APC2_ARATH
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 03-AUG-2022, entry version 125.
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};
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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.AT2G04660.1; -.
DR PaxDb; Q8H1U5; -.
DR PRIDE; Q8H1U5; -.
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; locus:2049173; AT2G04660.
DR eggNOG; KOG2165; Eukaryota.
DR HOGENOM; CLU_007149_4_2_1; -.
DR InParanoid; Q8H1U5; -.
DR OMA; VYEKFIM; -.
DR OrthoDB; 570797at2759; -.
DR PhylomeDB; Q8H1U5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8H1U5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8H1U5; baseline and differential.
DR Genevisible; Q8H1U5; AT.
DR GO; GO:0005680; C:anaphase-promoting complex; IBA:GO_Central.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009561; P:megagametogenesis; IMP:UniProtKB.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 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; PTHR45957; 1.
DR Pfam; PF08672; ANAPC2; 1.
DR Pfam; PF00888; Cullin; 1.
DR SMART; SM01013; APC2; 1.
DR SMART; SM00182; CULLIN; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
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