ORC2_DROME
ID ORC2_DROME Reviewed; 618 AA.
AC Q24168; Q9VFP4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Origin recognition complex subunit 2;
DE Short=DmORC2;
GN Name=Orc2; ORFNames=CG3041;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7502079; DOI=10.1126/science.270.5242.1674;
RA Gossen M., Pak D.T.S., Hansen S.K., Acharya J.K., Botchan M.R.;
RT "A Drosophila homolog of the yeast origin recognition complex.";
RL Science 270:1674-1677(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=11137005; DOI=10.1016/s0960-9822(00)00844-7;
RA Loupart M.-L., Krause S.A., Heck M.M.S.;
RT "Aberrant replication timing induces defective chromosome condensation in
RT Drosophila ORC2 mutants.";
RL Curr. Biol. 10:1547-1556(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP INTERACTION WITH MCM10.
RX PubMed=12808023; DOI=10.1091/mbc.e02-11-0706;
RA Christensen T.W., Tye B.K.;
RT "Drosophila MCM10 interacts with members of the prereplication complex and
RT is required for proper chromosome condensation.";
RL Mol. Biol. Cell 14:2206-2215(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-26; SER-30; SER-87;
RP SER-91; SER-92; THR-151; THR-154; THR-157; THR-160; THR-167; THR-170;
RP THR-181; THR-258 AND SER-260, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=27016737; DOI=10.1093/nar/gkw192;
RA Kopytova D., Popova V., Kurshakova M., Shidlovskii Y., Nabirochkina E.,
RA Brechalov A., Georgiev G., Georgieva S.;
RT "ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association
RT with mRNP and mRNA export in Drosophila.";
RL Nucleic Acids Res. 44:4920-4933(2016).
RN [9]
RP INTERACTION WITH CG9890.
RX PubMed=30713769;
RA Fursova N.A., Nikolenko J.V., Soshnikova N.V., Mazina M.Y., Vorobyova N.E.,
RA Krasnov A.N.;
RT "Zinc Finger Protein CG9890 - New Component of ENY2-Containing Complexes of
RT Drosophila.";
RL Acta Naturae 10:110-114(2018).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication (PubMed:11137005). DNA-binding is ATP-dependent,
CC however specific DNA sequences that define origins of replication have
CC not been identified so far (PubMed:11137005). ORC is required to
CC assemble the pre-replication complex necessary to initiate DNA
CC replication (PubMed:11137005). As part of the ORC complex, might also
CC have a role in mRNA export (Probable). {ECO:0000269|PubMed:11137005,
CC ECO:0000305|PubMed:27016737}.
CC -!- SUBUNIT: ORC is composed of six subunits. Interacts with Mcm10
CC (PubMed:12808023). Interacts with CG9890 (PubMed:30713769). Interaction
CC between the TREX-2/AMEX complex and the ORC complex is required for ORC
CC localization to mRNPs, and consequently mRNA export (PubMed:27016737).
CC {ECO:0000269|PubMed:12808023, ECO:0000269|PubMed:27016737,
CC ECO:0000269|PubMed:30713769}.
CC -!- INTERACTION:
CC Q24168; Q9VIE6: Mcm10; NbExp=2; IntAct=EBI-179453, EBI-91264;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11137005}. Chromosome
CC {ECO:0000269|PubMed:11137005}. Chromosome, centromere
CC {ECO:0000269|PubMed:11137005}. Note=Centromeres of metaphase and
CC anaphase chromosomes of early syncytial embryos. Later in development,
CC found in pericentric regions of late anaphase and telophase
CC chromosomes.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos (at protein level).
CC {ECO:0000269|PubMed:27016737}.
CC -!- DISRUPTION PHENOTYPE: Cause death late in larval development, with
CC defects in cell-cycle progression and chromosome condensation in
CC mitosis. {ECO:0000269|PubMed:11137005}.
CC -!- SIMILARITY: Belongs to the ORC2 family. {ECO:0000305}.
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DR EMBL; U43504; AAC46955.1; -; mRNA.
DR EMBL; AF246305; AAF99606.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55006.1; -; Genomic_DNA.
DR EMBL; AY051471; AAK92895.1; -; mRNA.
DR RefSeq; NP_731873.1; NM_169563.2.
DR PDB; 4XGC; X-ray; 3.50 A; B=266-618.
DR PDB; 7JGR; EM; 3.90 A; B=1-618.
DR PDB; 7JGS; EM; 3.20 A; B=1-618.
DR PDB; 7JK2; EM; 3.20 A; B=1-618.
DR PDB; 7JK3; EM; 3.40 A; B=1-618.
DR PDB; 7JK4; EM; 3.40 A; B=1-618.
