MCMBP_XENLA
ID MCMBP_XENLA Reviewed; 626 AA.
AC Q7ZYP6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE Short=MCM-BP;
DE Short=MCM-binding protein;
GN Name=mcmbp;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE MCM COMPLEX.
RX PubMed=21196493; DOI=10.1101/gad.614411;
RA Nishiyama A., Frappier L., Mechali M.;
RT "MCM-BP regulates unloading of the MCM2-7 helicase in late S phase.";
RL Genes Dev. 25:165-175(2011).
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. May also be required for sister
CC chromatid cohesion. {ECO:0000269|PubMed:21196493}.
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 mcm7.
CC {ECO:0000269|PubMed:21196493}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21196493}.
CC Note=Imported in the nucleus in late S phase when mcm2-7 dissociates
CC from chromatin.
CC -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR EMBL; BC042336; AAH42336.1; -; mRNA.
DR RefSeq; NP_001080558.1; NM_001087089.1.
DR AlphaFoldDB; Q7ZYP6; -.
DR BioGRID; 98492; 1.
DR DNASU; 380250; -.
DR GeneID; 380250; -.
DR KEGG; xla:380250; -.
DR CTD; 380250; -.
DR Xenbase; XB-GENE-5898075; mcmbp.L.
DR OrthoDB; 1011739at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 380250; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IDA: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; IMP: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 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA replication; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..626
FT /note="Mini-chromosome maintenance complex-binding protein"
FT /id="PRO_0000405811"
FT REGION 159..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 70356 MW; 2AE9F8B92401C523 CRC64;
MAGVEDWISA PLAVVQGLFS QRQANGDWEK NVTDYFHDKL QGNRSPASVP CLNDVPLHYL
KPNSLVRFRC MVQDMFDPEF YMGVYETVDT NTSARVLHFG KYRDLAESLP QQEVDLDSRR
NVTCERQTFY CVPVPGESPW VKDAYTSSSQ ARACASTSYT PSRQKRSYEE DEDVGPCDTR
TSHGLGEPKR LETEAAGLQQ NQPSSCSSAP DLNFPLPGEK GPACLIKVYE GWDSFKVNDI
IEVYGILSVD PALSAVNEDR DAVSALLDPS DNMETLEEQR AHCPPASLVP RIHSVVTWKL
QHNNPLLPGT LQGTEESKLF VSNLLCEVSA VRAELLGFLS HALLGDSLAA EYLIIHLIST
VYARRDVLPL GKFTLNLSGC PRNGIFSELL YRILQQIVPA AHYLPMTIEN MNKLRFIPHK
DYNANRLRSG LLQLSAHTSL LLDETLLEQG QLDTAGVHNV TALGNLITWQ KVDYDFSYHR
MEFPCNINVL VTSEGRSLLP SDCRVHLQPQ MTPPNLEQYM GALLSASLPS LLNKFRSYIG
LLRLLDYSIS DEITKAVEDD FVEMRKNDPQ SISADDLHRL LVVSRLLSLS SGQTTLSREM
WLRAKQLEQQ RKSRFREQKH VNGNEL