PVIP_PEA
ID PVIP_PEA Reviewed; 513 AA.
AC Q84N37;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 29-SEP-2021, entry version 42.
DE RecName: Full=OBERON-like protein;
DE AltName: Full=Potyvirus VPg-interacting protein;
DE Short=PVIPp;
DE Flags: Fragment;
GN Name=PVIP;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH POTYVIRUS VPG PROTEIN.
RC STRAIN=cv. Scout; TISSUE=Leaf;
RX PubMed=14963126; DOI=10.1128/jvi.78.5.2301-2309.2004;
RA Dunoyer P., Thomas C., Harrison S., Revers F., Maule A.;
RT "A cysteine-rich plant protein potentiates Potyvirus movement through an
RT interaction with the virus genome-linked protein VPg.";
RL J. Virol. 78:2301-2309(2004).
CC -!- FUNCTION: Required for the maintenance and/or establishment of both the
CC shoot and root meristems, probably by controlling the expression of the
CC meristem genes and of genes required for auxin responses. Involved in
CC the development of the basal pole and in auxin-mediated root and
CC vascular development in the embryo (By similarity). Confers sensitivity
CC to turnip mosaic virus (TuMV) probably by promoting viral movement and
CC multiplication via interaction with TuMV VPg (Probable). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBUNIT: Self-interacts and probably forms heteromers (By similarity).
CC Binds to VPg of pea seed borne mosaic virus (PSbMV), turnip mosaic
CC virus (TuMV) and lettuce mosaic virus (LMV), but not with VPg of
CC tobacco etch virus (TEV), cowpea mosaic virus (CPMV), tomato black ring
CC virus (TBRV) and grapevine fan leaf virus (GFLV). {ECO:0000250,
CC ECO:0000269|PubMed:14963126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AY271743; AAP22955.1; -; mRNA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; ISS:UniProtKB.
DR InterPro; IPR004082; OBERON.
DR InterPro; IPR032535; Oberon_cc.
DR InterPro; IPR032881; Oberon_PHD.
DR PANTHER; PTHR21736; PTHR21736; 1.
DR Pfam; PF16312; Oberon_cc; 1.
DR Pfam; PF07227; PHD_Oberon; 1.
DR PIRSF; PIRSF025218; DUF1423_pln; 1.
DR PRINTS; PR01544; ARATH130DUF.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Host-virus interaction; Metal-binding;
KW Nucleus; Zinc; Zinc-finger.
FT CHAIN <1..513
FT /note="OBERON-like protein"
FT /id="PRO_0000399750"
FT ZN_FING 166..235
FT /note="PHD-type"
FT REGION 468..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 372..469
FT /evidence="ECO:0000255"
FT COMPBIAS 468..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 513 AA; 58302 MW; B99C48E6505800E0 CRC64;
PTADAIAAKK MENGKAAIDF PDQSVIRRVS SADRISLQDI ARERVDVICD RMHRLPDEFL
DELKNGLRAI LEGGNGSQHR DEFFILQKLV QSRSDLTAKT LIRAHRVQLE ILVSINTGIQ
GFLHPSISLS QTSLIEIFLY KRCRNIACQN QLPADECSXD TCTNNNGFCN LCMCVICSKF
DFEVNTCRWI GCDLXSHWTH TDCAIREQLI CMGPSVKSGS GPSEMVFRCQ ACSXTSXLLG
WVKDVFQHCA PSWDGDALIR ELDFVSRIFH GSKDQRGMNL FWKCDDLKEK LKSRKMDSKA
ACRAILMVFQ ELDLDNSKSL ENAESGRLIA PQEACNRIAE VVQEAIRKME FVADEKMRMF
KKARIAVEAC DRELADKARE AGDLKVERQK KKSQIEELER IVRLKNAEAD MFQLKANEAK
REAERLQRIA LAKSDKSEEE YTSNYLKQKL SEAEAEKQYL YEKIKLQESS RLSQSSGDPS
SMLMYSKIHD LLYNGPPKAD SQSNDCHPFR TNP