ID   ORC4_MOUSE              Reviewed;         433 AA.
AC   O88708; Q91V62; Q9QYX1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Origin recognition complex subunit 4;
GN   Name=Orc4; Synonyms=Orc4l;
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].
RA   Komrskova T., Yang H., Gavin K., Pappin P., Canas B., Kobayashi R.,
RA   Hunt T., Stillman B.;
RT   "Identification of the Orc4p and Orc5p subunits of the Xenopus and human
RT   origin recognition complex.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10460412; DOI=10.1007/s004120050374;
RA   Springer J., Kneissl M., Putter V., Grummt F.;
RT   "Identification and characterization of MmORC4 and MmORC5, two subunits of
RT   the mouse origin of replication recognition complex.";
RL   Chromosoma 108:243-249(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Liver, and 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   [7]
RP   INTERACTION WITH DBF4.
RX   PubMed=12614612; DOI=10.1016/s0022-2836(03)00079-2;
RA   Kneissl M., Puetter V., Szalay A.A., Grummt F.;
RT   "Interaction and assembly of murine pre-replicative complex proteins in
RT   yeast and mouse cells.";
RL   J. Mol. Biol. 327:111-128(2003).
CC   -!- FUNCTION: Binds histone H3 and H4 trimethylation marks H3K9me3,
CC       H3K27me3 and H4K20me3 (By similarity). Component of the origin
CC       recognition complex (ORC) that binds origins of replication. DNA-
CC       binding is ATP-dependent. The specific DNA sequences that define
CC       origins of replication have not been identified yet. ORC is required to
CC       assemble the pre-replication complex necessary to initiate DNA
CC       replication. {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 DBF4 (PubMed:12614612). Interacts with POLQ
CC       (By similarity). {ECO:0000250|UniProtKB:O43929,
CC       ECO:0000269|PubMed:12614612}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ORC4 family. {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; Y16386; CAA76188.1; -; mRNA.
DR   EMBL; AJ003140; CAA05896.1; -; mRNA.
DR   EMBL; AK010258; BAB26801.1; -; mRNA.
DR   EMBL; AK147823; BAE28161.1; -; mRNA.
DR   EMBL; AK169291; BAE41048.1; -; mRNA.
DR   EMBL; AL732317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466519; EDL26871.1; -; Genomic_DNA.
DR   EMBL; BC015072; AAH15072.1; -; mRNA.
DR   EMBL; BC019748; AAH19748.1; -; mRNA.
DR   CCDS; CCDS16022.1; -.
DR   RefSeq; NP_036088.3; NM_011958.3.
DR   RefSeq; XP_006498126.1; XM_006498063.3.
DR   RefSeq; XP_006498127.1; XM_006498064.3.
DR   RefSeq; XP_006498128.1; XM_006498065.3.
DR   AlphaFoldDB; O88708; -.
DR   SMR; O88708; -.
DR   BioGRID; 204980; 1.
DR   ComplexPortal; CPX-1915; Nuclear origin recognition complex.
DR   CORUM; O88708; -.
DR   STRING; 10090.ENSMUSP00000028098; -.
DR   iPTMnet; O88708; -.
DR   PhosphoSitePlus; O88708; -.
DR   EPD; O88708; -.
DR   MaxQB; O88708; -.
DR   PaxDb; 10090-ENSMUSP00000028098; -.
DR   PeptideAtlas; O88708; -.
DR   ProteomicsDB; 293521; -.
DR   Pumba; O88708; -.
DR   Antibodypedia; 4189; 271 antibodies from 33 providers.
DR   DNASU; 26428; -.
DR   Ensembl; ENSMUST00000028098.11; ENSMUSP00000028098.5; ENSMUSG00000026761.13.
DR   GeneID; 26428; -.
DR   KEGG; mmu:26428; -.
DR   UCSC; uc008jpp.2; mouse.
DR   AGR; MGI:1347043; -.
DR   CTD; 5000; -.
DR   MGI; MGI:1347043; Orc4.
DR   VEuPathDB; HostDB:ENSMUSG00000026761; -.
DR   eggNOG; KOG2228; Eukaryota.
DR   GeneTree; ENSGT00390000016542; -.
DR   HOGENOM; CLU_007115_0_1_1; -.
DR   InParanoid; O88708; -.
DR   OMA; ETKFRHH; -.
DR   OrthoDB; 230201at2759; -.
DR   PhylomeDB; O88708; -.
DR   TreeFam; TF101094; -.
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; 26428; 27 hits in 78 CRISPR screens.
DR   ChiTaRS; Orc4; mouse.
DR   PRO; PR:O88708; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O88708; Protein.
DR   Bgee; ENSMUSG00000026761; Expressed in otic placode and 267 other cell types or tissues.
DR   ExpressionAtlas; O88708; baseline and differential.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
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:0003688; F:DNA replication origin binding; ISO:MGI.
DR   GO; GO:0000166; F:nucleotide binding; ISO:MGI.
DR   GO; GO:0006260; P:DNA replication; IMP:MGI.
DR   GO; GO:0006270; P:DNA replication initiation; ISO:MGI.
DR   GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:MGI.
DR   GO; GO:0051258; P:protein polymerization; IDA:MGI.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR016527; ORC4.
DR   InterPro; IPR032705; ORC4_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12087; ORIGIN RECOGNITION COMPLEX SUBUNIT 4; 1.
DR   PANTHER; PTHR12087:SF0; ORIGIN RECOGNITION COMPLEX SUBUNIT 4; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF14629; ORC4_C; 1.
DR   PIRSF; PIRSF007858; ORC4; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; O88708; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA replication; DNA-binding; Methylation; Nucleotide-binding;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..433
FT                   /note="Origin recognition complex subunit 4"
FT                   /id="PRO_0000127088"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43929"
FT   CONFLICT        141
FT                   /note="Q -> K (in Ref. 1; CAA76188)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   433 AA;  49982 MW;  9857AB8CCF41982D CRC64;
     MSSRKTKSNA HAECLSQVQR ILRERFCHHS PHSNLFGVQV QYKHLIELLK RTAIYGESNS
     VLIVGPRGSG KTTLLNHALK ELMEIEVSEN VIQVHLNGLL QTNEKIALKE ITRQLNLDNV
     VEDKVFGSFA ENLSFLLEAL QKGDRTSSCP VIFILDEFDI FAHQKNQTLL YNLFDISQSA
     QTPVAVIGLT CRLDILELLE KRVKSRFSHR QIHLMNSFDF PQYLKIFKEQ LSLPAEFPDK
     AFAERWNENV HCLSEDSTVL EVLQKHFSVN KNLQSLHMLL MLALNRVTVS HPFMTSADLM
     EAQHMCSLDS KANIVHGLSV LEICLIIAMK HLNDIYEEEP FNFQMVYNEF QKFIQRKAHS
     VYNFEKPVVM KAFEHLQQLE LIKPVERTSV NSQREYQLVK LLLDNTQIMN ALQKYSNCPT
     DVRQWATSSL SWL
//