APC4_MOUSE
ID APC4_MOUSE Reviewed; 807 AA.
AC Q91W96; Q99LR5; Q9CZZ0;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Anaphase-promoting complex subunit 4;
DE Short=APC4;
DE AltName: Full=Cyclosome subunit 4;
GN Name=Anapc4; Synonyms=D5Ertd249e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-807.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-779, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. In the context of the APC/C complex, directly interacts with
CC UBE2S. {ECO:0000250|UniProtKB:Q9UJX5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJX5}.
CC -!- SIMILARITY: Belongs to the APC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27965.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC002259; AAH02259.1; -; mRNA.
DR EMBL; BC016237; AAH16237.1; -; mRNA.
DR EMBL; BC024870; AAH24870.1; -; mRNA.
DR EMBL; AK011994; BAB27965.1; ALT_INIT; mRNA.
DR CCDS; CCDS19290.1; -.
DR RefSeq; NP_077175.1; NM_024213.2.
DR AlphaFoldDB; Q91W96; -.
DR SMR; Q91W96; -.
DR CORUM; Q91W96; -.
DR IntAct; Q91W96; 1.
DR MINT; Q91W96; -.
DR STRING; 10090.ENSMUSP00000031072; -.
DR iPTMnet; Q91W96; -.
DR PhosphoSitePlus; Q91W96; -.
DR EPD; Q91W96; -.
DR jPOST; Q91W96; -.
DR MaxQB; Q91W96; -.
DR PaxDb; Q91W96; -.
DR PRIDE; Q91W96; -.
DR ProteomicsDB; 296368; -.
DR Antibodypedia; 23215; 217 antibodies from 34 providers.
DR DNASU; 52206; -.
DR Ensembl; ENSMUST00000031072; ENSMUSP00000031072; ENSMUSG00000029176.
DR GeneID; 52206; -.
DR KEGG; mmu:52206; -.
DR UCSC; uc008xkw.1; mouse.
DR CTD; 29945; -.
DR MGI; MGI:1098673; Anapc4.
DR VEuPathDB; HostDB:ENSMUSG00000029176; -.
DR eggNOG; KOG4640; Eukaryota.
DR GeneTree; ENSGT00390000004612; -.
DR HOGENOM; CLU_018724_0_0_1; -.
DR InParanoid; Q91W96; -.
DR OMA; HCKLFVP; -.
DR OrthoDB; 351579at2759; -.
DR PhylomeDB; Q91W96; -.
DR TreeFam; TF105443; -.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 52206; 19 hits in 75 CRISPR screens.
DR ChiTaRS; Anapc4; mouse.
DR PRO; PR:Q91W96; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91W96; protein.
DR Bgee; ENSMUSG00000029176; Expressed in floor plate of midbrain and 273 other tissues.
DR ExpressionAtlas; Q91W96; baseline and differential.
DR Genevisible; Q91W96; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
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; IPR017169; APC4_metazoa.
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 PIRSF; PIRSF037303; APC4; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Isopeptide bond; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..807
FT /note="Anaphase-promoting complex subunit 4"
FT /id="PRO_0000064596"
FT REGION 755..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 469
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 772
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX5"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX5"
SQ SEQUENCE 807 AA; 91708 MW; 1F99C8824BCCC7FC CRC64;
MLRFPTCFPS FRVVGEKQLP QEIIFLAWSP KRDLIALANT TGEVLLHRLA SFHRVWSFPP
NESTGKEVTC LAWRPDGKLL AFALADTKKI ILCDVEKPES LHSFSVEAPV SCMHWTEVTV
ESSVLTSFYN AEDESNLLLP KLPTLPKNYN STSKIFSEEN SDEIIKLLGD VRLNILVLGG
SSGFIELYAY GMFKIARVTG IAGTCIALCL SSDLKSLSVV TEVSSGGESE VSYFQLETNL
LYSFLPEVTR MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKPTTTSV
QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS HLQSGSESLL
YHLSELKGMA SWKQKYEPLG LDAAGIEDAI TAVGSFILKA NELLQVIDSS MKNFKAFFRW
LYVAMLRMTE DHVLPELNKM TQKDITFVAE FLTEHFNEAP DLYNRKGKYF NVERVGQYLK
DEDDDLVSPP NTEGNQWYDF LQNSTHLKES PLLFPYYPRK SLHFVKRRME NVIDQCLQKP
ADVIGRSMNQ AICIPLYKDA RSMDCARRLL KFPFLWNNKT SNLHYLLFTI LEDSVYKMCI
LRRHTDISQS VSNGLIGIKF GSFTSASADK VRRSSYSCLD AQFYDDETVT VILKDSMGRE
GRDRILVQLS LSLVYNSEDS DEYEFTGSYS TRLDEQGSII PTRTMHFEKH WRLLESMRAQ
YVAGNGLRKV SCVLSSNLRH VRVFEMDIDD EWEIDESSDD EEEAGGKPVK IKEEVLSESE
TEAHQDAAAL DPDVVIKVEK LDPELDS
