CDA7L_RAT
ID CDA7L_RAT Reviewed; 438 AA.
AC Q4G059;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cell division cycle-associated 7-like protein;
GN Name=Cdca7l;
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 [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP 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: Plays a role in transcriptional regulation as a repressor
CC that inhibits monoamine oxidase A (MAOA) activity and gene expression
CC by binding to the promoter. Plays an important oncogenic role in
CC mediating the full transforming effect of MYC in medulloblastoma cells.
CC Involved in apoptotic signaling pathways; May act downstream of P38-
CC kinase and BCL-2, but upstream of CASP3/caspase-3 as well as
CC CCND1/cyclin D1 and E2F1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MYC (By similarity). Interacts (via IBM motifs)
CC with PSIP1 (via IBD domain); phosphorylation increases its affinity for
CC PSIP1 (By similarity). {ECO:0000250|UniProtKB:Q96GN5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Associates with chromatin. Translocates from cytoplasm to nucleus
CC under dexamethasone induction (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000250|UniProtKB:Q96GN5}.
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DR EMBL; BC098734; AAH98734.1; -; mRNA.
DR RefSeq; NP_001030125.1; NM_001034953.1.
DR AlphaFoldDB; Q4G059; -.
DR STRING; 10116.ENSRNOP00000061054; -.
DR iPTMnet; Q4G059; -.
DR PhosphoSitePlus; Q4G059; -.
DR PaxDb; Q4G059; -.
DR Ensembl; ENSRNOT00000064868; ENSRNOP00000061054; ENSRNOG00000005410.
DR GeneID; 619566; -.
DR KEGG; rno:619566; -.
DR UCSC; RGD:1564080; rat.
DR CTD; 55536; -.
DR RGD; 1564080; Cdca7l.
DR eggNOG; ENOG502QWH1; Eukaryota.
DR GeneTree; ENSGT00940000159108; -.
DR HOGENOM; CLU_035988_0_0_1; -.
DR InParanoid; Q4G059; -.
DR OMA; KAPCFKS; -.
DR OrthoDB; 1462540at2759; -.
DR PhylomeDB; Q4G059; -.
DR TreeFam; TF101076; -.
DR PRO; PR:Q4G059; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005410; Expressed in thymus and 18 other tissues.
DR ExpressionAtlas; Q4G059; baseline and differential.
DR Genevisible; Q4G059; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR040221; CDCA7/CDA7L.
DR InterPro; IPR033578; CDCA7L.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR PANTHER; PTHR31169; PTHR31169; 1.
DR PANTHER; PTHR31169:SF4; PTHR31169:SF4; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..438
FT /note="Cell division cycle-associated 7-like protein"
FT /id="PRO_0000249315"
FT REGION 55..114
FT /note="PSIP1-binding"
FT /evidence="ECO:0000250"
FT REGION 72..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..223
FT /note="MYC-binding"
FT /evidence="ECO:0000250"
FT MOTIF 9..33
FT /note="Integrase domain-binding motif 1 (IBM1)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOTIF 62..88
FT /note="Integrase domain-binding motif 2 (IBM2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT COMPBIAS 162..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922M5"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922M5"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GN5"
SQ SEQUENCE 438 AA; 49973 MW; 33D13AF4DE7F9612 CRC64;
MELATRSQIP KEVADIFNAP SDDEEFVGFQ DDVPMENLSE SCGSLDSLEL EKQNACLHSK
YFTEELRRIF KEDTDSDNED FEGFTESELN IGSNPELIES ELSDGDKTHP MMSDEEDDDD
EEEAAPRRGR QSTRSSFGLR VAFQFPTKKT AKTPDKNSPH LLGGKTDLRR EKSCRQPKEK
EDSASDAEDE SRAESQETSD ALLKRAMNIK ENKAMLAQLL AELNSVPDFF PVRTPPSASR
RRTPRRAFSE GQITRRVNPT RSARPPEKFA LENFTFSATK LTEELYSFRR RKTISGGKCQ
KYRRHRISSF RSVKDITEEE LENIAITVRD KVYDKVLGNT CHQCRQKTID TKTVCRNQGC
GGVRGQFCGP CLRNRYGEDV RTALLDPKWT CPPCRGICNC SYCRRRDGRC ATGILIHLAK
FYGYDNVKEY LESLQKQL
