P2A13_ARATH
ID P2A13_ARATH Reviewed; 290 AA.
AC Q9LEX0; Q3EAG4; Q94CC2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=F-box protein PP2-A13;
DE AltName: Full=Protein PHLOEM PROTEIN 2-LIKE A13;
DE Short=AtPP2-A13;
DE AltName: Full=SKP1-interacting partner 9;
GN Name=PP2A13; Synonyms=SKIP9; OrderedLocusNames=At3g61060;
GN ORFNames=T27I15.150;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=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 [4]
RP INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2; ASK5; ASK11 AND ASK13.
RX PubMed=12169662; DOI=10.1073/pnas.162339999;
RA Gagne J.M., Downes B.P., Shiu S.-H., Durski A.M., Vierstra R.D.;
RT "The F-box subunit of the SCF E3 complex is encoded by a diverse
RT superfamily of genes in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11519-11524(2002).
RN [5]
RP INTERACTION WITH SKPIA/ASK1 AND SKP1B/ASK2.
RX PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
RA Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
RA Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
RT "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
RT Arabidopsis.";
RL Plant J. 34:753-767(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12529520; DOI=10.1104/pp.013086;
RA Dinant S., Clark A.M., Zhu Y., Vilaine F., Palauqui J.-C., Kusiak C.,
RA Thompson G.A.;
RT "Diversity of the superfamily of phloem lectins (phloem protein 2) in
RT angiosperms.";
RL Plant Physiol. 131:114-128(2003).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with SKP1A/ASK1, SKP1B/ASK2, ASK5, ASK11 and
CC ASK13. {ECO:0000250, ECO:0000269|PubMed:12169662,
CC ECO:0000269|PubMed:12795696}.
CC -!- INTERACTION:
CC Q9LEX0; Q39255: SKP1A; NbExp=4; IntAct=EBI-604261, EBI-532357;
CC Q9LEX0; Q9FHW7: SKP1B; NbExp=6; IntAct=EBI-604261, EBI-604076;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LEX0-1; Sequence=Displayed;
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
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DR EMBL; AL358732; CAB94142.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80147.1; -; Genomic_DNA.
DR EMBL; AY034967; AAK59472.2; -; mRNA.
DR EMBL; BT000895; AAN41295.1; -; mRNA.
DR PIR; T50527; T50527.
DR RefSeq; NP_567108.2; NM_115970.4. [Q9LEX0-1]
DR AlphaFoldDB; Q9LEX0; -.
DR BioGRID; 10592; 11.
DR IntAct; Q9LEX0; 8.
DR STRING; 3702.AT3G61060.2; -.
DR PaxDb; Q9LEX0; -.
DR PRIDE; Q9LEX0; -.
DR DNASU; 825278; -.
DR EnsemblPlants; AT3G61060.1; AT3G61060.1; AT3G61060. [Q9LEX0-1]
DR GeneID; 825278; -.
DR Gramene; AT3G61060.1; AT3G61060.1; AT3G61060. [Q9LEX0-1]
DR KEGG; ath:AT3G61060; -.
DR Araport; AT3G61060; -.
DR eggNOG; ENOG502QPMH; Eukaryota.
DR InParanoid; Q9LEX0; -.
DR PhylomeDB; Q9LEX0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LEX0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LEX0; baseline and differential.
DR Genevisible; Q9LEX0; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR025886; PP2-like.
DR Pfam; PF14299; PP2; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..290
FT /note="F-box protein PP2-A13"
FT /id="PRO_0000272208"
FT DOMAIN 21..67
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT CONFLICT 207
FT /note="I -> T (in Ref. 3; AAK59472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 33115 MW; DCC145BB0D652EC9 CRC64;
MGANISGGSP EFDRNDDVYS RKLRLVDLPE NCVALIMTRL DPPEICRLAR LNRMFRRASS
ADFIWESKLP ANYRVIAHKV FDEITLTKLI KKDLYAKLSQ PNLFDDGTKE LWIDKNTGRL
CLSISSKALR ITGIDDRRYW SHIPTDESRF QSAAYVQQIW WFEVGGEFEI QFPSGTYSLF
FRIQLGKTSK RLGRRICNSE HIHGWDIKPV RFQLATSDNQ QAVSLCYLNN NPGSWSHYHV
GDFKVTNPDV STGIKFSMTQ IDCTHTKGGL CIDSVLILPK ECAKEVIGSQ
