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APC4_SCHPO
ID   APC4_SCHPO              Reviewed;         719 AA.
AC   O42839; Q9P545;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Anaphase-promoting complex subunit 4;
DE   AltName: Full=20S cyclosome/APC complex protein apc4;
DE   AltName: Full=Cell untimely torn protein 20;
GN   Name=cut20; Synonyms=apc4, lid1; ORFNames=SPAC19G12.01c, SPAPJ698.04c;
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 INTERACTION WITH APC1.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10526233; DOI=10.1046/j.1365-2443.1999.00274.x;
RA   Yamashita Y.M., Nakaseko Y., Kumada K., Nakagawa T., Yanagida M.;
RT   "Fission yeast APC/cyclosome subunits, Cut20/Apc4 and Cut23/Apc8, in
RT   regulating metaphase-anaphase progression and cellular stress responses.";
RL   Genes Cells 4:445-463(1999).
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   INTERACTION WITH DIM1.
RX   PubMed=10082519; DOI=10.1128/mcb.19.4.2535;
RA   Berry L.D., Feoktistova A., Wright M.D., Gould K.L.;
RT   "The Schizosaccharomyces pombe dim1(+) gene interacts with the anaphase-
RT   promoting complex or cyclosome (APC/C) component lid1(+) and is required
RT   for APC/C function.";
RL   Mol. Cell. Biol. 19:2535-2546(1999).
RN   [4]
RP   SUBUNIT.
RX   PubMed=12477395; DOI=10.1016/s0960-9822(02)01331-3;
RA   Yoon H.-J., Feoktistova A., Wolfe B.A., Jennings J.L., Link A.J.,
RA   Gould K.L.;
RT   "Proteomics analysis identifies new components of the fission and budding
RT   yeast anaphase-promoting complexes.";
RL   Curr. Biol. 12:2048-2054(2002).
CC   -!- FUNCTION: Component of the anaphase-promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC       that controls progression through mitosis and the G1 phase of the cell
CC       cycle. The APC/C is thought to confer substrate specificity and, in the
CC       presence of ubiquitin-conjugating E2 enzymes, it catalyzes the
CC       formation of protein-ubiquitin conjugates that are subsequently
CC       degraded by the 26S proteasome. Has a role in promoting metaphase to
CC       anaphase transition via the ubiquitination of specific mitotic
CC       substrates. {ECO:0000269|PubMed:10526233}.
CC   -!- SUBUNIT: The APC/C is composed of at least 13 subunits: apc1, apc2,
CC       nuc2, apc4, apc5, cut9, apc8, apc10, apc11, hcn1, apc13, apc14 and
CC       apc15. Interacts with apc1 and dim1. {ECO:0000269|PubMed:10082519,
CC       ECO:0000269|PubMed:10526233, ECO:0000269|PubMed:12477395}.
CC   -!- INTERACTION:
CC       O42839; O74358: apc13; NbExp=4; IntAct=EBI-1251472, EBI-1251583;
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DR   EMBL; AB025243; BAA82675.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB92101.1; -; Genomic_DNA.
DR   PIR; T43508; T43508.
DR   RefSeq; XP_001713100.1; XM_001713048.2.
DR   AlphaFoldDB; O42839; -.
DR   SMR; O42839; -.
DR   BioGRID; 279069; 35.
DR   ComplexPortal; CPX-763; Anaphase-Promoting Complex variant 1.
DR   ComplexPortal; CPX-764; Anaphase-Promoting Complex variant 2.
DR   ComplexPortal; CPX-765; Anaphase-Promoting Complex variant 3.
DR   ComplexPortal; CPX-766; Anaphase-Promoting Complex variant 4.
DR   IntAct; O42839; 12.
DR   STRING; 4896.SPAC19G12.01c.1; -.
DR   MaxQB; O42839; -.
DR   PaxDb; O42839; -.
DR   PRIDE; O42839; -.
DR   EnsemblFungi; SPAC19G12.01c.1; SPAC19G12.01c.1:pep; SPAC19G12.01c.
DR   PomBase; SPAC19G12.01c; cut20.
DR   VEuPathDB; FungiDB:SPAC19G12.01c; -.
DR   eggNOG; KOG4640; Eukaryota.
DR   HOGENOM; CLU_384570_0_0_1; -.
DR   InParanoid; O42839; -.
DR   OMA; AMYEEFD; -.
DR   PhylomeDB; O42839; -.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O42839; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IMP:PomBase.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR024789; APC4.
DR   InterPro; IPR024790; APC4_long_dom.
DR   InterPro; IPR024977; Apc4_WD40_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13260; PTHR13260; 1.
DR   Pfam; PF12896; ANAPC4; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Reference proteome;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..719
FT                   /note="Anaphase-promoting complex subunit 4"
FT                   /id="PRO_0000050949"
FT   REPEAT          57..96
FT                   /note="WD"
SQ   SEQUENCE   719 AA;  82605 MW;  714A9964499991B8 CRC64;
     MVSKSFKYPK KHKFEWINET NRVERVGSGL KRVILCPSME LIAILTCSNH LICCRSNSQR
     IWDVDFHDLE ATELCWNHDG NLIVVGFKNG ELKIIDSSTG HLVEQRPASR DLAVLMITWA
     MQETIVNEKR NDFLFDATAY MPLLGTLPSS AKEERIFSSK AIAQFFEPRK REGENNKKVE
     LLSILDERGI RYINMFSSYK IGESDSLKSA LNLGVPISHS ITNDLAYHVL ICKGGTNISL
     KTLYMPLLKN DLGSIVDIAT MSTRMQHLVR YLEEVLNAMY EEFDNVFKSE ASFIKTFDAL
     VSKYSDTTFF SLQLELYQFI MNGIPSDLLK EWINERVGDR VLKNWERAMV NSYTSLIIFC
     QEFVIPACER LTVLLSSARG KSIWGHMKGN TLLDAKLVED CLATLGYLQN NVFSFLNCLF
     EEKKYMKHFI SWLNYAIVEF NTSEPSSIPP QEIIEHINET VIYIRHSLFR SKLTSYFMGT
     KPLQLRDPDY YSLKDFANQD DSNSVDDFVS FKTLKESLRD SFNVIFSYPS LTCQKQWLKT
     GDLVLFEGTD WNVSSLIPKS CNEKNQLFSL FFRKDTPNIF LIISQLMENT MLPVSGCHFG
     LDYAELLGSS LLDFQPATVL DMKLLNGSSI LILGKLKEKC FLCEICLADV PLTFFEHQQK
     NSYLDAISHL PFIPLNSCLW LHEFEKDFLP STLEYALSEN SDYGVLISRE SSRYRLFSF
 
 
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