APC7_MOUSE
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 03-AUG-2022, entry version 164.
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;
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).
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: V-shaped homodimer. The mammalian APC/C is composed at least
CC of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC FZR1 and FBXO5. {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 -!- SIMILARITY: Belongs to the APC7 family. {ECO:0000305}.
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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_019805.4.
DR AlphaFoldDB; Q9WVM3; -.
DR SMR; Q9WVM3; -.
DR BioGRID; 207898; 7.
DR CORUM; Q9WVM3; -.
DR IntAct; Q9WVM3; 3.
DR MINT; Q9WVM3; -.
DR STRING; 10090.ENSMUSP00000113928; -.
DR iPTMnet; Q9WVM3; -.
DR PhosphoSitePlus; Q9WVM3; -.
DR EPD; Q9WVM3; -.
DR MaxQB; Q9WVM3; -.
DR PaxDb; Q9WVM3; -.
DR PRIDE; Q9WVM3; -.
DR ProteomicsDB; 296369; -.
DR Antibodypedia; 4033; 97 antibodies from 26 providers.
DR DNASU; 56317; -.
DR Ensembl; ENSMUST00000031422; ENSMUSP00000031422; ENSMUSG00000029466.
DR Ensembl; ENSMUST00000122010; ENSMUSP00000113928; ENSMUSG00000029466.
DR GeneID; 56317; -.
DR KEGG; mmu:56317; -.
DR UCSC; uc008zlh.2; mouse.
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; YRFEVYK; -.
DR OrthoDB; 808566at2759; -.
DR PhylomeDB; Q9WVM3; -.
DR TreeFam; TF105445; -.
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; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Anapc7; mouse.
DR PRO; PR:Q9WVM3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WVM3; protein.
DR Bgee; ENSMUSG00000029466; Expressed in ear vesicle and 249 other tissues.
DR ExpressionAtlas; Q9WVM3; baseline and differential.
DR Genevisible; Q9WVM3; MM.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
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:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
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 GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 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 101..134
FT /note="TPR 1"
FT REPEAT 169..202
FT /note="TPR 2"
FT REPEAT 203..236
FT /note="TPR 3"
FT REPEAT 237..270
FT /note="TPR 4"
FT REPEAT 339..372
FT /note="TPR 5"
FT REPEAT 373..406
FT /note="TPR 6"
FT REPEAT 407..439
FT /note="TPR 7"
FT REPEAT 442..474
FT /note="TPR 8"
FT REPEAT 475..508
FT /note="TPR 9"
FT REPEAT 509..531
FT /note="TPR 10"
FT REGION 513..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..548
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
