CDC5L_BOVIN
ID CDC5L_BOVIN Reviewed; 802 AA.
AC Q2KJC1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cell division cycle 5-like protein;
DE Short=Cdc5-like protein;
GN Name=CDC5L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q99459,
CC ECO:0000255|PROSITE-ProRule:PRU00625}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q99459, ECO:0000255|PROSITE-ProRule:PRU00625}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q99459}. Note=May shuttle between
CC cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q99459}.
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 ---------------------------------------------------------------------------
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; BC105417; AAI05418.1; -; mRNA.
DR RefSeq; NP_001070010.1; NM_001076542.1.
DR AlphaFoldDB; Q2KJC1; -.
DR BMRB; Q2KJC1; -.
DR SMR; Q2KJC1; -.
DR STRING; 9913.ENSBTAP00000026654; -.
DR PaxDb; Q2KJC1; -.
DR PRIDE; Q2KJC1; -.
DR Ensembl; ENSBTAT00000026654; ENSBTAP00000026654; ENSBTAG00000020012.
DR GeneID; 767817; -.
DR KEGG; bta:767817; -.
DR CTD; 988; -.
DR VEuPathDB; HostDB:ENSBTAG00000020012; -.
DR VGNC; VGNC:27080; CDC5L.
DR eggNOG; KOG0050; Eukaryota.
DR GeneTree; ENSGT00550000074922; -.
DR HOGENOM; CLU_009082_0_0_1; -.
DR InParanoid; Q2KJC1; -.
DR OMA; PFRTQRE; -.
DR OrthoDB; 975557at2759; -.
DR TreeFam; TF101061; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000020012; Expressed in oocyte and 111 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005662; C:DNA replication factor A complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0071987; F:WD40-repeat domain binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
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; 1.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 2: Evidence at transcript level;
KW Activator; Cell cycle; Coiled coil; Cytoplasm; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..802
FT /note="Cell division cycle 5-like protein"
FT /id="PRO_0000238915"
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 409..459
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 409..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 437
FT /note="Phosphoserine"
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; 92270 MW; D8B27B0ECEAE0A79 CRC64;
MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK
TEWSREEEEK LLHLAKLMPT QWRTIAPIIG RTAAQCLEHY EFLLDKAAQR DNEEETTDDP
RKLKPGEIDP NPETKPARPD PIDMDEDELE MLSEARARLA NTQGKKAKRK AREKQLEEAR
RLAALQKRRE LRAAGIEIQK KRKKKRGVDY NAEIPFEKKP ALGFYDTSEE NYQTLDADFR
KLRQQDLDGE LRSEKEGRDR KKDKQHLKRK KESDLPSAIL QTSGVSEFTK KRSKLVLPAP
QISDAELQEV VKVGQASEIA RQTAEESGIT NSASSTLLSE YNVTNNSIAL RTPRTPASQD
RILQEAQNLM ALTNVDTPLK GGLNTPLHES DFSGVTPQRQ VVQTPNTVLS TPFRTPSHGS
EGLTPRSGTT PKPVINSTPG RTPLRDKLNI NPEDGMADYS DPSYVKQMER ESREHLRLGL
LGLPAPKNDF EIVLPENAEK ELEEREIDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA
VQKDLPRPSE VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG
KTVGFGTNNA EHIAYLEHNP YEKFSKEELK KAQDVLVQEM EVVKQGMSHG ELSSEAYNQV
WEECYSQVLY LPGQSRYTRA NLASKKDRIE SLEKRLEINR GHMTTEAKRA AKMEKKMKIL
LGGYQSRAMG LMKQLNDLWD QIEQAYLELR TFEELKKHED SAIPRRLECL KEDVQRQQER
EKELQHRYAD LLLEKETLKA KF
