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WPP1_ARATH
ID   WPP1_ARATH              Reviewed;         155 AA.
AC   Q9FMH6; Q8L8R9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=WPP domain-containing protein 1;
DE   AltName: Full=MFP1 attachment factor 1;
GN   Name=WPP1; Synonyms=MAF1; OrderedLocusNames=At5g43070; ORFNames=MMG4.9;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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, MUTAGENESIS OF 45-W-P-46, WPP DOMAIN, TISSUE SPECIFICITY, AND
RP   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   INTERACTION WITH WIT1; HSP70-1 AND HSP70-3, 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 HSP70-1,
CC       HSP70-3 and WIT1. Component of a ternary complex composed of WPP1,
CC       HSP70-1 and WIT1. {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}. Nucleus
CC       matrix {ECO:0000250}. Note=Associated to the nuclear envelope (NE) in
CC       undifferentiated cells of the root tip. Associated with the outer NE
CC       and the nuclear pores in interphase cells and with the immature cell
CC       plate during cytokinesis. In differentiated cells, localized in both
CC       cytoplasm and nucleus. Accumulate in speckles of the cytoplasm
CC       belonging to the Golgi apparatus (By similarity). Appears at the NE as
CC       cells reenter the cell cycle during dedifferentiation. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC       {ECO:0000269|PubMed:15548735}.
CC   -!- DOMAIN: The WPP domain is required for the nuclear envelope
CC       localization.
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DR   EMBL; AB008267; BAB08271.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94907.1; -; Genomic_DNA.
DR   EMBL; BT025708; ABF82611.1; -; mRNA.
DR   EMBL; AY088852; AAM67159.1; -; mRNA.
DR   RefSeq; NP_199121.1; NM_123673.3.
DR   AlphaFoldDB; Q9FMH6; -.
DR   SMR; Q9FMH6; -.
DR   BioGRID; 19573; 9.
DR   IntAct; Q9FMH6; 3.
DR   STRING; 3702.AT5G43070.1; -.
DR   iPTMnet; Q9FMH6; -.
DR   PaxDb; Q9FMH6; -.
DR   PRIDE; Q9FMH6; -.
DR   ProteomicsDB; 242679; -.
DR   EnsemblPlants; AT5G43070.1; AT5G43070.1; AT5G43070.
DR   GeneID; 834323; -.
DR   Gramene; AT5G43070.1; AT5G43070.1; AT5G43070.
DR   KEGG; ath:AT5G43070; -.
DR   Araport; AT5G43070; -.
DR   TAIR; locus:2167831; AT5G43070.
DR   eggNOG; ENOG502S3QB; Eukaryota.
DR   HOGENOM; CLU_101563_1_0_1; -.
DR   InParanoid; Q9FMH6; -.
DR   OMA; KHISKLM; -.
DR   OrthoDB; 1595866at2759; -.
DR   PhylomeDB; Q9FMH6; -.
DR   PRO; PR:Q9FMH6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMH6; baseline and differential.
DR   Genevisible; Q9FMH6; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005640; C:nuclear outer membrane; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
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; Reference proteome.
FT   CHAIN           1..155
FT                   /note="WPP domain-containing protein 1"
FT                   /id="PRO_0000347191"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..131
FT                   /note="WPP"
FT   REGION          124..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         45..46
FT                   /note="WP->AA: Loss of nuclear envelope localization."
FT                   /evidence="ECO:0000269|PubMed:15548735"
FT   CONFLICT        20
FT                   /note="T -> I (in Ref. 4; AAM67159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="S -> A (in Ref. 4; AAM67159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="D -> E (in Ref. 4; AAM67159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="I -> V (in Ref. 4; AAM67159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="S -> N (in Ref. 4; AAM67159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  16634 MW;  A50DCCA4511B8484 CRC64;
     MAETETESIT TSSPPPISET ENSTTLPTTE TEKNPNPVTI SLRIWPPTQK TRDAVINRLI
     ETLSTESILS KRFGSLESEE ASSVAKSIED EAYAIASATV FGDDDGIEIL KAYSKEISKR
     MLESVKAKSN VASPPPKDGD GIESAVDSKI DSSEA
 
 
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