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MCL1_SCHPO
ID   MCL1_SCHPO              Reviewed;         815 AA.
AC   Q9C107;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Minichromosome loss protein 1;
DE   AltName: Full=DNA polymerase alpha accessory factor Mcl1;
GN   Name=mcl1; Synonyms=slr3; ORFNames=SPAPB1E7.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12455694; DOI=10.1128/ec.1.5.758-773.2002;
RA   Williams D.R., McIntosh J.R.;
RT   "mcl1+, the Schizosaccharomyces pombe homologue of CTF4, is important for
RT   chromosome replication, cohesion, and segregation.";
RL   Eukaryot. Cell 1:758-773(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH POL1.
RX   PubMed=15915339; DOI=10.1007/s00294-005-0584-2;
RA   Tsutsui Y., Morishita T., Natsume T., Yamashita K., Iwasaki H., Yamao F.,
RA   Shinagawa H.;
RT   "Genetic and physical interactions between Schizosaccharomyces pombe Mcl1
RT   and Rad2, Dna2 and DNA polymerase alpha: evidence for a multifunctional
RT   role of Mcl1 in DNA replication and repair.";
RL   Curr. Genet. 48:34-43(2005).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH POL1.
RX   PubMed=15643072; DOI=10.1128/ec.4.1.166-177.2005;
RA   Williams D.R., McIntosh J.R.;
RT   "Mcl1p is a polymerase alpha replication accessory factor important for S-
RT   phase DNA damage survival.";
RL   Eukaryot. Cell 4:166-177(2005).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH POF3.
RX   PubMed=16997270; DOI=10.1016/j.bbrc.2006.09.024;
RA   Mamnun Y.M., Katayama S., Toda T.;
RT   "Fission yeast Mcl1 interacts with SCF(Pof3) and is required for centromere
RT   formation.";
RL   Biochem. Biophys. Res. Commun. 350:125-130(2006).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Has a role in regulating DNA replication complexes. Acts as a
CC       regulator of post DNA replication initiation. Associates with chromatin
CC       during G1 and S phases of mitosis. Required for the transcriptional
CC       repression of the outer repeats of the centromeric region. Acts as a
CC       polymerase alpha replication accessory factor and is important for S-
CC       phase DNA damage survival. Plays a role in lagging-strand synthesis and
CC       Ozaki fragment processing, in addition to DNA repair.
CC       {ECO:0000269|PubMed:12455694, ECO:0000269|PubMed:15643072,
CC       ECO:0000269|PubMed:15915339, ECO:0000269|PubMed:16997270}.
CC   -!- SUBUNIT: Interacts with pof3 and pol1. {ECO:0000269|PubMed:15643072,
CC       ECO:0000269|PubMed:15915339, ECO:0000269|PubMed:16997270}.
CC   -!- INTERACTION:
CC       Q9C107; O74991: pof3; NbExp=2; IntAct=EBI-1203666, EBI-1153554;
CC       Q9C107; P28040: pol1; NbExp=10; IntAct=EBI-1203666, EBI-455823;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
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DR   EMBL; CU329670; CAC36919.1; -; Genomic_DNA.
DR   RefSeq; NP_594128.1; NM_001019552.2.
DR   AlphaFoldDB; Q9C107; -.
DR   SMR; Q9C107; -.
DR   BioGRID; 279809; 268.
DR   IntAct; Q9C107; 3.
DR   MINT; Q9C107; -.
DR   STRING; 4896.SPAPB1E7.02c.1; -.
DR   MaxQB; Q9C107; -.
DR   PaxDb; Q9C107; -.
DR   EnsemblFungi; SPAPB1E7.02c.1; SPAPB1E7.02c.1:pep; SPAPB1E7.02c.
DR   GeneID; 2543387; -.
DR   KEGG; spo:SPAPB1E7.02c; -.
DR   PomBase; SPAPB1E7.02c; mcl1.
DR   VEuPathDB; FungiDB:SPAPB1E7.02c; -.
DR   eggNOG; KOG1274; Eukaryota.
DR   HOGENOM; CLU_004219_2_1_1; -.
DR   InParanoid; Q9C107; -.
DR   OMA; NAWFPIC; -.
DR   PhylomeDB; Q9C107; -.
DR   PRO; PR:Q9C107; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0043596; C:nuclear replication fork; IDA:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IGI:PomBase.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR024977; Apc4_WD40_dom.
DR   InterPro; IPR022100; Mcl1_mid.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF12341; Mcl1_mid; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Chromosome; DNA damage; DNA repair; DNA replication; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   WD repeat.
FT   CHAIN           1..815
FT                   /note="Minichromosome loss protein 1"
FT                   /id="PRO_0000051073"
FT   REPEAT          11..50
FT                   /note="WD 1"
FT   REPEAT          53..90
FT                   /note="WD 2"
FT   REPEAT          93..132
FT                   /note="WD 3"
FT   REPEAT          135..174
FT                   /note="WD 4"
FT   REPEAT          228..267
FT                   /note="WD 5"
FT   REPEAT          517..553
FT                   /note="WD 6"
FT   REGION          306..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  90986 MW;  D3AD3EF2D7997C54 CRC64;
     MAGNRLVPRY AHTDGLTRLA YTRDGKFLLT VGSNQVIRKF QVGSDEEPDS IDNHQDPITG
     IAVAENYFCT CSEDATVCVY PIDSPTEHTL LARTTLPIRD VAYSVDGNWI AIASDETAVK
     VVSSTDSSQI FSLRPAKASN KHVTYSPNGN FLAVSSCNGI LYFYDTQTRE LIKFLTNTIA
     SLEAESEICS KAAWHPKNGT FAVASTDHFV SVISPDDWLP LYKLLPKENH SGVTDISWSS
     NGMYIAASFK KGGILIWDTQ SHEVVVELPY STVVALAWQP FENVLSFTTN QGILYSCPDV
     IPKSILKEEN DPTKPLTSSK SKNRTSKELD DLFGSDDEQS QNVNDLDGNS ANEENEFINH
     DGLDSSLDLD GDSYMVDEND LNLAKKRKQK ALIDRTTTIE NGSSKRRLLQ ASIHKPVHTG
     STPWQGNRRY LCLNLVGFIW TVQQDAEHNT ITVEFHDETT HRKYHFVDDQ KFEMACLDHE
     GALYASPATE SSPGVIYYKA HVDWSRKSEW AMALPMENES PVTISLSSSV VLVCTSAGYV
     RVFSRQGFPI SIHRSKHLPF VACSSFQDTI ITIANDGLSS DGNSRLVYSI EDISRDEMLQ
     TGDGVALPPQ GTLESVFFSD VGDPYIYDST GVLLVLMHWR IPGQAKWIPV LDTNELERRK
     SRQESYWPVT VADNQFHCIL LKGASRYPYF PRPMFTEFDF RIPCNTNNPD ASTSVPVLEE
     LQLRNKLFLT LLEDSIGDGD VTEDEKISIA RLEANIDKAL LQLIQKACLE ERIERVYELT
     KTLRRTTSIA AAQKIALHHS LTNVAEKIGN LLSNV
 
 
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