GRWD1_RAT
ID GRWD1_RAT Reviewed; 445 AA.
AC Q5XI13;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glutamate-rich WD repeat-containing protein 1;
GN Name=Grwd1;
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=Testis;
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).
CC -!- FUNCTION: Histone binding-protein that regulates chromatin dynamics and
CC minichromosome maintenance (MCM) loading at replication origins,
CC possibly by promoting chromatin openness.
CC {ECO:0000250|UniProtKB:Q9BQ67}.
CC -!- SUBUNIT: Interacts with METTL18. Interacts with CDT1; origin binding of
CC GRWD1 is dependent on CDT1. Interacts with CDC6; origin binding of
CC GRWD1 is dependent on CDC6. Binds to histone H2A-H2B and H3-H4
CC complexes. {ECO:0000250|UniProtKB:Q9BQ67}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9BQ67}. Nucleus {ECO:0000250|UniProtKB:Q9BQ67}.
CC Chromosome {ECO:0000250|UniProtKB:Q9BQ67}. Note=Present in the nucleus
CC throughout interphase and is detached from chromatin at the onset of
CC mitosis and rebinds at telophase when the pre-replication complexes
CC (pre-RC) is formed. {ECO:0000250|UniProtKB:Q9BQ67}.
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DR EMBL; BC083883; AAH83883.1; -; mRNA.
DR RefSeq; NP_001012067.1; NM_001012067.1.
DR AlphaFoldDB; Q5XI13; -.
DR SMR; Q5XI13; -.
DR STRING; 10116.ENSRNOP00000053027; -.
DR jPOST; Q5XI13; -.
DR PaxDb; Q5XI13; -.
DR PRIDE; Q5XI13; -.
DR GeneID; 308592; -.
DR KEGG; rno:308592; -.
DR UCSC; RGD:1310649; rat.
DR CTD; 83743; -.
DR RGD; 1310649; Grwd1.
DR eggNOG; KOG0302; Eukaryota.
DR HOGENOM; CLU_025272_1_1_1; -.
DR InParanoid; Q5XI13; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q5XI13; -.
DR PRO; PR:Q5XI13; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q5XI13; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; ISS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..445
FT /note="Glutamate-rich WD repeat-containing protein 1"
FT /id="PRO_0000051013"
FT REPEAT 211..251
FT /note="WD 1"
FT REPEAT 258..298
FT /note="WD 2"
FT REPEAT 305..344
FT /note="WD 3"
FT REPEAT 350..390
FT /note="WD 4"
FT REPEAT 411..444
FT /note="WD 5"
FT REGION 110..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ67"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ67"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ67"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ67"
SQ SEQUENCE 445 AA; 49169 MW; AF6653A73976A0B3 CRC64;
MAARKGRRHT CETGEPMEAE TYDLGSEGPS QVYLPGRGPP LGEGEELVMD EEAYVLYHRA
QTGAPCLSFD IVRDHLGDNR TELPLSLYLC AGTQAESAQS NRLMMLRMHN LHGTRPPPSE
GSDDEDDEDE EDEEERKPQL ELAMVPHYGG INRVRVSWLG EEPVAGVWSE KGQVEVFALR
RLLQVVDDPQ ALAIFLRDEQ ARVKPIFSFA GHMGEGFALD WSPRVPGRLL TGDCQKNIHL
WTPTDGGSWN VDQRPFVGHT RSVEDLQWSP TEDTVFASCS ADASIRIWDI RAAPGKACML
TTAAAHDGDV NVISWSRREP FLLSGGDDGT LKVWDLRQFK SGSPVATFKQ HVAPVTSVEW
HPQDSGVFAA SGADNQITQW DLAVERDPES GETETDPGLA ALPQQLLFVH QGETDLKELH
WHPQCPGVLI STALSGFTVF RTISV