ID APC7_MOUSE Reviewed; 565 AA. AC Q9WVM3; Q3UBM7; Q8BSR2; Q91W13; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2003, sequence version 3. DT 02-SEP-2026, entry version 183. DE RecName: Full=Anaphase-promoting complex subunit 7; DE Short=APC7; DE AltName: Full=Cyclosome subunit 7; DE AltName: Full=Prediabetic NOD sera-reactive autoantigen; GN Name=Anapc7; Synonyms=Apc7; 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 [MRNA]. RX PubMed=10515598; DOI=10.1016/s1016-8478(23)13554-0; RA Kang Y., Choi K.S., Kim K.H., Kim K.S., Choi S.E., Ko I.Y., Kim H.M., RA Yoon J.W.; RT "A new autoantigen reactive with prediabetic nonobese diabetic mice sera."; RL Mol. Cells 9:358-364(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Hippocampus; 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]. RC TISSUE=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=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). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=34942119; DOI=10.1016/j.molcel.2021.11.031; RA Ferguson C.J., Urso O., Bodrug T., Gassaway B.M., Watson E.R., Prabu J.R., RA Lara-Gonzalez P., Martinez-Chacin R.C., Wu D.Y., Brigatti K.W., RA Puffenberger E.G., Taylor C.M., Haas-Givler B., Jinks R.N., Strauss K.A., RA Desai A., Gabel H.W., Gygi S.P., Schulman B.A., Brown N.G., Bonni A.; RT "APC7 mediates ubiquitin signaling in constitutive heterochromatin in the RT developing mammalian brain."; RL Mol. Cell 82:90.e13-105.e13(2022). CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls CC progression through the cell cycle (By similarity). APC/C acts by CC mediating ubiquitination and subsequent degradation of target proteins: CC it mainly mediates the formation of 'Lys-11'-linked polyubiquitin CC chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'- CC linked polyubiquitin chains (By similarity). APC/C catalyzes assembly CC of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on CC target proteins (By similarity). APC/C is activated by CDC20 in the CC metaphase/anaphase transition of cell cycle, targeting the degradation CC of cyclin B and securin (By similarity). APC/C is regulated by the CC mitotic checkpoint complex (MCC), which inhibits APC/C and delays CC chromosome segregation (By similarity). Has an enzyme-substrate adapter CC activity mediating the processive ubiquitination of specific substrates CC (PubMed:34942119). Involved in brain development through the specific CC ubiquitination and clearance of MKI67 from constitutive heterochromatin CC after neuronal progenitors exit mitosis (PubMed:34942119). CC {ECO:0000250|UniProtKB:Q9UJX3, ECO:0000269|PubMed:34942119}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:34942119}. CC -!- SUBUNIT: Homodimer (By similarity). Component of the anaphase promoting CC complex/cyclosome (APC/C), composed of ANAPC1, ANAPC2, CDC27/ANAPC3, CC ANAPC4, ANAPC5, CDC16/ANAPC6, ANAPC7, CDC23/ANAPC8, ANAPC10, ANAPC11, CC CDC26/ANAPC12, ANAPC13, ANAPC15 and ANAPC16 (By similarity). APC/C CC associates with CDC20 to form the CDC20-APC/C complex, which is crucial CC for metaphase/anaphase transition in cell cycle; this interaction is CC dependent on APC/C phosphorylation (By similarity). APC/C associates CC with mitotic checkpoint complex (MCC), which inhibits APC/C and delays CC chromosome segregation (By similarity). APC/C interacts with FZR1 and CC FBXO5 (By similarity). {ECO:0000250|UniProtKB:Q9UJX3}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q9UJX3}. Nucleus {ECO:0000250|UniProtKB:Q9UJX3}. CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UJX3}. CC Note=Localizes to spindle during metaphase and to cytoplasmic CC microtubules during interphase. {ECO:0000250|UniProtKB:Q9UJX3}. CC -!- DISRUPTION PHENOTYPE: Mice lacking Anapc7 show growth delay around CC weaning, although birth weight and adult size are normal. They show CC sensorimotor dysfunction in locomotive assays, as well as defects in CC the regulation of short- and long-term memory retrieval of the CC contextual fear response. Loss of the protein does not alter the CC anatomy of brain regions. {ECO:0000269|PubMed:34942119}. CC -!- SIMILARITY: Belongs to the APC7 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; AF076607; AAD39343.2; -; mRNA. DR EMBL; AK030775; BAC27131.1; -; mRNA. DR EMBL; AK150764; BAE29831.1; -; mRNA. DR EMBL; AK150891; BAE29937.1; -; mRNA. DR EMBL; AK153114; BAE31731.1; -; mRNA. DR EMBL; AK159523; BAE35152.1; -; mRNA. DR EMBL; AK164202; BAE37680.1; -; mRNA. DR EMBL; BC006635; AAH06635.1; -; mRNA. DR CCDS; CCDS19649.1; -. DR RefSeq; NP_062779.3; NM_019805.5. DR RefSeq; XP_036021221.1; XM_036165328.1. DR AlphaFoldDB; Q9WVM3; -. DR SMR; Q9WVM3; -. DR BioGRID; 207898; 7. DR CORUM; Q9WVM3; -. DR FunCoup; Q9WVM3; 2533. DR IntAct; Q9WVM3; 3. DR MINT; Q9WVM3; -. DR STRING; 10090.ENSMUSP00000113928; -. DR GlyGen; Q9WVM3; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9WVM3; -. DR