ORC1_RAT
ID ORC1_RAT Reviewed; 848 AA.
AC Q80Z32;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Origin recognition complex subunit 1;
GN Name=Orc1; Synonyms=Orc1l;
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 [MRNA].
RA Saitoh Y., Ushio K., Tsutsumi K.;
RT "Rat origin recognition complex, subunit 1.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; AB105378; BAC65338.1; -; mRNA.
DR RefSeq; NP_808792.1; NM_177931.2.
DR AlphaFoldDB; Q80Z32; -.
DR SMR; Q80Z32; -.
DR STRING; 10116.ENSRNOP00000012492; -.
DR iPTMnet; Q80Z32; -.
DR PhosphoSitePlus; Q80Z32; -.
DR PaxDb; Q80Z32; -.
DR PRIDE; Q80Z32; -.
DR GeneID; 313479; -.
DR KEGG; rno:313479; -.
DR UCSC; RGD:631435; rat.
DR CTD; 4998; -.
DR RGD; 631435; Orc1.
DR eggNOG; KOG1514; Eukaryota.
DR InParanoid; Q80Z32; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; Q80Z32; -.
DR Reactome; R-RNO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-RNO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-RNO-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q80Z32; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000808; C:origin recognition complex; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
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; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR CDD; cd08768; Cdc6_C; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR020793; ORC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763:SF23; PTHR10763:SF23; 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; SSF52540; 1.
DR PROSITE; PS51038; BAH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; DNA replication; DNA-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..848
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000330357"
FT DOMAIN 44..170
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 189..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..848
FT /note="Necessary and sufficient for ORC complex assembly"
FT /evidence="ECO:0000250"
FT COMPBIAS 262..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 521..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 607
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 608
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 707
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:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
SQ SEQUENCE 848 AA; 95760 MW; 957F3C3FE4A99F48 CRC64;
MPSYVTRQKT RQTFSWVGRP LPNRKQFYQM YKEICMKING CSEIHIKVGQ FVLIQGEDNQ
KPYVAKLIEL FENGSEVPPK KYARVQWFVR FCEIPIPKRH LLGRRPSAQE IFWYDCSDCD
NDIHVETIIG PVQVVALAPE DEIPVNQKSE ETLFVKLSWN KKNFAPLPPE ELAALRRLEC
QKPLEAKTKS VKSPSWSTAE QEVKRIESSH STSRSYQDPA HTVTPNAMKS LECGGFTRKP
NMRLSRKILC DSLDSQKTCK RRAAFSETTS PPKKPQPGEI KTSSALETLG KNGHTQPFFA
KSSMVLRTRG TAVKTTKLTV ESALSPVRSR SRYSVAPSVG LTPQYIGRKA KEQETHKEPI
HTSLRARRRS SLLTLKRIKQ QLWLLDDDKS DQEEEESISS VEVSDSSSEE EDESVPSPPT
GKPVGQSRTR RTASKPSSQT PSKSPKKTFR PRPPLHATPQ IRDRNLAVQE PASVLEEARL
RLHVSAVPDS LPCREQEFQD IYSFVESKLL DGTGGCMYIS GVPGTGKTAT VHEVIRCLQQ
AAQTNDVPPF EYVEVNGMKL TEPHQVYVQI LQKLTGQKAT ANHAAELLAK QFCSRGSQKE
TTVLLVDELD LLWTHKQDVL YNLFDWPTHK GARLVVLTIA NTMDLPERIM MNRVASRLGL
TRMSFQPYSH SQLKQILVSR LKHLKAFEDD AVQLVARKVA ALSGDARRCL DICRRATEIC
EVSHQRGDSQ CLVTVAHLME AIDEMFSSSY ITAIKNSSVL EQSFLRAIIA EFRRSGLEEA
TFQQIYSQHV ALCRMEGLPY PTMSETMAVC SRLGSCRILL VEPSRNDLLL RVRLNVSQND
VLYALKEE
