MCMBP_CHICK
ID MCMBP_CHICK Reviewed; 633 AA.
AC Q5ZJV4; E1BXG4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE Short=MCM-BP;
DE Short=MCM-binding protein;
GN Name=MCMBP; ORFNames=RCJMB04_15g11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associates with
CC chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ720330; CAG31989.1; -; mRNA.
DR EMBL; AADN02030984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001012930.1; NM_001012912.1.
DR AlphaFoldDB; Q5ZJV4; -.
DR STRING; 9031.ENSGALP00000037974; -.
DR PaxDb; Q5ZJV4; -.
DR GeneID; 423933; -.
DR KEGG; gga:423933; -.
DR CTD; 79892; -.
DR VEuPathDB; HostDB:geneid_423933; -.
DR eggNOG; KOG2545; Eukaryota.
DR InParanoid; Q5ZJV4; -.
DR OrthoDB; 1011739at2759; -.
DR PhylomeDB; Q5ZJV4; -.
DR PRO; PR:Q5ZJV4; -.
DR Proteomes; UP000000539; Unplaced.
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..633
FT /note="Mini-chromosome maintenance complex-binding protein"
FT /id="PRO_0000089826"
FT REGION 154..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 144..148
FT /note="YLFSL -> AYISAS (in Ref. 1; CAG31989)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="M -> T (in Ref. 1; CAG31989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 71924 MW; 2BA9ADDFC0C9F6BA CRC64;
MPCVADWLNN PFSIVQGIFA QNTPNSDWEK KVTDYFKEKL KENNATNWVP SLNDVPVHYL
KPNSLVKFRC MVQDMFDPEF YMGVYETVDP NTNARVLHFG KYRDVAECGP QQEIDMNSSQ
TVTLERQTFY CVPVPGESAW VKEYLFSLQA RVSPSTSYTP SRHKRSYEED EDMEQHPSKQ
KEQHMGSGGD SHGCGEPKRL ETEASAGHHL ISPNCSPPLD LNFPLPGEKG PACLVKVYES
WDTFKVNDVL EVYGILSVDP VLSIVNSEER DSSMLDPMEC MDTAEEQRVH SPPSSLVPRI
HVILAHKLQH LNPLLPACLN EEESKTFVSN FMSELSPVRA ELLGFLTHAL LGDSLAAEYL
ILHLISTVYA RRDVLPLGKF TVNLSGCPRN SIFTEHIYRI IQQLVPASYR LQMTIENMNH
SRFIPRKDYT ANRLVSGILQ LASNTSLVID ETQLEQGQLD TKGVHNVKAL GNLITWQKVD
YDFSYHQMEF PCNINVLITS EGRSLLPSDC QVQLQPQIIP PNMEEYMNSL LTAVLPSVLN
KFRIYLSLLR LLDYSISDEV TKAVEEDFVE MRKNDPESIT ADDLHRTLLV ARFLSLSAGQ
TTLSRERWLR AKQLEALRKA RLQQQKCVNG NEL