PhosphoSitePlus; Q9WVM3; -. DR PaxDb; 10090-ENSMUSP00000113928; -. DR ProteomicsDB; 296369; -. DR Pumba; Q9WVM3; -. DR Antibodypedia; 4033; 99 antibodies from 27 providers. DR DNASU; 56317; -. DR Ensembl; ENSMUST00000031422.10; ENSMUSP00000031422.4; ENSMUSG00000029466.12. DR Ensembl; ENSMUST00000122010.8; ENSMUSP00000113928.2; ENSMUSG00000029466.12. DR GeneID; 56317; -. DR KEGG; mmu:56317; -. DR UCSC; uc008zlh.2; mouse. DR AGR; MGI:1929711; -. DR CTD; 51434; -. DR MGI; MGI:1929711; Anapc7. DR VEuPathDB; HostDB:ENSMUSG00000029466; -. DR eggNOG; KOG1174; Eukaryota. DR GeneTree; ENSGT00950000182950; -. DR HOGENOM; CLU_026953_2_0_1; -. DR InParanoid; Q9WVM3; -. DR OMA; MGECYYY; -. DR OrthoDB; 308440at2759; -. DR PhylomeDB; Q9WVM3; -. 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; 56317; 3 hits in 76 CRISPR screens. DR PRO; PR:Q9WVM3; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9WVM3; protein. DR Bgee; ENSMUSG00000029466; Expressed in ear vesicle and 252 other cell types or tissues. DR ExpressionAtlas; Q9WVM3; baseline and differential. DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB. DR GO; GO:0000792; C:heterochromatin; ISS:UniProtKB. DR GO; GO:0045171; C:intercellular bridge; ISO:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005819; C:spindle; ISS:UniProtKB. DR GO; GO:0140767; F:enzyme-substrate adaptor activity; ISS:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; ISO:GO_Central. DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:0051301; P:cell division; IBA:GO_Central. DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central. DR GO; GO:0141198; P:protein branched polyubiquitination; ISS:UniProtKB. DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR FunFam; 1.25.40.10:FF:000068; Anaphase promoting complex subunit 7; 1. DR FunFam; 1.25.40.10:FF:000126; Anaphase promoting complex subunit 7; 1. DR FunFam; 1.25.40.10:FF:000178; Anaphase promoting complex subunit 7; 1. DR FunFam; 1.25.40.10:FF:000238; Anaphase promoting complex subunit 7; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_rpt. DR PANTHER; PTHR12558:SF36; ANAPHASE-PROMOTING COMPLEX SUBUNIT 7; 1. DR PANTHER; PTHR12558; CELL DIVISION CYCLE 16,23,27; 1. DR Pfam; PF13432; TPR_16; 1. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 5. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis; KW Nucleus; Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway. FT CHAIN 1..565 FT /note="Anaphase-promoting complex subunit 7" FT /id="PRO_0000106262" FT REPEAT 36..71 FT /note="TPR 1" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 72..110 FT /note="TPR 2" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 132..165 FT /note="TPR 3" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 166..200 FT /note="TPR 4" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 201..232 FT /note="TPR 5" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 233..268 FT /note="TPR 6" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 269..302 FT /note="TPR 7" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 303..336 FT /note="TPR 8" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 337..370 FT /note="TPR 9" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 371..404 FT /note="TPR 10" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 405..439 FT /note="TPR 11" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 440..474 FT /note="TPR 12" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 475..508 FT /note="TPR 13" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REPEAT 509..540 FT /note="TPR 14" FT /evidence="ECO:0000250|UniProtKB:Q9UJX3" FT REGION 513..565 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..523 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 528..549 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 229 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT CONFLICT 156 FT /note="T -> A (in Ref. 1; AAD39343)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="M -> T (in Ref. 1; AAD39343)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="E -> K (in Ref. 2; BAC27131)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="Q -> K (in Ref. 2; BAC27131)" FT /evidence="ECO:0000305" SQ SEQUENCE 565 AA; 63021 MW; F7DFB8D45FDCD639 CRC64; MSVIDHVRDM AAAGLHSNVR LLSSLLLTMS NNNPELFSPS QKYQLLVYHA DSLFHDKEYR NAVSKYAMAL QQKKALSKTS KVRPSTGNSA STPQSQCLPS EIEVKYKMAE CYTMLKLDKD AIAVLDGIPS RQRTPKINMM LANLYKKAGQ ERPSVTSYKE VLRQCPLALD AILGLLSLSV KGAEVASMTM NVIQTVPNLD WLSVWIKAYA FVHTGDNSRA INTICSLEKK SLLRDNVDLL GSLADLYFRA GDSKNSVLKF EQAQMLDPYL IRGMDVYGYL LAREGRLEDV ENLGCRLFNI SDQHAEPWVV SGCHSFYSKR YSRALYLGAK AIQLNSNSVQ ALLLKGAALR NMGRVQEAII HFREAIRLAP CRLDCYEGLI ECYLASNSIR EAMVMANNVY KTLGANAQTL TLLATVCLED PVTQEKAKTL LDKALAQRPD YVKAVVKKAE LLSREQKYED GIALLRNALA NQSDCVLHRI LGDFLVAVNE YQEAMDQYSI ALSLDPNDQK SLEGMQKMEK EESPTDATQE EDVDDMEGSG EEGDLEGSDS EAAQWADQEQ WFGMQ //