P2A14_ARATH
ID P2A14_ARATH Reviewed; 291 AA.
AC Q9FJ80;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=F-box protein PP2-A14;
DE AltName: Full=Protein PHLOEM PROTEIN 2-LIKE A14;
DE Short=AtPP2-A14;
DE AltName: Full=SKP1-interacting partner 13;
GN Name=PP2A14; Synonyms=SKIP13; OrderedLocusNames=At5g52120;
GN ORFNames=MSG15.23;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 INTERACTION WITH SKP1A/ASK1 AND SPK1B/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 (SKP1-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with SKP1A/ASK1 and SPK1B/ASK2. {ECO:0000250,
CC ECO:0000269|PubMed:12795696}.
CC -!- INTERACTION:
CC Q9FJ80; Q9FHW7: SKP1B; NbExp=3; IntAct=EBI-604303, EBI-604076;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
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DR EMBL; AB015478; BAB11060.1; -; Genomic_DNA.
DR EMBL; AB025603; BAB11060.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED96174.1; -; Genomic_DNA.
DR EMBL; AY072088; AAL59911.1; -; mRNA.
DR EMBL; AY096374; AAM20015.1; -; mRNA.
DR RefSeq; NP_200025.1; NM_124591.6.
DR AlphaFoldDB; Q9FJ80; -.
DR BioGRID; 20533; 6.
DR IntAct; Q9FJ80; 6.
DR STRING; 3702.AT5G52120.1; -.
DR iPTMnet; Q9FJ80; -.
DR PaxDb; Q9FJ80; -.
DR PRIDE; Q9FJ80; -.
DR EnsemblPlants; AT5G52120.1; AT5G52120.1; AT5G52120.
DR GeneID; 835288; -.
DR Gramene; AT5G52120.1; AT5G52120.1; AT5G52120.
DR KEGG; ath:AT5G52120; -.
DR Araport; AT5G52120; -.
DR TAIR; locus:2173078; AT5G52120.
DR eggNOG; ENOG502QPMH; Eukaryota.
DR HOGENOM; CLU_050973_1_0_1; -.
DR InParanoid; Q9FJ80; -.
DR OMA; GEWAHYH; -.
DR OrthoDB; 910793at2759; -.
DR PhylomeDB; Q9FJ80; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FJ80; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ80; baseline and differential.
DR Genevisible; Q9FJ80; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; ISS:TAIR.
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 SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..291
FT /note="F-box protein PP2-A14"
FT /id="PRO_0000272209"
FT DOMAIN 18..64
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ SEQUENCE 291 AA; 33631 MW; BEB684A7A28A6CF3 CRC64;
MGAASSSIVR SEPFAGKLCG LEDVPENCIT AMFMYMEPPE ICLLARVNKS FHRASRSDAV
WEDKLPSNYK FLVRRILEDQ QQVGVKDKLI YRKKEIYARL CRPNLFDTGT KEAWLDKRSG
KVFLAISPKA MKITGIDDRR YWEHISSDES RFGSITYLRQ IWWLEAVGKI RFEFAPGKYS
LLFKIQLGKP IRKCGRKTCS LDQVHGWDIK PVRFQLSTSD GQCAMSERHL DESGRWVYHH
AGDFVVENQN SPVWVKFSML QIDCTHTKGG LCLDCVIICP FEYRGKYKYS D
