CDC5L_RAT
ID CDC5L_RAT Reviewed; 802 AA.
AC O08837;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cell division cycle 5-like protein;
DE AltName: Full=Cdc5-like protein;
DE AltName: Full=Pombe Cdc5-related protein;
GN Name=Cdc5l; Synonyms=Pcdc5rp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND
RP DNA-BINDING.
RC STRAIN=Noble;
RX PubMed=11694351; DOI=10.1016/s0303-7207(01)00585-8;
RA Johnson L.M., Too C.K.L.;
RT "Prolactin, interleukin-2 and FGF-2 stimulate expression, nuclear
RT distribution and DNA-binding of rat homolog of pombe Cdc5 in Nb2 T lymphoma
RT cells.";
RL Mol. Cell. Endocrinol. 184:151-161(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DAPK3, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fibroblast;
RX PubMed=11884640; DOI=10.1093/nar/30.6.1408;
RA Engemann H., Heinzel V., Page G., Preuss U., Scheidtmann K.H.;
RT "DAP-like kinase interacts with the rat homolog of Schizosaccharomyces
RT pombe CDC5 protein, a factor involved in pre-mRNA splicing and required for
RT G2/M phase transition.";
RL Nucleic Acids Res. 30:1408-1417(2002).
RN [3]
RP PROTEIN SEQUENCE OF 34-40; 400-414; 467-473; 478-487 AND 689-694, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION, AND INTERACTION WITH PPP1R8.
RX PubMed=10827081; DOI=10.1074/jbc.m001676200;
RA Boudrez A., Beullens M., Groenen P.M.A., Van Eynde A., Vulsteke V.,
RA Jagiello I., Murray M., Krainer A.R., Stalmans W., Bollen M.;
RT "NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a
RT regulator of pre-mRNA splicing and mitotic entry.";
RL J. Biol. Chem. 275:25411-25417(2000).
RN [5]
RP INTERACTION WITH PRPF19.
RX PubMed=16352598; DOI=10.1074/jbc.m510881200;
RA Urano Y., Iiduka M., Sugiyama A., Akiyama H., Uzawa K., Matsumoto G.,
RA Kawasaki Y., Tashiro F.;
RT "Involvement of the mouse Prp19 gene in neuronal/astroglial cell fate
RT decisions.";
RL J. Biol. Chem. 281:7498-7514(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-377; THR-385 AND THR-396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (PubMed:11884640). Component
CC of the precatalytic, catalytic and postcatalytic spliceosome complexes
CC (By similarity). Part of a spliceosomal 'core' complex consisting of
CC CDC5L, PLRG1, SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1,
CC Lodestar/TTF2, and NIPP1/PPP1R8 (PubMed:10827081). Identified in the
CC spliceosome C complex. Component of the PRP19-CDC5L splicing complex
CC composed of a core complex comprising a homotetramer of PRPF19, CDC5L,
CC PLRG1 and BCAS2, and at least three less stably associated proteins
CC CTNNBL1, CWC15 and HSPA8. Interacts (via its C-terminus) directly in
CC the complex with PRPF19 and BCAS2. Interacts (via its C-terminus)
CC directly with PRGL1 (via its WD40 repeat domain); the interaction is
CC required for mRNA splicing but not for spliceosome assembly. Also
CC interacts with CTNNBL1. Interacts with PRPF19 (via N-terminus)
CC (PubMed:16352598). Interacts with USB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q99459, ECO:0000269|PubMed:10827081,
CC ECO:0000269|PubMed:11884640, ECO:0000269|PubMed:16352598}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:11694351, ECO:0000269|PubMed:11884640}. Nucleus
CC speckle {ECO:0000255|PROSITE-ProRule:PRU00625}. Cytoplasm
CC {ECO:0000269|PubMed:11694351}. Note=May shuttle between cytoplasm and
CC nucleus. {ECO:0000303|PubMed:11694351}.
CC -!- INDUCTION: By prolactin, IL-2 and FGF-2 in prolactin-dependent lymphoid
CC cells (at protein level). {ECO:0000269|PubMed:11694351}.
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 (By similarity). Phosphorylation
CC enhances interaction with PPP1R8. {ECO:0000250,
CC ECO:0000269|PubMed:10827081}.
CC -!- SIMILARITY: Belongs to the CEF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF000578; AAD05365.2; -; mRNA.
DR RefSeq; NP_445979.1; NM_053527.1.
DR AlphaFoldDB; O08837; -.
DR BMRB; O08837; -.
DR SMR; O08837; -.
DR IntAct; O08837; 4.
DR STRING; 10116.ENSRNOP00000027264; -.
DR iPTMnet; O08837; -.
DR PhosphoSitePlus; O08837; -.
DR jPOST; O08837; -.
DR PaxDb; O08837; -.
DR PRIDE; O08837; -.
DR Ensembl; ENSRNOT00000027264; ENSRNOP00000027264; ENSRNOG00000019975.
DR GeneID; 85434; -.
DR KEGG; rno:85434; -.
DR UCSC; RGD:70892; rat.
DR CTD; 988; -.
DR RGD; 70892; Cdc5l.
DR eggNOG; KOG0050; Eukaryota.
DR GeneTree; ENSGT00550000074922; -.
DR HOGENOM; CLU_009082_0_0_1; -.
DR InParanoid; O08837; -.
DR OMA; PFRTQRE; -.
DR OrthoDB; 975557at2759; -.
DR PhylomeDB; O08837; -.
DR TreeFam; TF101061; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:O08837; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019975; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; O08837; baseline and differential.
DR Genevisible; O08837; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; IDA:RGD.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
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:RGD.
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:RGD.
DR GO; GO:0043522; F:leucine zipper domain binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:RGD.
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:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:RGD.
DR GO; GO:0071987; F:WD40-repeat domain binding; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071352; P:cellular response to interleukin-2; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:RGD.
DR GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
DR GO; GO:1904568; P:cellular response to wortmannin; IDA:RGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:RGD.
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:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:RGD.
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_0000197093"
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:0000269|PubMed:11884640"
FT REGION 706..800
FT /note="Interaction with PLRG1"
FT /evidence="ECO:0000250|UniProtKB:Q99459"
FT COILED 146..192
FT /evidence="ECO:0000255"
FT COILED 676..701
FT /evidence="ECO:0000255"
FT COILED 761..801
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:0007744|PubMed:22673903"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 92218 MW; 3795F3D37E10FCC8 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 ELEEREMDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA
VQKDLPRPSE VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG
KNVGFATNNS EHITYLEHSP YEKFSKEDLK KAQDVLVQEM EVVKQGMSHG ELSSEAYNQV
WEECYSQVLY LPAQSRYTRA NLASKKDRIE SLEKRLEINR GHMTTEAKRA AKMEKKMKIL
LGGYQSRAMG LLKQLNDLWD QIEQAHLELR TFEELKKHED SAIPRRLECL KEDVQRQQER
EKELQQRYAD LLMEKETLQA KF
