PVIP_NICBE
ID PVIP_NICBE Reviewed; 549 AA.
AC Q84N38;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=OBERON-like protein;
DE AltName: Full=Potyvirus VPg-interacting protein;
DE Short=PVIPnb;
GN Name=PVIP;
OS Nicotiana benthamiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4100;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH POTYVIRUS VPG PROTEIN.
RC 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; AY271742; AAP22954.1; -; mRNA.
DR AlphaFoldDB; Q84N38; -.
DR SMR; Q84N38; -.
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 InterPro; IPR001965; Znf_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 SMART; SM00249; PHD; 1.
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..549
FT /note="OBERON-like protein"
FT /id="PRO_0000399751"
FT ZN_FING 224..288
FT /note="PHD-type"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..520
FT /evidence="ECO:0000255"
FT COMPBIAS 9..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 62233 MW; A63AC23A0DA458B9 CRC64;
MLPPRQQPRP GGLQTSLSLV SPDACGSPNP QERGSTSDQA RDSPSESASS RETWPTSDAL
MLKKLEKEKE NGYTEHSVVR NISNSDKMSL RDIARERVDV IAERMRNLPD EYLEKFKHEL
RVILEGLGGA QHREEFLFLQ RLVNSRGDLT DGTLIITHRT QLEILVAIKT GIQAFLHPSV
SLSQASLIDI FLYKRCRNIA CGSMLPAEEC SCEICAKKNG FCNLCMCVIC YKFDFEVNSC
RWIGCDLCSH WTHTDCAISN GQIGTGPSVK NGASSAETLF RCHACSRTSE LLGWVKDVFQ
HCAPSWDAEA FVRELDYVRR IFQRSEDARG RKLFWKCEEL IEKLKNGVAD PMACKVILSF
FQELDVDPSK SQDNDEGGRL IAPEEAFNKI ADVVQEAIRK MEAVAEEKMR MVKKARLALD
ACDQELKDKA REVTSLKMER QRKKQQIDEL ESIVRLKQAE ADMFDLKAGE ARREAERLQR
IALAKTEKSE EDYASRYLKQ RLSEAEAEKQ YLFEKIKLQE SSRASQSSAG GNDPSQMMYS
KIQDLIKNM