CDC5L_MOUSE
ID CDC5L_MOUSE Reviewed; 802 AA.
AC Q6A068; Q8K1J9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cell division cycle 5-like protein;
DE AltName: Full=Cdc5-like protein;
GN Name=Cdc5l; Synonyms=Kiaa0432;
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 TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 34-40 AND 766-771, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10570151; DOI=10.1073/pnas.96.24.13789;
RA Burns C.G., Ohi R., Krainer A.R., Gould K.L.;
RT "Evidence that Myb-related CDC5 proteins are required for pre-mRNA
RT splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13789-13794(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: DNA-binding protein involved in cell cycle control. May act
CC as a transcription activator. Plays role in pre-mRNA splicing as core
CC component of precatalytic, catalytic and postcatalytic spliceosomal
CC complexes. Component of the PRP19-CDC5L complex that forms an integral
CC part of the spliceosome and is required for activating pre-mRNA
CC splicing. The PRP19-CDC5L complex may also play a role in the response
CC to DNA damage (DDR). {ECO:0000250|UniProtKB:Q99459}.
CC -!- SUBUNIT: Homodimer. Interacts with DAPK3 (By similarity). Component of
CC the precatalytic, catalytic and postcatalytic spliceosome complexes (By
CC similarity). Part of a spliceosomal 'core' complex consisting of CDC5L,
CC PLRG1, SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1,
CC Lodestar/TTF2, and NIPP1/PPP1R8. Component of the PRP19-CDC5L splicing
CC complex composed of a core complex comprising a homotetramer of PRPF19,
CC CDC5L, PLRG1 and BCAS2, and at least three less stably associated
CC proteins CTNNBL1, CWC15 and HSPA8. Interacts (via its C-terminus)
CC directly in the complex with PRPF19 and BCAS2. Interacts (via its C-
CC terminus) directly with PRGL1 (via its WD40 repeat domain); the
CC interaction is required for mRNA splicing but not for spliceosome
CC assembly. Also interacts with CTNNBL1. Interacts with PRPF19 (via N-
CC terminus) (By similarity). Interacts with USB1 (By similarity).
CC {ECO:0000250|UniProtKB:O08837, ECO:0000250|UniProtKB:Q99459}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:10570151}. Nucleus speckle {ECO:0000255|PROSITE-
CC ProRule:PRU00625, ECO:0000269|PubMed:10570151}. Cytoplasm
CC {ECO:0000269|PubMed:10570151}. Note=May shuttle between cytoplasm and
CC nucleus. {ECO:0000269|PubMed:10570151}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylation
CC on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing.
CC Has no effect on subcellular location nor on homodimerization.
CC Phosphorylated in vitro by CDK2. Phosphorylation enhances interaction
CC with PPP1R8. {ECO:0000250|UniProtKB:Q99459}.
CC -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32228.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK172950; BAD32228.1; ALT_INIT; mRNA.
DR EMBL; BC031480; AAH31480.1; -; mRNA.
DR CCDS; CCDS37627.1; -.
DR RefSeq; NP_690023.1; NM_152810.2.
DR AlphaFoldDB; Q6A068; -.
DR BMRB; Q6A068; -.
DR SMR; Q6A068; -.
DR BioGRID; 214866; 100.
DR ComplexPortal; CPX-5825; PRP19-CDC5L complex.
DR IntAct; Q6A068; 23.
DR MINT; Q6A068; -.
DR STRING; 10090.ENSMUSP00000024727; -.
DR iPTMnet; Q6A068; -.
DR PhosphoSitePlus; Q6A068; -.
DR EPD; Q6A068; -.
DR jPOST; Q6A068; -.
DR MaxQB; Q6A068; -.
DR PaxDb; Q6A068; -.
DR PRIDE; Q6A068; -.
DR ProteomicsDB; 281434; -.
DR DNASU; 71702; -.
DR Ensembl; ENSMUST00000024727; ENSMUSP00000024727; ENSMUSG00000023932.
