ID APC2_ARATH Reviewed; 865 AA. AC Q8H1U5; Q8GX39; Q9SJ93; DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Anaphase-promoting complex subunit 2; DE AltName: Full=Cyclosome subunit 2; GN Name=APC2; OrderedLocusNames=At2g04660; ORFNames=F28I8.30; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., RA Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP FUNCTION, INTERACTION WITH APC8 AND APC11, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=14508008; DOI=10.1105/tpc.013847; RA Capron A., Serralbo O., Fulop K., Frugier F., Parmentier Y., Dong A., RA Lecureuil A., Guerche P., Kondorosi E., Scheres B., Genschik P.; RT "The Arabidopsis anaphase-promoting complex or cyclosome: molecular and RT genetic characterization of the APC2 subunit."; RL Plant Cell 15:2370-2382(2003). RN [6] RP INTERACTION WITH CDC27A AND CDC27B. RX PubMed=17944809; DOI=10.1111/j.1365-313x.2007.03312.x; RA Perez-Perez J.M., Serralbo O., Vanstraelen M., Gonzalez C., Criqui M.C., RA Genschik P., Kondorosi E., Scheres B.; RT "Specialization of CDC27 function in the Arabidopsis thaliana anaphase- RT promoting complex (APC/C)."; RL Plant J. 53:78-89(2008). 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 complex controls several key steps in the cell cycle CC by mediating ubiquitination and subsequent degradation of target CC proteins such as cyclins. The APC/C complex is required for the female CC gametophyte development and is involved in several aspect of CC development by controlling cell division and cell elongation. Involved CC in the control of endoreduplication. {ECO:0000269|PubMed:14508008}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: The APC/C is composed of at least 10 subunits. Interacts with CC APC8, APC11, CDC27A and CDC27B. {ECO:0000269|PubMed:14508008, CC ECO:0000269|PubMed:17944809}. CC -!- INTERACTION: CC Q8H1U5; Q9M9L0: APC11; NbExp=4; IntAct=EBI-1749410, EBI-2130744; CC Q8H1U5; Q9STS3: APC8; NbExp=3; IntAct=EBI-1749410, EBI-2130714; CC Q8H1U5; Q06AN9: CDC27A; NbExp=2; IntAct=EBI-1749410, EBI-1749373; CC Q8H1U5; Q8LGU6: CDC27B; NbExp=3; IntAct=EBI-1749410, EBI-1668733; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14508008}. CC -!- TISSUE SPECIFICITY: Highly expressed in immature flowers. Expressed in CC stems, leaves and flowers. {ECO:0000269|PubMed:14508008}. CC -!- DISRUPTION PHENOTYPE: Gametophytic lethal phenotype. CC {ECO:0000269|PubMed:14508008}. CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE- CC ProRule:PRU00330}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD22340.1; Type=Erroneous gene model prediction; Evidence={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; AC006955; AAD22340.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002685; AEC05853.1; -; Genomic_DNA. DR EMBL; AK118453; BAC43061.1; -; mRNA. DR EMBL; AY138228; AAN10196.1; -; mRNA. DR PIR; H84459; H84459. DR RefSeq; NP_178543.2; NM_126495.3. DR AlphaFoldDB; Q8H1U5; -. DR SMR; Q8H1U5; -. DR BioGRID; 409; 18. DR IntAct; Q8H1U5; 19. DR STRING; 3702.Q8H1U5; -. DR PaxDb; 3702-AT2G04660-1; -. DR ProteomicsDB; 244486; -. DR EnsemblPlants; AT2G04660.1; AT2G04660.1; AT2G04660. DR GeneID; 815008; -. DR Gramene; AT2G04660.1; AT2G04660.1; AT2G04660. DR KEGG; ath:AT2G04660; -. DR Araport; AT2G04660; -. DR TAIR; AT2G04660; APC2. DR eggNOG; KOG2165; Eukaryota. DR HOGENOM; CLU_007149_4_2_1; -. DR InParanoid; Q8H1U5; -. DR OMA; WRHFDAY; -. DR OrthoDB; 2786196at2759; -. DR PhylomeDB; Q8H1U5; -. DR UniPathway; UPA00143; -. DR PRO; PR:Q8H1U5; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q8H1U5; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0009561; P:megagametogenesis; IMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR Gene3D; 1.20.1310.10; Cullin Repeats; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR044554; APC2-like. DR InterPro; IPR014786; APC2_C. DR InterPro; IPR016158; Cullin_homology. DR InterPro; IPR036317; Cullin_homology_sf. DR InterPro; IPR001373; Cullin_N. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR45957; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1. DR PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1. DR Pfam; PF08672; ANAPC2; 1. DR Pfam; PF00888; Cullin; 1. DR SMART; SM01013; APC2; 1. DR SMART; SM00182; CULLIN; 1. DR SUPFAM; SSF75632; Cullin homology domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50069; CULLIN_2; 1. DR Genevisible; Q8H1U5; AT. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; KW Ubl conjugation pathway. FT CHAIN 1..865 FT /note="Anaphase-promoting complex subunit 2" FT /id="PRO_0000396838" FT CONFLICT 247 FT /note="V -> A (in Ref. 3; BAC43061)" FT /evidence="ECO:0000305" SQ SEQUENCE 865 AA; 97791 MW; 277D9DD60E4399C3 CRC64; MEALGSSDCN LEILETLSDD AIQEITESYD GFFTTVESLI AGTGDSLVED EFVSHVYCLC KYGLDSLVRD HFLRSLEQAF EKGGASSFWQ HFDAYSEKKH HNYGEEIQIV LCKALEEISI EKQYHEKCLS IVVHALQSFK EQSSDDRQNS DTERVHLFSR FQSMLSSTLM TTLPQHFPEI LHWYFKERLE ELSAIMDGDG IEEQEDDCMD LDEKLRYKNG EMDVDEGCSQ GKRLGHDKLV KNIGKVVRDL RSIGFTSMAE NAYASAIFLL LKAKVHDLAG DDYRTSVLES IKEWIQTVPL QFLNALLSYL GDSVSYGTTS SGLTSPLACC PSPSFSRVVT PSEGIVRWKL RLEYFAYETL QDLRIAKLFE IIVDYPESSP AIEDLKQCLE YTGQHSKLVE SFISSLKYRL LTAGASTNDI LHQYVSTIKA LRAIDPAGVF LEAVGEPIRD YLRGRKDTIK CIVTMLTDGS GGNANGSGNP GDSLLEELMR DEESQENVGF DDDFHTDDKQ AWINASRWEP DPVEADPLKG SLSQRKVDIL GMLVDIIGSK EQLVNEYRVM LAEKLLNKTD YDIDTEIRTV ELLKIHFGEA SMQRCEIMLN DLIDSKRVNT NIKKASQTGA ELRENELSVD TLTSTILSTN FWPPIQDEPL ELPGPVDKLL SDYANRYHEI KTPRKLLWKK NLGTVKLELQ FEDRAMQFTV SPTHAAIIMQ FQEKKSWTYK DLAEVIGIPI DALNRRVNFW ISKGVLREST GANSNSSVLT LVESITDSGK NEGEELLTGE EEGETSIASV EDQLRKEMTI YEKFIMGMLT NFGSMALERI HNTLKMFCVA DPSYDKSLQQ LQSFLSGLVS EEKLEFRDGM YLLKK //