WPP2_ARATH
ID WPP2_ARATH Reviewed; 180 AA.
AC Q9C500; Q8LE13;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=WPP domain-containing protein 2;
DE AltName: Full=MFP1 attachment factor 2;
GN Name=WPP2; Synonyms=MAF2; OrderedLocusNames=At1g47200;
GN ORFNames=F2G19.18, F8G22.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15548735; DOI=10.1105/tpc.104.026740;
RA Patel S., Rose A., Meulia T., Dixit R., Cyr R.J., Meier I.;
RT "Arabidopsis WPP-domain proteins are developmentally associated with the
RT nuclear envelope and promote cell division.";
RL Plant Cell 16:3260-3273(2004).
RN [6]
RP INTERACTION WITH WAP.
RX PubMed=16231153; DOI=10.1007/s00425-005-0076-0;
RA Patel S., Brkljacic J., Gindullis F., Rose A., Meier I.;
RT "The plant nuclear envelope protein MAF1 has an additional location at the
RT Golgi and binds to a novel Golgi-associated coiled-coil protein.";
RL Planta 222:1028-1040(2005).
RN [7]
RP INTERACTION WITH WIP1; WIP2 AND WIP3.
RX PubMed=17600715; DOI=10.1016/j.cub.2007.05.076;
RA Xu X.M., Meulia T., Meier I.;
RT "Anchorage of plant RanGAP to the nuclear envelope involves novel nuclear-
RT pore-associated proteins.";
RL Curr. Biol. 17:1157-1163(2007).
RN [8]
RP INTERACTION WITH WIT1.
RX PubMed=18591351; DOI=10.1105/tpc.108.059220;
RA Zhao Q., Brkljacic J., Meier I.;
RT "Two distinct interacting classes of nuclear envelope-associated coiled-
RT coil proteins are required for the tissue-specific nuclear envelope
RT targeting of Arabidopsis RanGAP.";
RL Plant Cell 20:1639-1651(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP INTERACTION WITH WIT1 AND HSP70-1, AND FUNCTION.
RX PubMed=19617588; DOI=10.1104/pp.109.143404;
RA Brkljacic J., Zhao Q., Meier I.;
RT "WPP-domain proteins mimic the activity of the HSC70-1 chaperone in
RT preventing mistargeting of RanGAP1-anchoring protein WIT1.";
RL Plant Physiol. 151:142-154(2009).
CC -!- FUNCTION: Regulates the mitotic activity in roots. Plays a role with
CC HSP70-1 in facilitating WIT1 nuclear envelope targeting.
CC {ECO:0000269|PubMed:15548735, ECO:0000269|PubMed:19617588}.
CC -!- SUBUNIT: Binds to FPP proteins (By similarity). Interacts with WAP,
CC WIP1, WIP2 and WIP3 through its WPP domain. Interacts with WIT1 and
CC HSP70-1. {ECO:0000250, ECO:0000269|PubMed:16231153,
CC ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:18591351,
CC ECO:0000269|PubMed:19617588}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:15548735}.
CC Cytoplasm {ECO:0000269|PubMed:15548735}. Nucleus
CC {ECO:0000269|PubMed:15548735}. Golgi apparatus {ECO:0000250}.
CC Note=Associated to the nuclear envelope (NE) in undifferentiated cells
CC of the root tip. Associated with the outer NE and the nuclear pores in
CC interphase cells and with the immature cell plate during cytokinesis.
CC In differentiated cells, localized in both cytoplasm and nucleus.
CC Accumulate in speckles of the cytoplasm belonging to the Golgi
CC apparatus (By similarity). Appears at the NE as cells reenter the cell
CC cycle during dedifferentiation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:15548735}.
CC -!- DOMAIN: The WPP domain is required for the nuclear envelope
CC localization. {ECO:0000250}.
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DR EMBL; AC079677; AAG52640.1; -; Genomic_DNA.
DR EMBL; AC083835; AAG50616.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32136.1; -; Genomic_DNA.
DR EMBL; AY072148; AAL59970.1; -; mRNA.
DR EMBL; AY096476; AAM20116.1; -; mRNA.
DR EMBL; AY085683; AAM62902.1; -; mRNA.
DR PIR; F96512; F96512.
DR RefSeq; NP_564498.1; NM_103613.3.
DR AlphaFoldDB; Q9C500; -.
DR SMR; Q9C500; -.
DR BioGRID; 26348; 11.
DR IntAct; Q9C500; 6.
DR STRING; 3702.AT1G47200.1; -.
DR iPTMnet; Q9C500; -.
DR PaxDb; Q9C500; -.
DR PRIDE; Q9C500; -.
DR ProteomicsDB; 242550; -.
DR EnsemblPlants; AT1G47200.1; AT1G47200.1; AT1G47200.
DR GeneID; 841123; -.
DR Gramene; AT1G47200.1; AT1G47200.1; AT1G47200.
DR KEGG; ath:AT1G47200; -.
DR Araport; AT1G47200; -.
DR TAIR; locus:2036736; AT1G47200.
DR eggNOG; ENOG502S3QB; Eukaryota.
DR HOGENOM; CLU_101563_1_0_1; -.
DR InParanoid; Q9C500; -.
DR OrthoDB; 1595866at2759; -.
DR PhylomeDB; Q9C500; -.
DR PRO; PR:Q9C500; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C500; baseline and differential.
DR Genevisible; Q9C500; AT.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:TAIR.
DR Gene3D; 1.10.246.200; -; 1.
DR InterPro; IPR044692; WPP1/2/3.
DR InterPro; IPR025265; WPP_dom.
DR InterPro; IPR038214; WPP_sf.
DR PANTHER; PTHR34362; PTHR34362; 1.
DR Pfam; PF13943; WPP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..180
FT /note="WPP domain-containing protein 2"
FT /id="PRO_0000347192"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..147
FT /note="WPP"
FT REGION 140..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 172
FT /note="A -> G (in Ref. 4; AAM62902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 19134 MW; F71F090976FA3826 CRC64;
MAETAETINT TISSPPPESE SSTTISAMTD PTSQEAASKD TDLTKEAESE KKPGGISLRI
WPPTQKTRDA VLNRLIETLS TESILSKRYG TLKSDDATTV AKLIEEEAYG VASNAVSSDD
DGIKILELYS KEISKRMLES VKARSNASVG NGSVEDANTD ASEVSKDDAG PASEEEKSEA
