ORC3_HUMAN
ID ORC3_HUMAN Reviewed; 711 AA.
AC Q9UBD5; A2A2T5; B4E025; Q13565; Q53GY6; Q5T159; Q6IUY7; Q86TN5; Q9UG44;
AC Q9UNT6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Origin recognition complex subunit 3;
DE AltName: Full=Origin recognition complex subunit Latheo;
GN Name=ORC3; Synonyms=LATHEO, ORC3L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Tugal T., Zou-Yang X.H., Gavin K., Pappin D., Canas B., Kobayashi R.,
RA Hunt T., Stillman B.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dean F.B., O'Donnell M.;
RT "cDNA cloning of a homolog for Saccharomyces cerevisiae ORC3 from Homo
RT sapiens.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10402192; DOI=10.1016/s0896-6273(00)80752-7;
RA Pinto S., Quintana D.G., Smith P., Mihalek R.M., Hou Z.-H., Boynton S.,
RA Jones C.J., Handricks M., Velinzon K., Wohlschlegel J.A., Austin R.J.,
RA Lane W.S., Dutta A., Tully T.;
RT "Latheo encodes a subunit of the origin recognition complex and disrupts
RT neuronal proliferation and adult olfactory memory when mutant.";
RL Neuron 23:45-54(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-94; ARG-126; ILE-217;
RP VAL-247 AND THR-626.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-671 (ISOFORM 2).
RC TISSUE=Testis, and Uterus;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-542 (ISOFORM 1).
RC TISSUE=Brain;
RA Mihalek R., Homanics G.E.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP IDENTIFICATION IN THE ORC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ASSEMBLY OF THE ORC COMPLEX.
RX PubMed=12909626; DOI=10.1074/jbc.m307535200;
RA Ohta S., Tatsumi Y., Fujita M., Tsurimoto T., Obuse C.;
RT "The ORC1 cycle in human cells: II. Dynamic changes in the human ORC
RT complex during the cell cycle.";
RL J. Biol. Chem. 278:41535-41540(2003).
RN [12]
RP RECONSTITUTION OF THE ORC COMPLEX, AND DISASSEMBLY OF THE ORC COMPLEX.
RX PubMed=17716973; DOI=10.1074/jbc.m705905200;
RA Siddiqui K., Stillman B.;
RT "ATP-dependent assembly of the human origin recognition complex.";
RL J. Biol. Chem. 282:32370-32383(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION, AND BINDING TO HISTONE H3 AND H4 TRIMETHYLATION MARKS.
RX PubMed=22427655; DOI=10.1074/jbc.m111.337980;
RA Chan K.M., Zhang Z.;
RT "Leucine-rich repeat and WD repeat-containing protein 1 is recruited to
RT pericentric heterochromatin by trimethylated lysine 9 of histone H3 and
RT maintains heterochromatin silencing.";
RL J. Biol. Chem. 287:15024-15033(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=31160578; DOI=10.1038/s41467-019-10321-x;
RA Coulombe P., Nassar J., Peiffer I., Stanojcic S., Sterkers Y.,
RA Delamarre A., Bocquet S., Mechali M.;
RT "The ORC ubiquitin ligase OBI1 promotes DNA replication origin firing.";
RL Nat. Commun. 10:2426-2426(2019).
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. Binds histone H3 and H4 trimethylation
CC marks H3K9me3, H3K27me3 and H4K20me3. {ECO:0000269|PubMed:22427655,
CC ECO:0000269|PubMed:31160578}.
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.
CC {ECO:0000269|PubMed:12909626}.
CC -!- INTERACTION:
CC Q9UBD5; Q13415: ORC1; NbExp=16; IntAct=EBI-374916, EBI-374847;
CC Q9UBD5; Q13416: ORC2; NbExp=28; IntAct=EBI-374916, EBI-374957;
CC Q9UBD5; O43929: ORC4; NbExp=12; IntAct=EBI-374916, EBI-374889;
CC Q9UBD5; O43913: ORC5; NbExp=15; IntAct=EBI-374916, EBI-374928;
CC Q9UBD5; Q9Y5N6: ORC6; NbExp=4; IntAct=EBI-374916, EBI-374840;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31160578}. Chromosome
CC {ECO:0000269|PubMed:31160578}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UBD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBD5-2; Sequence=VSP_017129;
CC Name=3;
CC IsoId=Q9UBD5-3; Sequence=VSP_044893;
CC -!- PTM: Multi-mono-ubiquitinated by OBI1; ubiquitination is important for
CC efficient DNA replication origin site activation. Ubiquitination levels
CC are low in mitotic and early G1-phAse cells and are induced in late
CC G1-/early S-phase, peaking in S-phase and decrease toward the end of
CC the cell cycle. {ECO:0000269|PubMed:31160578}.
CC -!- SIMILARITY: Belongs to the ORC3 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/orc3l/";
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DR EMBL; AF135044; AAD30282.1; -; mRNA.
DR EMBL; AF125507; AAD18057.1; -; mRNA.
