ID ORC1_MOUSE Reviewed; 840 AA.
AC Q9Z1N2; A2A8R3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=Orc1; Synonyms=Orc1l;
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].
RX PubMed=9862484; DOI=10.1007/s004380050898;
RA Zisimopoulou P., Staib C., Nanda I., Schmid M., Grummt F.;
RT "Mouse homolog of the yeast origin recognition complex subunit ORC1 and
RT chromosomal localization of the cognate mouse gene Orc1.";
RL Mol. Gen. Genet. 260:295-299(1998).
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 MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-258 AND SER-332, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 9-170, AND INTERACTION WITH
RP H4K20ME2.
RX PubMed=22398447; DOI=10.1038/nature10956;
RA Kuo A.J., Song J., Cheung P., Ishibe-Murakami S., Yamazoe S., Chen J.K.,
RA Patel D.J., Gozani O.;
RT "The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and
RT Meier-Gorlin syndrome.";
RL Nature 484:115-119(2012).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent. The specific DNA
CC sequences that define origins of replication have not been identified
CC yet. ORC is required to assemble the pre-replication complex necessary
CC to initiate DNA replication (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase (By
CC similarity). Interacts with CDC6 and KAT7/HBO1 (By similarity).
CC Interacts with LRWD1 predominantly during the G1 phase and with less
CC affinity during mitosis, when phosphorylated (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The BAH domain mediates binding to dimethylated histone H4
CC 'Lys-20' (H4K20me2), which is enriched at replication origins.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; AJ003133; CAA05890.1; -; mRNA.
DR EMBL; AL626783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015073; AAH15073.1; -; mRNA.
DR CCDS; CCDS18453.1; -.
DR RefSeq; NP_035145.2; NM_011015.2.
DR PDB; 4DOV; X-ray; 1.70 A; A/C=9-170.
DR PDB; 4DOW; X-ray; 1.95 A; A/B=9-170.
DR PDBsum; 4DOV; -.
DR PDBsum; 4DOW; -.
DR AlphaFoldDB; Q9Z1N2; -.
DR SMR; Q9Z1N2; -.
DR BioGRID; 201974; 12.
DR ComplexPortal; CPX-1915; Nuclear origin recognition complex.
DR CORUM; Q9Z1N2; -.
DR DIP; DIP-32115N; -.
DR IntAct; Q9Z1N2; 6.
DR STRING; 10090.ENSMUSP00000099805; -.
DR iPTMnet; Q9Z1N2; -.
DR PhosphoSitePlus; Q9Z1N2; -.
DR EPD; Q9Z1N2; -.
DR jPOST; Q9Z1N2; -.
DR MaxQB; Q9Z1N2; -.
DR PaxDb; 10090-ENSMUSP00000099805; -.
DR PeptideAtlas; Q9Z1N2; -.
DR ProteomicsDB; 293939; -.
DR Pumba; Q9Z1N2; -.
DR Antibodypedia; 19104; 255 antibodies from 32 providers.
DR DNASU; 18392; -.
DR Ensembl; ENSMUST00000102744.4; ENSMUSP00000099805.4; ENSMUSG00000028587.19.
DR GeneID; 18392; -.
DR KEGG; mmu:18392; -.
DR UCSC; uc008ubh.2; mouse.
DR AGR; MGI:1328337; -.
DR CTD; 4998; -.
DR MGI; MGI:1328337; Orc1.
DR VEuPathDB; HostDB:ENSMUSG00000028587; -.
DR eggNOG; KOG1514; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_0_1_1; -.
DR InParanoid; Q9Z1N2; -.
DR OMA; CKQHLLG; -.
DR OrthoDB; 118994at2759; -.
DR PhylomeDB; Q9Z1N2; -.
DR TreeFam; TF313743; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-MMU-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR BioGRID-ORCS; 18392; 25 hits in 83 CRISPR screens.
DR ChiTaRS; Orc1; mouse.
DR PRO; PR:Q9Z1N2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z1N2; Protein.
DR Bgee; ENSMUSG00000028587; Expressed in animal zygote and 141 other cell types or tissues.
DR Genevisible; Q9Z1N2; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; TAS:MGI.
DR GO; GO:0000808; C:origin recognition complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; TAS:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; TAS:MGI.
DR GO; GO:0006270; P:DNA replication initiation; ISO:MGI.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR CDD; cd08768; Cdc6_C; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10763:SF23; ORIGIN RECOGNITION COMPLEX SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51038; BAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..840
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127068"
FT DOMAIN 44..170
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 195..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..840
FT /note="Necessary and sufficient for ORC complex assembly"
FT /evidence="ECO:0000250"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 513..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 600
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT SITE 93
FT /note="Histone H4K20me2 binding"
FT /evidence="ECO:0000269|PubMed:22398447"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 230
FT /note="N -> S (in Ref. 1; CAA05890 and 3; AAH15073)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:4DOV"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4DOV"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4DOV"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4DOW"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4DOV"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:4DOV"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4DOV"
SQ SEQUENCE 840 AA; 95103 MW; 12769943A354CA8B CRC64;
MPSYLTRQKT RQTFSWVGRP LPNRKQFQQM YREICMKIND GSEIHIKVGQ FVLIQGEDNK
KPYVAKLIEL FQNGAEVPPK KCARVQWFVR FLEIPVSKRH LLGRSPPAQE IFWYDCSDWD
NKINVETIIG PVQVVALAPE EVIPVDQKSE ETLFVKLSWN KKDFAPLPPE VLAALREQED
SPEWQKPLKA KIKNVKSPAR NTTEQEVKGI KSNHSTSKFH QTPANIVIPN AKKSLELDGL
GFTRKPNTRW SKKSSCDSLD YQKTSKRRAA FSETTSPPKK PNKPREIKPS SALETRVKNG
QTQPFCAKSS VVLRARNPAM TTTKLGVDNT LSPIRNGLRS SVVPSGGLTP VYIRRKAKEQ
ETHKEPIRTS RVHRKSSLLT LKRIRQQLCL LDGDDRDQEE EESVDSESEE EDEFISSLPT
RNSLGQSRTR QTPSKSPQKN PKPRTPHRAT PQIRDRNLAV QEPASALEEA RLRLHVSAVP
DSLPCREQEF QDIYSFVESK LLDGTGGCMY ISGVPGTGKT ATVHEVIRCL QQAAETDDVP
PFQYVEVNGM KLTEPHQVYV QILKKLTGQK ATANHAAELL AKQFCGQGSQ KETTVLLVDE
LDLLWTHKQD VMYNLFDWPT HKGAHLIVLT IANTMDLPER IMMNRVSSRL GLTRMSFQPY
SHSQLKQILV SRLRNLRAFE DDAIQLVARK VAALSGDARR CLDICRRATE ICELSHLRGD
SLSLVTVAHL MEAIDEMFSS SYITAIKNSS VVEQSFLRAI IAEFRRSGLE EATFQQIYSQ
HVALCRMEGL PYPTMSETMA VCSRLGSCRL LLVEPSRNDL LLRVRLNVSQ NDVLFALKEE
//