DR GeneID; 71702; -.
DR KEGG; mmu:71702; -.
DR UCSC; uc008cqj.2; mouse.
DR CTD; 988; -.
DR MGI; MGI:1918952; Cdc5l.
DR VEuPathDB; HostDB:ENSMUSG00000023932; -.
DR eggNOG; KOG0050; Eukaryota.
DR GeneTree; ENSGT00550000074922; -.
DR HOGENOM; CLU_009082_0_0_1; -.
DR InParanoid; Q6A068; -.
DR OMA; PFRTQRE; -.
DR OrthoDB; 975557at2759; -.
DR PhylomeDB; Q6A068; -.
DR TreeFam; TF101061; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 71702; 24 hits in 111 CRISPR screens.
DR ChiTaRS; Cdc5l; mouse.
DR PRO; PR:Q6A068; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6A068; protein.
DR Bgee; ENSMUSG00000023932; Expressed in undifferentiated genital tubercle and 271 other tissues.
DR ExpressionAtlas; Q6A068; baseline and differential.
DR Genevisible; Q6A068; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005662; C:DNA replication factor A complex; 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:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043522; F:leucine zipper domain binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0071987; F:WD40-repeat domain binding; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:1904568; P:cellular response to wortmannin; ISO:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR021786; Cdc5p/Cef1_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF11831; Myb_Cef; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Coiled coil; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA repair; DNA-binding; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spliceosome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..802
FT /note="Cell division cycle 5-like protein"
FT /id="PRO_0000197092"
FT DOMAIN 1..56
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 57..108
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 31..54
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 82..104
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 108..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..206
FT /note="Required for interaction with CTNNBL1"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT REGION 246..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..606
FT /note="Interaction with PPP1R8"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT REGION 408..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..659
FT /note="Interaction with DAPK3"
FT /evidence="ECO:0000250|UniProtKB:O08837"
FT REGION 706..800
FT /note="Interaction with PLRG1"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT COILED 142..245
FT /evidence="ECO:0000255"
FT COILED 676..701
FT /evidence="ECO:0000255"
FT COILED 764..802
FT /evidence="ECO:0000255"
FT MOTIF 165..271
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 108..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 415
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
SQ SEQUENCE 802 AA; 92190 MW; 7EFFBC4A1B7ABA3F CRC64;
MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK
TEWSREEEEK LLHLAKLMPT QWRTIAPIIG RTAAQCLEHY EFLLDKTAQR DNEEETTDDP
RKLKPGEIDP NPETKPARPD PIDMDEDELE MLSEARARLA NTQGKKAKRK AREKQLEEAR
RLAALQKRRE LRAAGIEIQK KRKKKRGVDY NAEIPFEKKP ALGFYDTSEE NYQALDADFR
KLRQQDLDGE LRSEKEGRDR KKDKQHLKRK KESDLPSAIL QTSGVSEFTK KRSKLVLPAP
QISDAELQEV VKVGQASEVA RQTAEESGIT NSASSTLLSE YNVTNNSIAL RTPRTPASQD
RILQEAQNLM ALTNVDTPLK GGLNTPLHES DFSGVTPQRQ VVQTPNTVLS TPFRTPSNGA
EGLTPRSGTT PKPVTNATPG RTPLRDKLNI NPEDGMADYS DPSYVKQMER ESREHLRLGL
LGLPAPKNDF EIVLPENAEK ELEEREIDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA
VQKDLPRPSE VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG
KNVGFATNNS EHITYLEHSP YEKFSKEDLK KAQDALVQEM EVVKQGMSHG ELSSEAYNQV
WEECYSQVLY LPAQSRYTRA NLASKKDRIE SLEKRLEINR GHMTTEAKRA AKMEKKMKIL
LGGYQSRAMG LMKQLNDLWD QIEQAHLELR TFEELKKHED SAIPRRLECL KEDVQRQQER
EKELQQRYAD LLMEKETLQA KF