DR EMBL; AF093535; AAD40220.1; -; mRNA.
DR EMBL; AL080116; CAB45715.1; -; mRNA.
DR EMBL; AK222795; BAD96515.1; -; mRNA.
DR EMBL; AK303195; BAG64287.1; -; mRNA.
DR EMBL; AK315911; BAH14282.1; -; mRNA.
DR EMBL; AY623113; AAT38109.1; -; Genomic_DNA.
DR EMBL; AL451126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035494; AAH35494.1; -; mRNA.
DR EMBL; BC047689; AAH47689.1; ALT_TERM; mRNA.
DR EMBL; U50950; AAA96313.1; -; mRNA.
DR CCDS; CCDS43486.1; -. [Q9UBD5-1]
DR CCDS; CCDS5012.1; -. [Q9UBD5-2]
DR CCDS; CCDS56440.1; -. [Q9UBD5-3]
DR PIR; T12452; T12452.
DR RefSeq; NP_001184188.1; NM_001197259.1. [Q9UBD5-3]
DR RefSeq; NP_036513.2; NM_012381.3. [Q9UBD5-1]
DR RefSeq; NP_862820.1; NM_181837.2. [Q9UBD5-2]
DR PDB; 5UJ8; X-ray; 6.00 A; A/B/C/D=1-711.
DR PDB; 5UJM; EM; 18.00 A; C=1-711.
DR PDB; 7CTE; EM; 3.80 A; C=1-711.
DR PDB; 7CTF; EM; 4.80 A; C=1-711.
DR PDB; 7CTG; EM; 5.00 A; C=1-711.
DR PDB; 7JPO; EM; 3.20 A; C=1-711.
DR PDB; 7JPP; EM; 3.70 A; C=1-711.
DR PDB; 7JPQ; EM; 3.50 A; C=1-711.
DR PDB; 7JPR; EM; 4.00 A; C=1-711.
DR PDB; 7JPS; EM; 4.40 A; C=1-711.
DR PDBsum; 5UJ8; -.
DR PDBsum; 5UJM; -.
DR PDBsum; 7CTE; -.
DR PDBsum; 7CTF; -.
DR PDBsum; 7CTG; -.
DR PDBsum; 7JPO; -.
DR PDBsum; 7JPP; -.
DR PDBsum; 7JPQ; -.
DR PDBsum; 7JPR; -.
DR PDBsum; 7JPS; -.
DR AlphaFoldDB; Q9UBD5; -.
DR SMR; Q9UBD5; -.
DR BioGRID; 117130; 83.
DR ComplexPortal; CPX-1880; Nuclear origin of replication recognition complex.
DR CORUM; Q9UBD5; -.
DR DIP; DIP-31735N; -.
DR IntAct; Q9UBD5; 48.
DR MINT; Q9UBD5; -.
DR STRING; 9606.ENSP00000257789; -.
DR iPTMnet; Q9UBD5; -.
DR PhosphoSitePlus; Q9UBD5; -.
DR BioMuta; ORC3; -.
DR DMDM; 8928268; -.
DR EPD; Q9UBD5; -.
DR jPOST; Q9UBD5; -.
DR MassIVE; Q9UBD5; -.
DR MaxQB; Q9UBD5; -.
DR PaxDb; Q9UBD5; -.
DR PeptideAtlas; Q9UBD5; -.
DR PRIDE; Q9UBD5; -.
DR ProteomicsDB; 5643; -.
DR ProteomicsDB; 83947; -. [Q9UBD5-1]
DR ProteomicsDB; 83948; -. [Q9UBD5-2]
DR Antibodypedia; 18665; 244 antibodies from 29 providers.
DR DNASU; 23595; -.
DR Ensembl; ENST00000257789.4; ENSP00000257789.4; ENSG00000135336.16. [Q9UBD5-2]
DR Ensembl; ENST00000392844.8; ENSP00000376586.3; ENSG00000135336.16. [Q9UBD5-1]
DR Ensembl; ENST00000546266.5; ENSP00000444695.1; ENSG00000135336.16. [Q9UBD5-3]
DR GeneID; 23595; -.
DR KEGG; hsa:23595; -.
DR MANE-Select; ENST00000392844.8; ENSP00000376586.3; NM_012381.4; NP_036513.2.
DR UCSC; uc003pmg.4; human. [Q9UBD5-1]
DR CTD; 23595; -.
DR DisGeNET; 23595; -.
DR GeneCards; ORC3; -.
DR HGNC; HGNC:8489; ORC3.
DR HPA; ENSG00000135336; Low tissue specificity.
DR MIM; 604972; gene.
DR neXtProt; NX_Q9UBD5; -.
DR OpenTargets; ENSG00000135336; -.
DR PharmGKB; PA32810; -.
DR VEuPathDB; HostDB:ENSG00000135336; -.
DR eggNOG; KOG2538; Eukaryota.
DR GeneTree; ENSGT00390000011376; -.
