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ORC5_ARATH
ID   ORC5_ARATH              Reviewed;         534 AA.
AC   Q6EWX0; Q9SZR2;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Origin of replication complex subunit 5 {ECO:0000303|PubMed:16179646};
DE            Short=AtORC5 {ECO:0000303|PubMed:16179646};
GN   Name=ORC5 {ECO:0000303|PubMed:16179646};
GN   OrderedLocusNames=At4g29910 {ECO:0000312|Araport:AT4G29910};
GN   ORFNames=F27B13.150 {ECO:0000312|EMBL:CAB43666.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|EMBL:CAE01429.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Diaz-Trivino S., Castellano M.M., Gutierrez C.;
RT   "Organization of Arabidopsis origin recognition complex genes.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   SUBUNIT, INTERACTION WITH ORC3, TISSUE SPECIFICITY, INDUCTION BY SUCROSE,
RP   AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=15358564; DOI=10.1016/j.febslet.2004.07.088;
RA   Masuda H.P., Ramos G.B.A., de Almeida-Engler J., Cabral L.M.,
RA   Coqueiro V.M., Macrini C.M.T., Ferreira P.C.G., Hemerly A.S.;
RT   "Genome based identification and analysis of the pre-replicative complex of
RT   Arabidopsis thaliana.";
RL   FEBS Lett. 574:192-202(2004).
RN   [6]
RP   SUBUNIT, INTERACTION WITH ORC1A; ORC1B; ORC2; ORC3; ORC4 AND ORC6, TISSUE
RP   SPECIFICITY, INDUCTION BY SUCROSE, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16179646; DOI=10.1093/nar/gki854;
RA   Diaz-Trivino S., Castellano M.M., Sanchez M.P., Ramirez-Parra E.,
RA   Desvoyes B., Gutierrez C.;
RT   "The genes encoding Arabidopsis ORC subunits are E2F targets and the two
RT   ORC1 genes are differently expressed in proliferating and endoreplicating
RT   cells.";
RL   Nucleic Acids Res. 33:5404-5414(2005).
RN   [7]
RP   REVIEW ON THE CORE DNA REPLICATION MACHINERY.
RX   PubMed=17556508; DOI=10.1104/pp.107.101105;
RA   Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT   "Genome-wide analysis of the core DNA replication machinery in the higher
RT   plants Arabidopsis and rice.";
RL   Plant Physiol. 144:1697-1714(2007).
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. {ECO:0000250|UniProtKB:O43913}.
CC   -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC       at least ORC1 (ORC1A or ORC1B), ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is
CC       regulated in a cell-cycle and development dependent manner. It is
CC       sequentially assembled at the exit from anaphase of mitosis and
CC       disassembled as cells enter S phase. Interacts directly with ORC1A,
CC       ORC1B, ORC2, ORC3, ORC4 and ORC6. {ECO:0000269|PubMed:15358564,
CC       ECO:0000269|PubMed:16179646}.
CC   -!- INTERACTION:
CC       Q6EWX0; Q38899: ORC2; NbExp=2; IntAct=EBI-2114109, EBI-2114089;
CC       Q6EWX0; Q6EWX1: ORC4; NbExp=2; IntAct=EBI-2114109, EBI-2114176;
CC       Q6EWX0; Q9ZVH3: ORC6; NbExp=2; IntAct=EBI-2114109, EBI-2114077;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43913}.
CC   -!- TISSUE SPECIFICITY: Follow a cell-cycle regulation with a peak at the
CC       G1/S-phase (PubMed:16179646). Mostly expressed in flower buds and
CC       cauline leaves, and, to a lower exent, in roots, leaves and stems
CC       (PubMed:16179646). Expressed at low levels ubiquitously
CC       (PubMed:15358564). {ECO:0000269|PubMed:15358564,
CC       ECO:0000269|PubMed:16179646}.
CC   -!- INDUCTION: Accumulates 13 hours after cell cycle reactivation by
CC       sucrose addition following cell cycle arrest mediated by sucrose
CC       deprivation. {ECO:0000269|PubMed:15358564,
CC       ECO:0000269|PubMed:16179646}.
CC   -!- SIMILARITY: Belongs to the ORC5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB43666.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79749.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ575583; CAE01429.1; -; mRNA.
DR   EMBL; AL050352; CAB43666.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161575; CAB79749.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85692.1; -; Genomic_DNA.
DR   EMBL; AK226860; BAE98949.1; -; mRNA.
DR   PIR; T08552; T08552.
DR   RefSeq; NP_194720.2; NM_119137.5.
DR   AlphaFoldDB; Q6EWX0; -.
DR   SMR; Q6EWX0; -.
DR   IntAct; Q6EWX0; 5.
DR   STRING; 3702.AT4G29910.1; -.
DR   iPTMnet; Q6EWX0; -.
DR   PaxDb; Q6EWX0; -.
DR   PRIDE; Q6EWX0; -.
DR   ProteomicsDB; 248771; -.
DR   EnsemblPlants; AT4G29910.1; AT4G29910.1; AT4G29910.
DR   GeneID; 829114; -.
DR   Gramene; AT4G29910.1; AT4G29910.1; AT4G29910.
DR   KEGG; ath:AT4G29910; -.
DR   Araport; AT4G29910; -.
DR   TAIR; locus:2123934; AT4G29910.
DR   eggNOG; KOG2543; Eukaryota.
DR   HOGENOM; CLU_028223_1_0_1; -.
DR   InParanoid; Q6EWX0; -.
DR   OMA; QLRRWHG; -.
DR   PhylomeDB; Q6EWX0; -.
DR   PRO; PR:Q6EWX0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q6EWX0; baseline and differential.
DR   Genevisible; Q6EWX0; AT.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; IBA:GO_Central.
DR   GO; GO:0000808; C:origin recognition complex; ISS:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; ISS:TAIR.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR020796; ORC5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12705; PTHR12705; 1.
DR   Pfam; PF14630; ORC5_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA replication; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..534
FT                   /note="Origin of replication complex subunit 5"
FT                   /id="PRO_0000431435"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           129..136
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        13..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   534 AA;  60638 MW;  8DA66E2E9577403C CRC64;
     MPPKEESSKV TRRSTRSSAS VTVENSEPIE SHTPTIDDLT FGEESITIDA VLSNFPGRRS
     QIFDFIRLMG PLDCPTLPIM IYGGASTGKT SVVLQVLRHL NRPFVYSSCR TCYNPRILFE
     SILNQSLLHR KCSLNGYSSA KRCDKPSDFV NLLREALSSV IKTLESTSET SRSDKPDEKP
     MGKMVYLILD NVDLIRDWDK GTIILQFLFS LYTVLKMPQL GIILISGLPP DVYYSNMGYT
     DPIPLYFPEY SEEDLRQIFL RNQPNRKLYS AFLDVVLKPF CRVTRRVEEL STTFSLLFRK
     FCEPLDDLGI SPNEDMKRRL YSHLKPLIAH CLNEIFRVSS HPHDGETRGE RRQKASYSSE
     NREELEILDF HMSTSAKFLL LSAFLASRNP ATLDASMFDS TGGMDNRKRK RKASEKSMEK
     KEIAEQEAVM KGPGSFPLER LLAIFQCIAS VGDSSFGEED EEEENTTGYD KENNNLMSDI
     LLQVSSLCDA NFLIKSGSCP LEGSIRYRSM VSEDLAQKVA KSLSFPLSKY LYRR
 
 
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