MCMBP_DANRE
ID MCMBP_DANRE Reviewed; 631 AA.
AC Q803A6; A8E7D0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE Short=MCM-BP;
DE Short=MCM-binding protein;
GN Name=mcmbp; ORFNames=si:dkey-192p21.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associated component of the mcm complex that acts as a
CC regulator of DNA replication. Binds to the MCM complex during late S
CC phase and promotes the disassembly of the mcm complex from chromatin,
CC thereby acting as a key regulator of pre-replication complex (pre-RC)
CC unloading from replicated DNA. Can dissociate the mcm complex without
CC addition of ATP; probably acts by destabilizing interactions of each
CC individual subunits of the mcm complex. Required for sister chromatid
CC cohesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the mcm complex: associates with the mcm3-7
CC complex which lacks mcm2, while it does not interact with the mcm
CC complex when mcm2 is present (mcm2-7 complex). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR EMBL; BX005252; CAP09248.1; -; Genomic_DNA.
DR EMBL; BC044562; AAH44562.1; -; mRNA.
DR RefSeq; NP_997743.1; NM_212578.1.
DR AlphaFoldDB; Q803A6; -.
DR STRING; 7955.ENSDARP00000120704; -.
DR PaxDb; Q803A6; -.
DR Ensembl; ENSDART00000135788; ENSDARP00000120704; ENSDARG00000055314.
DR Ensembl; ENSDART00000168099; ENSDARP00000130337; ENSDARG00000055314.
DR GeneID; 321119; -.
DR KEGG; dre:321119; -.
DR CTD; 79892; -.
DR ZFIN; ZDB-GENE-030131-9676; mcmbp.
DR eggNOG; KOG2545; Eukaryota.
DR GeneTree; ENSGT00390000017265; -.
DR HOGENOM; CLU_029811_0_0_1; -.
DR InParanoid; Q803A6; -.
DR OrthoDB; 1011739at2759; -.
DR PhylomeDB; Q803A6; -.
DR TreeFam; TF324793; -.
DR PRO; PR:Q803A6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000055314; Expressed in blastula and 41 other tissues.
DR ExpressionAtlas; Q803A6; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
DR InterPro; IPR019140; MCM_complex-bd.
DR PANTHER; PTHR13489; PTHR13489; 1.
DR Pfam; PF09739; MCM_bind; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; DNA replication; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..631
FT /note="Mini-chromosome maintenance complex-binding protein"
FT /id="PRO_0000405809"
FT REGION 148..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 189
FT /note="S -> T (in Ref. 2; AAH44562)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="F -> Y (in Ref. 2; AAH44562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 71062 MW; 8ED47656E40781CC CRC64;
MPTTHDWINN PLGVVDGLFA QSNSSPDWEK KVVEYFKEKL KLNDAHTWVP SLNDVPLHYL
KPNSLVKFRC MVQDMFDPEF FMGVYEMNDP TSNSKQVKCG KYKDVTECGQ VDFNSRNTVT
SERQTFYCVP IPGESNWVKE SYAGTSQARV VPSTSYVPNR HKRSYEEDDE MDTQCQQTKD
ISQGAQSSSE SHGNTEPKRQ ETEAPSQDSS SSHCTSSLDL NFPLPGEKGP ACLVKVYEDW
DSFKLNDMLE VFGILSVDPA LSVIADEREA SSLLDPTEGM ETMEEQRVHS PPASLVPRLH
MLYAQPLAHN NPLLPSSPLE NNADYLSCVL GELASVRAEL LTFFTHILMG DSLAAEFLIL
HLISNVYSRR DVLPLGKFTL NLSGCPLSSP FTEHLFKVIQ QLVPSSYRLS MSLHNMNTQR
MVPRKDYTAN RLVSGTLQLA KNTSLFLDET QLEQGQLDST GVRNITALGN LISWQKVDYD
FNYHQMEFPC NINVLIASEG RSLLPSDCQV HLRASLNPPN LEEYLSAVQV AQVPSQLNKY
RVYLSVARAL NYTISDEITK AVEEDFVDMR KDDPQSMSAE DLHRLLVVAR LLSLSHGQNT
LSRDGWMKAK QLEALRISRT QQQKCVNGNE P