DR PDB; 7JK5; EM; 3.90 A; B=1-618.
DR PDB; 7JK6; EM; 4.00 A; B=1-618.
DR PDBsum; 4XGC; -.
DR PDBsum; 7JGR; -.
DR PDBsum; 7JGS; -.
DR PDBsum; 7JK2; -.
DR PDBsum; 7JK3; -.
DR PDBsum; 7JK4; -.
DR PDBsum; 7JK5; -.
DR PDBsum; 7JK6; -.
DR AlphaFoldDB; Q24168; -.
DR SMR; Q24168; -.
DR BioGRID; 66780; 22.
DR DIP; DIP-23209N; -.
DR IntAct; Q24168; 6.
DR MINT; Q24168; -.
DR STRING; 7227.FBpp0082329; -.
DR iPTMnet; Q24168; -.
DR PaxDb; Q24168; -.
DR PRIDE; Q24168; -.
DR DNASU; 41703; -.
DR EnsemblMetazoa; FBtr0082866; FBpp0082329; FBgn0015270.
DR GeneID; 41703; -.
DR KEGG; dme:Dmel_CG3041; -.
DR CTD; 4999; -.
DR FlyBase; FBgn0015270; Orc2.
DR VEuPathDB; VectorBase:FBgn0015270; -.
DR eggNOG; KOG2928; Eukaryota.
DR GeneTree; ENSGT00390000015228; -.
DR HOGENOM; CLU_018596_3_0_1; -.
DR InParanoid; Q24168; -.
DR OMA; FPQWAFE; -.
DR OrthoDB; 1404162at2759; -.
DR PhylomeDB; Q24168; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DME-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-DME-68949; Orc1 removal from chromatin.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR SignaLink; Q24168; -.
DR BioGRID-ORCS; 41703; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41703; -.
DR PRO; PR:Q24168; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015270; Expressed in secondary oocyte and 33 other tissues.
DR Genevisible; Q24168; DM.
DR GO; GO:0005723; C:alpha-heterochromatin; IDA:FlyBase.
DR GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR GO; GO:0006260; P:DNA replication; IMP:FlyBase.
DR GO; GO:0006270; P:DNA replication initiation; IDA:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISS:FlyBase.
DR GO; GO:0007307; P:eggshell chorion gene amplification; IMP:FlyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR InterPro; IPR007220; ORC2.
DR PANTHER; PTHR14052; PTHR14052; 1.
DR Pfam; PF04084; ORC2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromosome; DNA replication; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..618
FT /note="Origin recognition complex subunit 2"
FT /id="PRO_0000127079"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 113
FT /note="A -> T (in Ref. 1; AAC46955)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> G (in Ref. 1; AAC46955)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="N -> I (in Ref. 1; AAC46955)"
FT /evidence="ECO:0000305"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 362..371
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:7JK4"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 457..465
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:7JGS"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 516..523
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 528..543
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 571..583
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:7JGS"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:7JGS"
FT HELIX 605..614
FT /evidence="ECO:0007829|PDB:7JGS"
SQ SEQUENCE 618 AA; 68996 MW; 39378D065F04BD88 CRC64;
MSASNKGGYK TPRKENLMSI ENLTNSEEES EDLNTAMVGN AVESQPKVTS RRSTRRPSPT
KKYQAYQKES NGKGQEERIV VNYVEMSDER SSDAEDQEEE ESIEESENAA RPAAKDLHLI
QSEYNVAGTS MFGFNTPKKR DAMALAALNA TPCTPKTPKT PRLGVKTPDT KRKKSMDQPK
TPAHVRTRVK KQIAKIVADS DEDFSGDESD FRPSDEESSS SSSSSDAGNS SDNDAADDEP
KTPSRARRAI VVPVLPKTPS AARLRQSARA KKSNEFVPES DGYFHSHASS KILTSDHTLD
RLKNPRLAAD RVFSLLSEIK TSAEHEGSIN AIMEEYRSYF PKWMCILNEG FNILLYGLGS
KHQLLQSFHR EVLHKQTVLV VNGFFPSLTI KDMLDSITSD ILDAGISPAN PHEAVDMIEE
EFALIPETHL FLIVHNLDGA MLRNVKAQAI LSRLARIPNI HLLASIDHIN TPLLWDQGKL
CSFNFSWWDC TTMLPYTNET AFENSLLVQN SGELALSSMR SVFSSLTTNS RGIYMLIVKY
QLKNKGNATY QGMPFRDLYS SCREAFLVSS DLALRAQLTE FLDHKLVKSK RSVDGSEQLT
IPIDGALLQQ FLEEQEKK
