacts with the snRNP via the Nop domain.
CC       {ECO:0000250|UniProtKB:Q8WWY3}.
CC   -!- DOMAIN: The coiled coil domain is formed by two non-contiguous helices.
CC       {ECO:0000250|UniProtKB:Q8WWY3}.
CC   -!- SIMILARITY: Belongs to the PRP31 family. {ECO:0000305}.
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DR   EMBL; BC084759; AAH84759.1; -; mRNA.
DR   RefSeq; NP_001088437.1; NM_001094968.1.
DR   AlphaFoldDB; Q5U5C5; -.
DR   SMR; Q5U5C5; -.
DR   BioGRID; 105381; 1.
DR   DNASU; 495301; -.
DR   GeneID; 495301; -.
DR   KEGG; xla:495301; -.
DR   CTD; 495301; -.
DR   Xenbase; XB-GENE-865857; prpf31.S.
DR   OrthoDB; 791296at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 495301; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR   GO; GO:0005690; C:U4atac snRNP; ISS:UniProtKB.
DR   GO; GO:0030622; F:U4atac snRNA binding; ISS:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IEA:InterPro.
DR   Gene3D; 1.10.246.90; -; 1.
DR   InterPro; IPR042239; Nop_C.
DR   InterPro; IPR002687; Nop_dom.
DR   InterPro; IPR036070; Nop_dom_sf.
DR   InterPro; IPR012976; NOSIC.
DR   InterPro; IPR027105; Prp31.
DR   InterPro; IPR019175; Prp31_C.
DR   PANTHER; PTHR13904; PTHR13904; 1.
DR   Pfam; PF01798; Nop; 1.
DR   Pfam; PF09785; Prp31_C; 1.
DR   SMART; SM00931; NOSIC; 1.
DR   SUPFAM; SSF89124; SSF89124; 1.
DR   PROSITE; PS51358; NOP; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Spliceosome.
FT   CHAIN           1..498
FT                   /note="U4/U6 small nuclear ribonucleoprotein Prp31"
FT                   /id="PRO_0000227802"
FT   DOMAIN          214..332
FT                   /note="Nop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          84..119
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   COILED          180..214
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   MOTIF           350..363
FT                   /note="Nuclear localization signal (NLS)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   COMPBIAS        9..24
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            246
FT                   /note="Interaction with U4 snRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   SITE            269
FT                   /note="Interaction with U4 snRNA and U4atac snRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   SITE            288
FT                   /note="Interaction with U4atac snRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   SITE            292
FT                   /note="Interaction with U4 snRNA and U4atac snRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
FT   SITE            297
FT                   /note="Interaction with U4 snRNA and U4atac snRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWY3"
SQ   SEQUENCE   498 AA;  55563 MW;  665F88951D8F4D3B CRC64;
     MSLADELLAD LEEAAEEEEE NLIDEDDLET IEEVDEEMQV DLNAESVKSI AKLSDSKLFS
     EILLKIEGYI QKQPKASEVM GPVEAAPEYK VIVDANNLTV EIENELNIIH KFIRDKYSKR
     FPELESLVPN ALDYIRTVKE LGNNLDKCKN NENLQQILTN ATIMVVSVTA STTQGQQLTD
     EELERIEEAC DMALELNQSK HRIYEYVESR MSFIAPNLSI IVGASTAAKI MGIAGGLTNL
     SKMPACNVML LGAQRKTLTG FSSTSVLPHT GYIYHSEIVQ SLPSDLHRKA ARLVSAKCTL
     ASRVDSFHEN PEGKIGYDLK EEIERKFDKW QEPPPVKQVK PLPAPLDGQR KKRGGRRYRK
     MKERLGLTEI RKQANRMSFG EIEEDAYQED LGFSLGHLGK SGSGRIRQAQ VNEATKARIS
     KTLQRTLQKQ SVVYGGKSTV RDRSSGTASS VAFTPLQGLE IVNPQAAEKK VAEANQKYFS
     SMAEFLKVKS EKSGTMTQ