MCMBP_SALSA
ID MCMBP_SALSA Reviewed; 626 AA.
AC B5DG51;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE Short=MCM-BP;
DE Short=MCM-binding protein;
GN Name=mcmbp;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=White muscle;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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; BT043610; ACH70725.1; -; mRNA.
DR RefSeq; NP_001135159.1; NM_001141687.1.
DR AlphaFoldDB; B5DG51; -.
DR STRING; 8030.ENSSSAP00000043894; -.
DR GeneID; 100196658; -.
DR KEGG; sasa:100196658; -.
DR CTD; 79892; -.
DR OrthoDB; 1011739at2759; -.
DR Proteomes; UP000087266; Chromosome ssa18.
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..626
FT /note="Mini-chromosome maintenance complex-binding protein"
FT /id="PRO_0000405810"
FT REGION 152..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 70816 MW; 02E7B7649C31A283 CRC64;
MPSSHDWINK PLGVVEAMFA QNNSNPEWEE KVLEYFRGQL KEKESLSWVP SLNDVPLHYL
KPNSLVKFRC LVQDMFDPEF YMGVYETVDP STKTNVLRCG KYKDVTECGV DLNSRNTVTA
ERQTFYCVPI PGESPWAKES YGCSSQARVV PSTSYVPSRQ KRSYEEDDDD MDTQPQKQRE
PHTEPHGNGD SKRQETEAPS SQTTAPSDCS SHLDLNFPLP GERGPACLVK VYEGLDSFKL
NDTLEIYGIL SVNPVLTVLG EEKDPSSLLL NPSESMESPE EQRAHDPPAS LVPRLHMLYA
RPLQHNNPLL PSAPTEDHSA FVSSFLVEMA SVRAELLAYL THVLLGDGLA AEYLLLHLIS
NVYTRRDVLP LGKFTLNLSG CPLNSYTERL YQIIQQLVPC SYRLSMSLHT MNSMRLVPKK
DYVANRLVSG ALQLARNTSL FLDETQLEQG QLDSSGVRNI TALGNLISWQ KVDYDFSYHQ
MEFPCNINVL VTSEGRSLLP SDCQVPLQPQ VTPPNMEEYL TTIHMAQFTS QMNKFRVYLS
LARTLDYSIS DEVTKAVEDD FVDMRKDDPQ SVTAEDLHRM LVVARLLSLS MGQTTLSRDG
WMRAKHIDML RRSRTEQQKS LNSNEP