ID   MVP1_GLRV3              Reviewed;         549 AA.
AC   O71192;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Movement protein Hsp70h;
DE   AltName: Full=Heat shock protein 70 homolog;
DE            Short=Hsp70h;
GN   ORFNames=ORF4;
OS   Grapevine leafroll-associated virus 3 (isolate United States/NY1) (GLRaV-3)
OS   (Grapevine leafroll-associated closterovirus (isolate 109)).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Closteroviridae; Ampelovirus.
OX   NCBI_TaxID=651354;
OH   NCBI_TaxID=29760; Vitis vinifera (Grape).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9603346; DOI=10.1099/0022-1317-79-5-1299;
RA   Ling K.S., Zhu H.Y., Drong R.F., Slightom J.L., McFerson J.R.,
RA   Gonsalves D.;
RT   "Nucleotide sequence of the 3'-terminal two-thirds of the grapevine
RT   leafroll-associated virus-3 genome reveals a typical monopartite
RT   closterovirus.";
RL   J. Gen. Virol. 79:1299-1307(1998).
CC   -!- FUNCTION: Transports viral genome to neighboring plant cells directly
CC       through plasmosdesmata, without any budding. The movement protein
CC       allows efficient cell to cell propagation, by bypassing the host cell
CC       wall barrier. Two movement proteins, p6, Hsp70h and three structural
CC       proteins, CP, CPm, and P64 are essential for cell-cell movement. Also
CC       plays a role in virion formation. Together with CPm and p64,
CC       encapsidates the 5'-terminal portion of the viral genome (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF037268; AAC40708.1; -; Genomic_RNA.
DR   RefSeq; NP_813799.1; NC_004667.1.
DR   SMR; O71192; -.
DR   PRIDE; O71192; -.
DR   GeneID; 1444470; -.
DR   KEGG; vg:1444470; -.
DR   Proteomes; UP000006707; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome; Virion.
FT   CHAIN           1..549
FT                   /note="Movement protein Hsp70h"
FT                   /id="PRO_0000402534"
SQ   SEQUENCE   549 AA;  59013 MW;  DC35C6A811D61480 CRC64;
     MEVGIDFGTT FSTICFSPSG VSGCTPVAGS VYVETQIFIP EGSSTYLIGK AAGKAYRDGV
     EGRLYVNPKR WAGVTRDNVE RYVEKLKPTY TVKIDSGGAL LIGGLGSGPD TLLRVVDVIC
     LFLRALILEC ERYTSTTVTA AVVTVPADYN SFKRSFVVEA LKGLGIPVRG VVNEPTAAAL
     YSLAKSRVED LLLAVFDFGG GTFDVSFVKK KGNILCVIFS VGDNFLGGRD IDRAIVEVIK
     QKIKGKASDA KLGIFVSSMK EDLSNNNAIT QHLIPVEGGV EVVDLTSDEL DAIVAPFSAR
     AVEVFKTGLD NFYPDPVIAV MTGGSSALVK VRSDVANLPQ ISKVVFDSTD FRCSVACGAK
     VYCDTLAGNS GLRLVDTLTN TLTDEVVGLQ PVVIFPKGSP IPCSYTHRYT VGGGDVVYGI
     FEGENNRAFL NEPTFRGVSK RRGDPVETDV AQFNLSTDGT VSVIVNGEEV KNEYLVPGTT
     NVLDSLVYKS GREDLEAKAI PEYLTTLNIL HDKAFTRRNL GNKDKGFSDL RIEENFLKSA
     VDTDTILNG