ORC2_SCHPO
ID ORC2_SCHPO Reviewed; 535 AA.
AC Q09142;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Origin recognition complex subunit 2;
GN Name=orc2 {ECO:0000312|PomBase:SPBC685.09};
GN Synonyms=orp2 {ECO:0000303|PubMed:15314153,
GN ECO:0000312|PomBase:SPBC685.09};
GN ORFNames=SPBC685.09 {ECO:0000312|PomBase:SPBC685.09};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8552194; DOI=10.1038/379360a0;
RA Leatherwood J., Lopez-Girona A., Russell P.R.;
RT "Interaction of Cdc2 and Cdc18 with a fission yeast ORC2-like protein.";
RL Nature 379:360-363(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP IDENTIFICATION IN THE ORC COMPLEX.
RX PubMed=10535928; DOI=10.1073/pnas.96.22.12367;
RA Moon K.-Y., Kong D., Lee J.-K., Raychaudhuri S., Hurwitz J.;
RT "Identification and reconstitution of the origin recognition complex from
RT Schizosaccharomyces pombe.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12367-12372(1999).
RN [4]
RP FUNCTION, PHOSPHORYLATION AT THR-44; THR-57; THR-62 AND THR-65, AND
RP MUTAGENESIS OF THR-44; THR-57; THR-62 AND THR-65.
RX PubMed=11486016; DOI=10.1128/mcb.21.17.5767-5777.2001;
RA Vas A., Mok W., Leatherwood J.;
RT "Control of DNA rereplication via Cdc2 phosphorylation sites in the origin
RT recognition complex.";
RL Mol. Cell. Biol. 21:5767-5777(2001).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE ORC COMPLEX, AND INTERACTION WITH CDC18.
RX PubMed=11850415; DOI=10.1074/jbc.m107710200;
RA Chuang R.-Y., Chretien L., Dai J., Kelly T.J.;
RT "Purification and characterization of the Schizosaccharomyces pombe origin
RT recognition complex: interaction with origin DNA and Cdc18 protein.";
RL J. Biol. Chem. 277:16920-16927(2002).
RN [6]
RP INTERACTION WITH SPB70 AND SPP2, AND SUBCELLULAR LOCATION.
RX PubMed=15314153; DOI=10.1128/mcb.24.17.7419-7434.2004;
RA Uchiyama M., Wang T.S.;
RT "The B-subunit of DNA polymerase alpha-primase associates with the origin
RT recognition complex for initiation of DNA replication.";
RL Mol. Cell. Biol. 24:7419-7434(2004).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication (PubMed:11850415). It has a role in both
CC chromosomal replication and mating type transcriptional silencing
CC (PubMed:11850415). ORC binds to multiple sites within the ars1 origin
CC of DNA replication in an ATP-independent manner (PubMed:11850415).
CC Together with cdc18, plays a role in preventing DNA rereplication and
CC resulting genetic instability upon cell cycle-regulated phosphorylation
CC by cdc2 (PubMed:11486016). {ECO:0000269|PubMed:11486016,
CC ECO:0000269|PubMed:11850415}.
CC -!- SUBUNIT: ORC is composed of six subunits. ORC interacts with cdc18,
CC recruiting it to the ars1 origin of replication (PubMed:10535928,
CC PubMed:11850415). Interacts with spb70 (PubMed:15314153). Interacts
CC with spp2; preferentially associates with the unphosphorylated orc2 in
CC G1 pre-Start prior to orc2 being phosphorylated by cdc2, the
CC interaction is mediated by spb70 and might enable the association of
CC the whole alpha DNA polymerase complex to orc2/spb70 complex on
CC chromatin (PubMed:15314153). {ECO:0000269|PubMed:10535928,
CC ECO:0000269|PubMed:11850415, ECO:0000269|PubMed:15314153}.
CC -!- INTERACTION:
CC Q09142; P04551: cdc2; NbExp=2; IntAct=EBI-2028187, EBI-1187862;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15314153}. Chromosome
CC {ECO:0000269|PubMed:15314153}.
CC -!- PTM: Phosphorylated by cdc2 and cdc13 (in vitro) (PubMed:11486016).
CC Phosphorylation appears first in S phase and becomes maximal in G2 and
CC M when cdc2 kinase activity is required to prevent reinitiation of DNA
CC replication (PubMed:11486016). {ECO:0000269|PubMed:11486016}.
CC -!- SIMILARITY: Belongs to the ORC2 family. {ECO:0000305}.