DR HOGENOM; CLU_015257_2_0_1; -.
DR InParanoid; Q9UBD5; -.
DR OMA; HLECGRM; -.
DR OrthoDB; 1196817at2759; -.
DR PhylomeDB; Q9UBD5; -.
DR TreeFam; TF101093; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; Q9UBD5; -.
DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR SignaLink; Q9UBD5; -.
DR SIGNOR; Q9UBD5; -.
DR BioGRID-ORCS; 23595; 379 hits in 1088 CRISPR screens.
DR ChiTaRS; ORC3; human.
DR GeneWiki; ORC3; -.
DR GeneWiki; ORC3L; -.
DR GenomeRNAi; 23595; -.
DR Pharos; Q9UBD5; Tbio.
DR PRO; PR:Q9UBD5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UBD5; protein.
DR Bgee; ENSG00000135336; Expressed in triceps brachii and 205 other tissues.
DR ExpressionAtlas; Q9UBD5; baseline and differential.
DR Genevisible; Q9UBD5; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000808; C:origin recognition complex; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:UniProtKB.
DR InterPro; IPR020795; ORC3.
DR InterPro; IPR045663; ORC3_ins.
DR InterPro; IPR045667; ORC3_N.
DR InterPro; IPR040855; ORC_WH_C.
DR PANTHER; PTHR12748; PTHR12748; 1.
DR Pfam; PF19675; ORC3_ins; 1.
DR Pfam; PF07034; ORC3_N; 1.
DR Pfam; PF18137; ORC_WH_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA replication;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..711
FT /note="Origin recognition complex subunit 3"
FT /id="PRO_0000127083"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044893"
FT VAR_SEQ 505
FT /note="D -> DA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017129"
FT VARIANT 94
FT /note="Q -> K (in dbSNP:rs2307365)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_014516"
FT VARIANT 126
FT /note="Q -> R (in dbSNP:rs2307371)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_014517"
FT VARIANT 217
FT /note="V -> I (in dbSNP:rs2307389)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_014518"
FT VARIANT 247
FT /note="I -> V (in dbSNP:rs2307374)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_014519"
FT VARIANT 287
FT /note="T -> M (in dbSNP:rs2307381)"
FT /id="VAR_014520"
FT VARIANT 389
FT /note="T -> P (in dbSNP:rs2307372)"
FT /id="VAR_014521"
FT VARIANT 588
FT /note="R -> C (in dbSNP:rs2307370)"
FT /id="VAR_014522"
FT VARIANT 626
FT /note="A -> T (in dbSNP:rs28381545)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_020656"
FT CONFLICT 56
FT /note="S -> F (in Ref. 5; BAD96515)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="K -> R (in Ref. 4; CAB45715)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Q -> R (in Ref. 4; CAB45715)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="I -> M (in Ref. 5; BAD96515)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="K -> R (in Ref. 4; CAB45715)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="L -> F (in Ref. 3; AAD40220 and 10; AAA96313)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 26..30
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 39..65
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 67..86
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 239..243
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 391..425
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 435..443
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 465..481
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 488..499
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 548..565
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 584..591
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 606..609
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:7JPQ"
FT HELIX 645..659
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 676..689
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 690..692
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:7JPO"
SQ SEQUENCE 711 AA; 82254 MW; E713569A11B39B1C CRC64;
MATSSMSKGC FVFKPNSKKR KISLPIEDYF NKGKNEPEDS KLRFETYQLI WQQMKSENER
LQEELNKNLF DNLIEFLQKS HSGFQKNSRD LGGQIKLREI PTAALVLGVN VTDHDLTFGS
LTEALQNNVT PYVVSLQAKD CPDMKHFLQK LISQLMDCCV DIKSKEEESV HVTQRKTHYS
MDSLSSWYMT VTQKTDPKML SKKRTTSSQW QSPPVVVILK DMESFATKVL QDFIIISSQH
LHEFPLILIF GIATSPIIIH RLLPHAVSSL LCIELFQSLS CKEHLTTVLD KLLLTTQFPF
KINEKVLQVL TNIFLYHDFS VQNFIKGLQL SLLEHFYSQP LSVLCCNLPE AKRRINFLSN
NQCENIRRLP SFRRYVEKQA SEKQVALLTN ERYLKEETQL LLENLHVYHM NYFLVLRCLH
KFTSSLPKYP LGRQIRELYC TCLEKNIWDS EEYASVLQLL RMLAKDELMT ILEKCFKVFK
SYCENHLGST AKRIEEFLAQ FQSLDETKEE EDASGSQPKG LQKTDLYHLQ KSLLEMKELR
RSKKQTKFEV LRENVVNFID CLVREYLLPP ETQPLHEVVY FSAAHALREH LNAAPRIALH
TALNNPYYYL KNEALKSEEG CIPNIAPDIC IAYKLHLECS RLINLVDWSE AFATVVTAAE
KMDANSATSE EMNEIIHARF IRAVSELELL GFIKPTKQKT DHVARLTWGG C
