GRWD1_MOUSE
ID GRWD1_MOUSE Reviewed; 446 AA.
AC Q810D6; G3UVT6; Q922H3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glutamate-rich WD repeat-containing protein 1;
DE AltName: Full=Protein A301;
GN Name=Grwd1; Synonyms=A301;
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 [MRNA].
RC STRAIN=ICR; TISSUE=Forebrain;
RA Sakuma-Takagi M., Ichimiya T., Kurihara T.;
RT "Isolation of the cDNA encoding a novel WD repeat protein (A301) from mouse
RT brain.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-446.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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: 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 (By similarity). {ECO:0000250|UniProtKB:Q9BQ67}.
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DR EMBL; AB001539; BAC66461.1; -; mRNA.
DR EMBL; AC149053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466603; EDL22902.1; -; Genomic_DNA.
DR EMBL; BC008121; AAH08121.1; -; mRNA.
DR CCDS; CCDS21266.2; -.
DR RefSeq; NP_700468.2; NM_153419.2.
DR AlphaFoldDB; Q810D6; -.
DR SMR; Q810D6; -.
DR BioGRID; 221697; 2.
DR IntAct; Q810D6; 1.
DR STRING; 10090.ENSMUSP00000116252; -.
DR iPTMnet; Q810D6; -.
DR PhosphoSitePlus; Q810D6; -.
DR SwissPalm; Q810D6; -.
DR EPD; Q810D6; -.
DR jPOST; Q810D6; -.
DR MaxQB; Q810D6; -.
DR PaxDb; Q810D6; -.
DR PRIDE; Q810D6; -.
DR ProteomicsDB; 271465; -.
DR Antibodypedia; 31711; 136 antibodies from 22 providers.
DR Ensembl; ENSMUST00000107723; ENSMUSP00000103351; ENSMUSG00000053801.
DR Ensembl; ENSMUST00000131384; ENSMUSP00000116252; ENSMUSG00000053801.
DR GeneID; 101612; -.
DR KEGG; mmu:101612; -.
DR UCSC; uc009gxj.2; mouse.
DR CTD; 83743; -.
DR MGI; MGI:2141989; Grwd1.
DR VEuPathDB; HostDB:ENSMUSG00000053801; -.
DR eggNOG; KOG0302; Eukaryota.
DR GeneTree; ENSGT00550000075124; -.
DR HOGENOM; CLU_025272_1_1_1; -.
DR InParanoid; Q810D6; -.
DR OMA; DWSPLQP; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q810D6; -.
DR TreeFam; TF312982; -.
DR BioGRID-ORCS; 101612; 31 hits in 77 CRISPR screens.
DR PRO; PR:Q810D6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q810D6; protein.
DR Bgee; ENSMUSG00000053801; Expressed in internal carotid artery and 263 other tissues.
DR ExpressionAtlas; Q810D6; baseline and differential.
DR Genevisible; Q810D6; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
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 1: Evidence at protein level;
KW Chromosome; Nucleus; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..446
FT /note="Glutamate-rich WD repeat-containing protein 1"
FT /id="PRO_0000051012"
FT REPEAT 212..252
FT /note="WD 1"
FT REPEAT 259..299
FT /note="WD 2"
FT REPEAT 306..345
FT /note="WD 3"
FT REPEAT 351..391
FT /note="WD 4"
FT REPEAT 412..445
FT /note="WD 5"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
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 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ67"
FT CONFLICT 391
FT /note="S -> P (in Ref. 1; BAC66461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49224 MW; B008DEE44FC98433 CRC64;
MAARKGRSRT CETGEPMEAE TCDPGTEGPS QVYLPGRGPP LSEGEELVMD EEAYVLYHRA
QTGAPCLSFD IVRDHLGDNR TELPLSLYLC AGTQAESAQS NRLMMLRMHN LHGTRPSPSE
GSDDDEEDED EEDEEEQKPQ LELAMVPHYG GINRVRVSWL GEEPVAGVWS EKGQVEVFAL
RRLLQVVDDP QALAIFLRDE QARIKPIFSF AGHMGEGFAL DWSPRVPGRL LTGDCQKNVH
LWTPTEGGSW NVDQRPFVGH TRSVEDLQWS PTEDTVFASC SADASIRIWD IRAAPGKACM
LTTATAHDGD VNVISWSRRE PFLLSGGDDG ALKVWDLRQF KSGSPVATFK QHMAPVTSVE
WHPQDSGVFA ASGADNQITQ WDLAVERDPE SGETETDPGL AALPQQLLFV HQGETDLKEL
HWHPQCPGVL ISTALSGFTV FRTISV
