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ORC3_MOUSE
ID   ORC3_MOUSE              Reviewed;         715 AA.
AC   Q9JK30; A2AMF4; A2AMF5; Q6P8H2; Q8BR83; Q8C395;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Origin recognition complex subunit 3;
DE   AltName: Full=Origin recognition complex subunit Latheo;
GN   Name=Orc3; Synonyms=Orc3l;
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] (ISOFORM 1).
RX   PubMed=10702681; DOI=10.1159/000015435;
RA   Springer J., Nanda I., Hoehn K., Schmid M., Grummt F.;
RT   "Identification and chromosomal localization of murine ORC3, a new member
RT   of the mouse origin recognition complex.";
RL   Cytogenet. Cell Genet. 87:245-251(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=15634681; DOI=10.1074/jbc.m413280200;
RA   Miyake Y., Mizuno T., Yanagi K., Hanaoka F.;
RT   "Novel splicing variant of mouse Orc1 is deficient in nuclear translocation
RT   and resistant for proteasome-mediated degradation.";
RL   J. Biol. Chem. 280:12643-12652(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Head;
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 MRNA] (ISOFORM 2).
RC   TISSUE=Pituitary;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
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).
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:0000250|UniProtKB:Q9UBD5}.
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:0000250|UniProtKB:Q9UBD5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UBD5}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9UBD5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JK30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JK30-2; Sequence=VSP_026407;
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:0000250|UniProtKB:Q9UBD5}.
CC   -!- SIMILARITY: Belongs to the ORC3 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AJ132830; CAB76399.1; -; mRNA.
DR   EMBL; AB190257; BAD91665.2; -; mRNA.
DR   EMBL; AK045388; BAC32339.1; -; mRNA.
DR   EMBL; AK086579; BAC39695.1; -; mRNA.
DR   EMBL; AL807397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL928738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC061252; AAH61252.1; -; mRNA.
DR   CCDS; CCDS18028.1; -. [Q9JK30-1]
DR   CCDS; CCDS51137.1; -. [Q9JK30-2]
DR   RefSeq; NP_001153035.1; NM_001159563.1. [Q9JK30-2]
DR   RefSeq; NP_056639.3; NM_015824.4. [Q9JK30-1]
DR   AlphaFoldDB; Q9JK30; -.
DR   SMR; Q9JK30; -.
DR   BioGRID; 206124; 4.
DR   ComplexPortal; CPX-1915; Nuclear origin of replication recognition complex.
DR   CORUM; Q9JK30; -.
DR   STRING; 10090.ENSMUSP00000048319; -.
DR   iPTMnet; Q9JK30; -.
DR   PhosphoSitePlus; Q9JK30; -.
DR   EPD; Q9JK30; -.
DR   MaxQB; Q9JK30; -.
DR   PaxDb; Q9JK30; -.
DR   PeptideAtlas; Q9JK30; -.
DR   PRIDE; Q9JK30; -.
DR   ProteomicsDB; 294107; -. [Q9JK30-1]
DR   ProteomicsDB; 294108; -. [Q9JK30-2]
DR   Antibodypedia; 18665; 244 antibodies from 29 providers.
DR   DNASU; 50793; -.
DR   Ensembl; ENSMUST00000048706; ENSMUSP00000048319; ENSMUSG00000040044. [Q9JK30-1]
DR   Ensembl; ENSMUST00000108142; ENSMUSP00000103777; ENSMUSG00000040044. [Q9JK30-2]
DR   GeneID; 50793; -.
DR   KEGG; mmu:50793; -.
DR   UCSC; uc008sgb.2; mouse. [Q9JK30-1]
DR   UCSC; uc008sgd.1; mouse. [Q9JK30-2]
DR   CTD; 23595; -.
DR   MGI; MGI:1354944; Orc3.
DR   VEuPathDB; HostDB:ENSMUSG00000040044; -.
DR   eggNOG; KOG2538; Eukaryota.
DR   GeneTree; ENSGT00390000011376; -.
DR   HOGENOM; CLU_015257_2_0_1; -.
DR   InParanoid; Q9JK30; -.
DR   OMA; HLECGRM; -.
DR   OrthoDB; 1196817at2759; -.
DR   PhylomeDB; Q9JK30; -.
DR   TreeFam; TF101093; -.
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; 50793; 19 hits in 73 CRISPR screens.
DR   ChiTaRS; Orc3; mouse.
DR   PRO; PR:Q9JK30; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9JK30; protein.
DR   Bgee; ENSMUSG00000040044; Expressed in undifferentiated genital tubercle and 254 other tissues.
DR   ExpressionAtlas; Q9JK30; baseline and differential.
DR   Genevisible; Q9JK30; MM.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IBA:GO_Central.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; ISS:UniProtKB.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000808; C:origin recognition complex; ISO:MGI.
DR   GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; TAS:MGI.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0014009; P:glial cell proliferation; IMP:MGI.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
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.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromosome; DNA replication; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..715
FT                   /note="Origin recognition complex subunit 3"
FT                   /id="PRO_0000127084"
FT   MOD_RES         523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBD5"
FT   VAR_SEQ         512
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:15634681"
FT                   /id="VSP_026407"
FT   CONFLICT        114
FT                   /note="L -> F (in Ref. 3; BAC39695)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="A -> P (in Ref. 2; BAD91665 and 5; AAH61252)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="R -> G (in Ref. 3; BAC32339)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        645
FT                   /note="L -> R (in Ref. 2; BAD91665 and 5; AAH61252)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q9JK30-2:522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
SQ   SEQUENCE   715 AA;  82342 MW;  1E915A719A2E33EB CRC64;
     MHTGPRTMAT SSVSKGCFVF KPDFKKRKVF VPIEDYFNNE ELDSEDSKLR FETYSLLWQR
     MKSETEQLQE ELNENLFDNL VDFLQKSHPE FQKNSRDWGS QMKFREIPTA ALILGVNVTD
     HDVILRSLTE TLQNNVTPYV VSLQAKDCPD VKHFLQKFTS QLMDCCVDRH SKEVTSGKAL
     KKTNYSMDSL CSWYSAVTQK ADHKVTIKKR TASGHWRSPP VVLILKSMES FTSKVLQDFI
     TISSQHLHEF PLILIFGIAT SPVIIHRLLP HSVSSLLCVE LFQSLSCEQH LTVVLDKLLL
     TPQFPFKLSK KALQVLTNIF LYHDFSIQSF IKGIKLSLLE HFYSQPLSVL CCDLSEAKKR
     VNVFSVSQCE NIRRLPSFRR YVENQPLGKQ VALLTNETFL KEKTQSLLED LHVYHINYFL
     VLRCLHNFTS SLPKYPLGRQ IRELYCTCLE KKIWDSEEYK SALQLLRMLA KDELVSILQR
     CIEVLDSSTE KQLGNTTQKI KDFLTQFQNL DADSKEEEDA CGSQPKGLQK TDLYHLQKSL
     LEMKELRRTK KPTKFEMLRE NVMNFIDNLV RDYLLPPESQ PLHEVVYFSA ANTLREHLNA
     APRIALHTAL NNPYYYLKNE ELEGCIPNTA PDICIAYKLH LECSLLINLV DWAEAFATVV
     TAAEKMDANS TVSEEMSEVI HARFIRAVSE LELLGFIKPT KQKTDHVARL TWGGC
 
 
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