LRWD1_DANRE
ID LRWD1_DANRE Reviewed; 763 AA.
AC B0R160; Q503J1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Leucine-rich repeat and WD repeat-containing protein 1;
DE AltName: Full=ORC-associated protein;
DE Short=ORCA;
DE AltName: Full=Origin recognition complex-associated protein;
GN Name=lrwd1; Synonyms=orca;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; THR-280 AND SER-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: Required for G1/S transition. Recruits and stabilizes the
CC origin recognition complex (ORC) onto chromatin during G1 to establish
CC pre-replication complex (preRC) and to heterochromatic sites in post-
CC replicated cells. Binds a combination of DNA and histone methylation
CC repressive marks on heterochromatin. Required for silencing of major
CC satellite repeats. May be important ORC2, ORC3 and ORC4 stability (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ORC complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UFC0}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q9UFC0}. Chromosome,
CC telomere {ECO:0000250|UniProtKB:Q9UFC0}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8BUI3}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9UFC0}.
CC -!- DOMAIN: The entire WD repeat region is required for the interaction
CC with ORC complex components, as well as for association with chromatin
CC and for binding to histone H3 and H4 trimethylation marks H3K9me3 and
CC H4K20me3. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRWD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH95309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AL935280; CAQ13767.1; -; Genomic_DNA.
DR EMBL; BC095309; AAH95309.1; ALT_INIT; mRNA.
DR RefSeq; NP_001292591.1; NM_001305662.1.
DR RefSeq; XP_017211530.1; XM_017356041.1.
DR AlphaFoldDB; B0R160; -.
DR SMR; B0R160; -.
DR STRING; 7955.ENSDARP00000050905; -.
DR iPTMnet; B0R160; -.
DR PaxDb; B0R160; -.
DR PeptideAtlas; B0R160; -.
DR PRIDE; B0R160; -.
DR Ensembl; ENSDART00000050906; ENSDARP00000050905; ENSDARG00000035147.
DR GeneID; 327124; -.
DR KEGG; dre:327124; -.
DR CTD; 222229; -.
DR ZFIN; ZDB-GENE-030131-5335; lrwd1.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154248; -.
DR HOGENOM; CLU_022994_0_0_1; -.
DR InParanoid; B0R160; -.
DR PhylomeDB; B0R160; -.
DR TreeFam; TF329554; -.
DR PRO; PR:B0R160; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000035147; Expressed in gastrula and 27 other tissues.
DR ExpressionAtlas; B0R160; baseline and differential.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR032675; LRR_dom_sf.
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; PF12799; LRR_4; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromatin regulator; Chromosome; Cytoplasm; Cytoskeleton;
KW DNA replication; Kinetochore; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Telomere; WD repeat.
FT CHAIN 1..763
FT /note="Leucine-rich repeat and WD repeat-containing protein
FT 1"
FT /id="PRO_0000403769"
FT REPEAT 22..43
FT /note="LRR 1"
FT REPEAT 48..69
FT /note="LRR 2"
FT REPEAT 70..91
FT /note="LRR 3"
FT REPEAT 92..113
FT /note="LRR 4"
FT REPEAT 499..539
FT /note="WD 1"
FT REPEAT 608..647
FT /note="WD 2"
FT REPEAT 653..704
FT /note="WD 3"
FT REPEAT 729..763
FT /note="WD 4"
FT REGION 206..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 15
FT /note="T -> P (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="K -> T (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="V -> I (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="M -> T (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="D -> G (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="I -> V (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="K -> D (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="I -> N (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="L -> Q (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="G -> V (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="K -> N (in Ref. 2; AAH95309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 85048 MW; 1361087984CA8DF5 CRC64;
MEKITEKILL EKSSTKTNKL DQIKTLNLSR MSLKSEDLPV PLLSKLCRLE KLDLSGNMLQ
KIPKGLRLPC LKILNCSNND MEDVLSLEAL TNLEELRLED NLYLTVNDEH KVIFLLPNLR
MFNGKDISST AHHIRHGSTE ILRKRVIGVW ERDFSLPDPI SAKSLAAVEK SFVNAACTQV
KYGPNSLSDY TKWRVEKIAK EYLKSLTSSE EEERVADTTP TKENKTKACD VGGNSITSPQ
KRTRNNTDVV AEASPRKSSR LVSAAPVEAS PRKSARVLNT PQKTQPVVSS PRKHARLTSA
ETPESSPRKS SRLENVTQKA ASQTESPRKP GMSTPTSKQA KCESPRKQSK QSTAKMEKST
PRKTTKAKLQ VPQEPVSLTP LHVLQCHSRQ NDPDDFSTQL WACAFEPQQD DSIDISGGSQ
TIATCGGETL CVINCESGLV LKKYKVPGED FFSLAWSTVL MSRTGGSARP CNILAAGGKR
GCVKLIHPRV NLAFGEFRVS RRAISIMRFN PRKPTFLFTG TYDKKIFLWD IGGLDQDYNF
KISKLLTLET SSTPLHLALL PSSPDTHLLS GCDEGLYCFD VQLSKNTLKR NEEIEIVFPI
YKKNDKKNNY RTIDGLSFLS DDVVASKSHM QGSIYLWSWS ATRASWNSRK KEVPAVILAE
LQWSSTDIPY LSLGTCPGYG YVVCGDEQGR LWMYHITDTM MENFKSGKTI SATEVLQWPS
PIRAGKGALE GPSINSTAMD PGLHYLVALT DKNMVVVWKR ESH
