APC5_MOUSE
ID APC5_MOUSE Reviewed; 740 AA.
AC Q8BTZ4; Q3TGA7; Q80UJ6; Q80W43; Q8BWW7; Q8C0F7; Q9CRX0; Q9CSL1; Q9JJB8;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Anaphase-promoting complex subunit 5;
DE Short=APC5;
DE AltName: Full=Cyclosome subunit 5;
GN Name=Anapc5; ORFNames=MNCb-2778;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Embryo, Heart, Kidney, Spinal cord, Testis, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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. {ECO:0000250|UniProtKB:Q9UJX4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJX4}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UJX4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BTZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BTZ4-2; Sequence=VSP_008472;
CC -!- SIMILARITY: Belongs to the APC5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95076.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB041593; BAA95076.1; ALT_FRAME; mRNA.
DR EMBL; AK012579; BAB28331.1; -; mRNA.
DR EMBL; AK013978; BAB29097.1; -; mRNA.
DR EMBL; AK031432; BAC27401.1; -; mRNA.
DR EMBL; AK049719; BAC33891.1; -; mRNA.
DR EMBL; AK088327; BAC40284.1; -; mRNA.
DR EMBL; AK159916; BAE35479.1; -; mRNA.
DR EMBL; AK168814; BAE40641.1; -; mRNA.
DR EMBL; AK169196; BAE40972.1; -; mRNA.
DR EMBL; BC010339; AAH10339.1; -; mRNA.
DR EMBL; BC046566; AAH46566.1; -; mRNA.
DR EMBL; BC046804; AAH46804.1; -; mRNA.
DR CCDS; CCDS39258.1; -. [Q8BTZ4-1]
DR CCDS; CCDS80397.1; -. [Q8BTZ4-2]
DR RefSeq; NP_001035956.1; NM_001042491.2. [Q8BTZ4-2]
DR RefSeq; NP_067480.2; NM_021505.3. [Q8BTZ4-1]
DR AlphaFoldDB; Q8BTZ4; -.
DR SMR; Q8BTZ4; -.
DR BioGRID; 208479; 20.
DR CORUM; Q8BTZ4; -.
DR IntAct; Q8BTZ4; 10.
DR STRING; 10090.ENSMUSP00000083393; -.
DR iPTMnet; Q8BTZ4; -.
DR PhosphoSitePlus; Q8BTZ4; -.
DR EPD; Q8BTZ4; -.
DR MaxQB; Q8BTZ4; -.
DR PaxDb; Q8BTZ4; -.
DR PRIDE; Q8BTZ4; -.
DR ProteomicsDB; 281898; -. [Q8BTZ4-1]
DR ProteomicsDB; 281899; -. [Q8BTZ4-2]
DR Antibodypedia; 31562; 374 antibodies from 37 providers.
DR DNASU; 59008; -.
DR Ensembl; ENSMUST00000086216; ENSMUSP00000083393; ENSMUSG00000029472. [Q8BTZ4-1]
DR Ensembl; ENSMUST00000200645; ENSMUSP00000142922; ENSMUSG00000029472. [Q8BTZ4-2]
DR GeneID; 59008; -.
DR KEGG; mmu:59008; -.
DR UCSC; uc008zmg.2; mouse. [Q8BTZ4-1]
DR CTD; 51433; -.
DR MGI; MGI:1929722; Anapc5.
DR VEuPathDB; HostDB:ENSMUSG00000029472; -.
DR eggNOG; KOG4322; Eukaryota.
DR GeneTree; ENSGT00390000018674; -.
DR HOGENOM; CLU_020635_0_0_1; -.
DR InParanoid; Q8BTZ4; -.
DR OMA; TVMHLTG; -.
DR OrthoDB; 240631at2759; -.
DR PhylomeDB; Q8BTZ4; -.
DR TreeFam; TF105444; -.
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; 59008; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Anapc5; mouse.
DR PRO; PR:Q8BTZ4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BTZ4; protein.
DR Bgee; ENSMUSG00000029472; Expressed in bone fossa and 263 other tissues.
DR ExpressionAtlas; Q8BTZ4; baseline and differential.
DR Genevisible; Q8BTZ4; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; 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:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR037679; Apc5.
DR InterPro; IPR026000; Apc5_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12830; PTHR12830; 1.
DR Pfam; PF12862; ANAPC5; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..740
FT /note="Anaphase-promoting complex subunit 5"
FT /id="PRO_0000064598"
FT REPEAT 194..234
FT /note="TPR 1"
FT REPEAT 235..285
FT /note="TPR 2"
FT REPEAT 286..322
FT /note="TPR 3"
FT REPEAT 323..363
FT /note="TPR 4"
FT REPEAT 364..403
FT /note="TPR 5"
FT REPEAT 404..451
FT /note="TPR 6"
FT REPEAT 452..485
FT /note="TPR 7"
FT REPEAT 486..525
FT /note="TPR 8"
FT REPEAT 526..565
FT /note="TPR 9"
FT REPEAT 566..605
FT /note="TPR 10"
FT REPEAT 606..645
FT /note="TPR 11"
FT REPEAT 646..681
FT /note="TPR 12"
FT REPEAT 682..721
FT /note="TPR 13"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX4"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJX4"
FT VAR_SEQ 360..372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008472"
FT CONFLICT 72
FT /note="E -> V (in Ref. 1; BAA95076)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> E (in Ref. 2; BAC33891)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="R -> H (in Ref. 1; BAA95076)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="F -> S (in Ref. 1; BAA95076)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="H -> Y (in Ref. 1; BAA95076)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="I -> V (in Ref. 1; BAA95076)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="V -> I (in Ref. 3; AAH46566)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="S -> T (in Ref. 2; BAC27401)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="I -> V (in Ref. 3; AAH46566)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="A -> T (in Ref. 2; BAC33891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 83098 MW; 43CCD0615BCFC184 CRC64;
MMTNGVVHAN LFGIKDWVTP YKIAVLVLLN EMGRTGEGAV SLVERRKLNQ LLLPLLQGPD
ITLSKLYKLI EESCPQLANS VQIRIKLMAE GELKDMEQFF DDLSDSFSGT EPEVHKTSVV
GLFLRHMILA YSKLSFSQVF KLYTALQQYF QNGEKKTVED ADMDREDGEK QMEKEELDVS
VREEEVSCSG PLSQKQAEFF LSQQAALLKN DETKALTPAS LQKELNNLLK FNPDFAEAHY
LSYLNNLRVQ DVFSSTHSLL HYFDRLILTG AEGKSNGEEG YGRSLRYAAL NLAALHCRFG
HYQQAELALQ EAIRIAQESN DHVCLQHCLS WLYVLGQKRA DSYVLLEHSV KKAVHFGLPY
LASLGIQSLV QQRAFAGKTA NKLMDALKDS DLLHWKHSLS ELIDISIAQK TAIWRLYGRS
TMALQQAQML LSMNSLESLN AGVQQNNTES FAVALCHLAE LHAEQGCFAA AGEVLKHLKD
RFPPNSQHAQ LWMLCDQKIQ FDRAMNDGKF HLADSLVTGI TALNGIEGVY RKAVVLQAQN
QMTEAHKLLQ KLLTYCQKLK NTEMVISVLL SVAELYWRSS SPTIAMPVLL EALALSKEYR
LQYLASETVL NLAYAQLILG IPEQALTLLH MAIEPILADG AVLDKGRAMF LVSKCQVASA
ASYDPVKKAE ALEAAIQNLS EAKNYFAQVD CRERIRDVAY FQARLYHALG KTQERNHCAM
IFRQLHQELP AHGVPLINHL
