ID   MCMBP_BOVIN             Reviewed;         642 AA.
AC   A5PJM5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE            Short=MCM-BP;
DE            Short=MCM-binding protein;
GN   Name=MCMBP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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). 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; BC142172; AAI42173.1; -; mRNA.
DR   RefSeq; NP_001092444.1; NM_001098974.1.
DR   AlphaFoldDB; A5PJM5; -.
DR   STRING; 9913.ENSBTAP00000013028; -.
DR   PaxDb; A5PJM5; -.
DR   PRIDE; A5PJM5; -.
DR   Ensembl; ENSBTAT00000013028; ENSBTAP00000013028; ENSBTAG00000009877.
DR   GeneID; 514863; -.
DR   KEGG; bta:514863; -.
DR   CTD; 79892; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009877; -.
DR   VGNC; VGNC:31316; MCMBP.
DR   eggNOG; KOG2545; Eukaryota.
DR   GeneTree; ENSGT00390000017265; -.
DR   HOGENOM; CLU_029811_0_0_1; -.
DR   InParanoid; A5PJM5; -.
DR   OMA; HTEMIQQ; -.
DR   OrthoDB; 1011739at2759; -.
DR   TreeFam; TF324793; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000009877; Expressed in neutrophil and 107 other tissues.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0042555; C:MCM complex; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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_0000328426"
FT   REGION          151..188
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;  73096 MW;  72449E5C071CDF03 CRC64;
     MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP SLNEVPLHYL
     KPNSFVKFRC MVQDMFDPEF YMGVYETVNR NTKARVLHFG KYRDVAECGP QQEVDLNSPR
     TTTLERQTFY CVPVPGESMW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DEDMDLQPNK
     QKDQHMGARQ AGNVGGLQWC GEPKRLETEA SSGQQLSSLN LSSPFDLNFP LPGEKGPACL
     VKVYEDWDCF KVNDVLELYG ILSVDPVLSI LNNDERDASS LLDPMECTDM AEEQRVHSPP
     ASLVPRIHVV LAQKLQHINP LLPACLNKEE SKTCKFVSGF MSELSPVRAE LLGFLTHALL
     GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPRNS TFTEHLYRII QHLVPASFRL
     QMTIENMNHL KFIPHKDYTA NRLVSGLLQL PSNTSLVIDE TLLEQGQLDT PGVHNVTALS
     NLITWQKVDY DFSYHQMEFP CNINVFITSE GRSLLPADCQ IHLQPQLMPP NMEEYMNSLL
     SAVLPSVLNK FRIYLTLLRF LDYSISDEIT KAVEDDFVEM RKNDPQSITA DDLHQLLIVA
     RFLSLSAGQT TLSRERWLRA KQLESLRRAR LQQQKCVNGN EL