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ORC1_MOUSE
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   03-AUG-2022, entry version 164.
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 of replication 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; Q9Z1N2; -.
DR   PeptideAtlas; Q9Z1N2; -.
DR   PRIDE; Q9Z1N2; -.
DR   ProteomicsDB; 293939; -.
DR   Antibodypedia; 19104; 221 antibodies from 32 providers.
DR   DNASU; 18392; -.
DR   Ensembl; ENSMUST00000102744; ENSMUSP00000099805; ENSMUSG00000028587.
DR   GeneID; 18392; -.
DR   KEGG; mmu:18392; -.
DR   UCSC; uc008ubh.2; mouse.
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; ICEFSCQ; -.
DR   OrthoDB; 935804at2759; -.
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 78 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 137 other tissues.
DR   Genevisible; Q9Z1N2; MM.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
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; ISO: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:0003688; F:DNA replication origin binding; IBA:GO_Central.
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; 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; 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; -; 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   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
 
 
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