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DR EMBL; U38472; AAC49165.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB39366.1; -; Genomic_DNA.
DR PIR; S68446; S68446.
DR RefSeq; NP_596143.1; NM_001022061.2.
DR AlphaFoldDB; Q09142; -.
DR SMR; Q09142; -.
DR BioGRID; 277674; 20.
DR IntAct; Q09142; 4.
DR STRING; 4896.SPBC685.09.1; -.
DR iPTMnet; Q09142; -.
DR MaxQB; Q09142; -.
DR PaxDb; Q09142; -.
DR PRIDE; Q09142; -.
DR EnsemblFungi; SPBC685.09.1; SPBC685.09.1:pep; SPBC685.09.
DR GeneID; 2541159; -.
DR KEGG; spo:SPBC685.09; -.
DR PomBase; SPBC685.09; orc2.
DR VEuPathDB; FungiDB:SPBC685.09; -.
DR eggNOG; KOG2928; Eukaryota.
DR HOGENOM; CLU_509161_0_0_1; -.
DR InParanoid; Q09142; -.
DR OMA; YDFELAY; -.
DR PhylomeDB; Q09142; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SPO-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q09142; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IC:PomBase.
DR InterPro; IPR007220; ORC2.
DR PANTHER; PTHR14052; PTHR14052; 1.
DR Pfam; PF04084; ORC2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..535
FT /note="Origin recognition complex subunit 2"
FT /id="PRO_0000127081"
FT REGION 132..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11486016"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11486016"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11486016"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 44
FT /note="T->A: Loss of phosphorylation by cdc2 and enhanced
FT rereplication induced by overexpression of a cdc18 mutant
FT lacking four cdc2 phosphorylation sites; when associated
FT with A-57; A-62 and A-65."
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 44
FT /note="T->D: Does not affect function on preventing
FT rereplication; when associated with D-62 and D-65."
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 57
FT /note="T->A: Loss of phosphorylation by cdc2 and enhanced
FT rereplication induced by overexpression of a cdc18 mutant
FT lacking four cdc2 phosphorylation sites; when associated
FT with A-44; A-62 and A-65."
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 62
FT /note="T->A: Loss of phosphorylation by cdc2 and enhanced
FT rereplication induced by overexpression of a cdc18 mutant
FT lacking four cdc2 phosphorylation sites; when associated
FT with A-44; A-57 and A-65."
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 62
FT /note="T->D: Does not affect function on preventing
FT rereplication; when associated with D-44 and A-65."
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 65
FT /note="T->A: Loss of phosphorylation by cdc2 and enhanced
FT rereplication induced by overexpression of a cdc18 mutant
FT lacking four cdc2 phosphorylation sites; when associated
FT with A-44; A-57 and A-62."
FT /evidence="ECO:0000269|PubMed:11486016"
FT MUTAGEN 65
FT /note="T->D: Does not affect function on preventing
FT rereplication; when associated with D-44 and D-62."
FT /evidence="ECO:0000269|PubMed:11486016"
SQ SEQUENCE 535 AA; 61023 MW; 7B04A316D94BAF88 CRC64;
MLINEHVRER YHFLRVSLTR VAHLVFANSH ESNDLKMVEN VSSTPKKGVL EDPSTLTPEV
VTPRTPGHRI IKAKGAYTKD RSAKRRRGRI EIERHLLGEF DDNVGSNSLL DVPLYSLEAE
PLSPSVMLED ESMEGINQSP QGISVEKLGK EDNRSRSSTP ASPSLESHEF SESREAGLSQ
SNGFEARSHG TGFDEYFDKF SQRKTSSNTL SQLPVLDNQV YLDTVKEICT ETEQHTQTLV
HFQSRNFHQW YFELVNNFNL LFYGFGSKEH FLSSFVEKKL PCFPIFVVKG YFPQLQLKNV
LSSFLEFLEV TPAASVSDML IQSLSIINSP SFSLGKIVFL VHNIDGESLI DERFQSALAA
IASSKNVYFI ASVDHVNFAL LWDTSLESSF NFVMHDATTF ARYYNETTYE NSLGIGRANV
SNKEKAIKHV LYSLPANSRG IFKFLLIHQL ERMMDTQDFD ARQGEKVGIE YRSFFQKCSA
EFLCSNEPNF RSQLTEFFDH NIIESKRDVS NSEILWVPYP KNLLEILLED MMEDV
