ID   MCMBP_RAT               Reviewed;         642 AA.
AC   B1H268;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE            Short=MCM-BP;
DE            Short=MCM-binding protein;
GN   Name=Mcmbp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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).
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). Interacts with the RPA
CC       complex, when composed of all RPA1, RPA2 and RPA3 components, but not
CC       with RPA1 or RPA2 alone (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC       chromatin. Highly associated with chromatin in G1/S and S phases,
CC       reduced binding to chromatin in G2, and further decreased binding in
CC       early M phase. It then reassociates with chromatin in late M phase.
CC       Dissociates from chromatin later than component of the MCM complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR   EMBL; BC160884; AAI60884.1; -; mRNA.
DR   RefSeq; NP_001034697.2; NM_001039608.2.
DR   AlphaFoldDB; B1H268; -.
DR   STRING; 10116.ENSRNOP00000027644; -.
DR   iPTMnet; B1H268; -.
DR   PhosphoSitePlus; B1H268; -.
DR   jPOST; B1H268; -.
DR   PaxDb; B1H268; -.
DR   PeptideAtlas; B1H268; -.
DR   PRIDE; B1H268; -.
DR   GeneID; 309009; -.
DR   KEGG; rno:309009; -.
DR   UCSC; RGD:1306730; rat.
DR   CTD; 79892; -.
DR   RGD; 1306730; Mcmbp.
DR   VEuPathDB; HostDB:ENSRNOG00000020394; -.
DR   eggNOG; KOG2545; Eukaryota.
DR   HOGENOM; CLU_029811_0_0_1; -.
DR   InParanoid; B1H268; -.
DR   OMA; HTEMIQQ; -.
DR   OrthoDB; 1011739at2759; -.
DR   PhylomeDB; B1H268; -.
DR   TreeFam; TF324793; -.
DR   PRO; PR:B1H268; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020394; Expressed in thymus and 19 other tissues.
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   Phosphoprotein; Reference proteome.
FT   CHAIN           1..642
FT                   /note="Mini-chromosome maintenance complex-binding protein"
FT                   /id="PRO_0000405808"
FT   REGION          151..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTE3"
FT   MOD_RES         160
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTE3"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTE3"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTE3"
SQ   SEQUENCE   642 AA;  73007 MW;  F23D2B87F85A4E31 CRC64;
     MPCGEDWLSH PLGIVQGFFA QNGVTPDWEK KVIDYFKEKL KENNAPKWVP SLNEVPLHYL
     KPNSFVKFRC MIQDMFDPEF YMGVYETVNQ NTKARVLHFG KYRDVAECGP QQELDLNSPR
     STTSERQTFY CVPVPGESLW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DEDMDLQPNK
     QKDQHSGARQ AGGLGGLHWR GEPKRLETEA SSGQQLNSLN LSSPFDLNFP LPGEKGPACL
     VKVYEDWDCF KVNDVLELYG VLSVDPILSI LNNEERDASA LLDPMECTDM AEEQRVHSPP
     ASLVPRIHVI LAQKLQHINP LLPTCLNKEE SRTCQFVSNF MSELSPVRAE LLGFLTHALL
     GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPQNS TFTEHLYRII QHLVPASFRL
     QMTIENMNQL KLIPHKDYTA NRLVSGLLQL PNNTSLVIDE TLLEQGQLDT PGVHNVAALS
     NLITWQKVDY DFSYHQMEFP CNINVLITSE GRSLLPADCQ IHLQPQLIPP NMEEYMNGLL
     SAVLPSVLNK FRIYLTLLRF LDYNLSDDIT KAVEDDFVEM RKNDPQSITA DDLHQLLVVA
     RFLSLSAGQT TLSRERWLRA KQLEHSRRSR LQQQKSVNGN EL