VP35_MABVO
ID VP35_MABVO Reviewed; 329 AA.
AC Q6UY68; O36425;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Polymerase cofactor VP35;
DE AltName: Full=Marburg VP35;
DE Short=mVP35;
GN Name=VP35;
OS Lake Victoria marburgvirus (strain Ozolin-75) (MARV) (Marburg virus (strain
OS South Africa/Ozolin/1975)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=482820;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Sanchez;
RX PubMed=9448698; DOI=10.1006/viro.1997.8902;
RA Sanchez A., Trappier S.G., Stroeher U., Nichol S.T., Bowen M.D.,
RA Feldmann H.;
RT "Variation in the glycoprotein and VP35 genes of Marburg virus strains.";
RL Virology 240:138-146(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Bowen M.D., Thurman K., Minor E., Ibrahim M.S., Meyer R.F., Malfatti S.A.,
RA Do L.H., Smith K.L., McCready P.M., Chain P.S.G.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:5XSQ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-28, AND INTERACTION WITH NP.
RX PubMed=28659479; DOI=10.1128/jvi.00996-17;
RA Zhu T., Song H., Peng R., Shi Y., Qi J., Gao G.F.;
RT "Crystal Structure of the Marburg Virus Nucleoprotein Core Domain
RT Chaperoned by a VP35 Peptide Reveals a Conserved Drug Target for
RT Filovirus.";
RL J. Virol. 91:0-0(2017).
RN [4] {ECO:0007744|PDB:5F5O}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-29, INTERACTION WITH NP, AND
RP FUNCTION.
RX PubMed=28566377; DOI=10.1128/jvi.00825-17;
RA Liu B., Dong S., Li G., Wang W., Liu X., Wang Y., Yang C., Rao Z., Guo Y.;
RT "Structural Insight into Nucleoprotein Conformation Change Chaperoned by
RT VP35 Peptide in Marburg Virus.";
RL J. Virol. 91:0-0(2017).
CC -!- FUNCTION: Plays an essential role in viral RNA synthesis and also a
CC role in suppressing innate immune signaling.
CC {ECO:0000250|UniProtKB:P35259, ECO:0000269|PubMed:28566377}.
CC -!- SUBUNIT: Homooligomer. Homomultimerization via the coiled coil domain
CC is a prerequisite for binding to L. Found in a trimeric complex in
CC which VP35 bridges L and the nucleoprotein (By similarity). Interacts
CC with NP (PubMed:28566377, PubMed:28659479). Disrupts innate immune
CC signaling in infected host cell (By similarity).
CC {ECO:0000250|UniProtKB:P35259, ECO:0000269|PubMed:28566377,
CC ECO:0000269|PubMed:28659479}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P35259}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P35259}.
CC -!- SIMILARITY: Belongs to the filoviridae polymerase cofactor VP35 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01071, ECO:0000305}.
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DR EMBL; AF005730; AAC40455.1; -; Genomic_RNA.
DR EMBL; AY358025; AAQ55256.1; -; Genomic_RNA.
DR PDB; 5F5O; X-ray; 2.20 A; B/D/F=1-29.
DR PDB; 5XSQ; X-ray; 2.60 A; B/D/F=1-28.
DR PDBsum; 5F5O; -.
DR PDBsum; 5XSQ; -.
DR SMR; Q6UY68; -.
DR PRIDE; Q6UY68; -.
DR Proteomes; UP000000838; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.8.950; -; 1.
DR Gene3D; 2.10.10.70; -; 1.
DR InterPro; IPR002953; Filo_VP35.
DR InterPro; IPR031163; VP35_IID.
DR InterPro; IPR043061; VP35_IID_b-sht.
DR InterPro; IPR043060; VP35_IID_hlx.
DR Pfam; PF02097; Filo_VP35; 1.
DR PIRSF; PIRSF018326; VP35_FiloV; 1.
DR PRINTS; PR01240; FILOVP35.
DR PROSITE; PS51735; VP35_IID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Host cytoplasm; Reference proteome;
KW Transcription; Viral RNA replication; Virion.
FT CHAIN 1..329
FT /note="Polymerase cofactor VP35"
FT /id="PRO_0000314996"
FT DOMAIN 204..329
FT /note="VP35 IID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01071"
FT COILED 70..120
FT /evidence="ECO:0000255"
FT VARIANT 49
FT /note="P -> L (in strain: Isolate Sanchez)"
FT VARIANT 72
FT /note="L -> H (in strain: Isolate Sanchez)"
FT VARIANT 83..84
FT /note="IS -> TL (in strain: Isolate Sanchez)"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5F5O"
SQ SEQUENCE 329 AA; 36131 MW; 3AE46FB8DDB09386 CRC64;
MWDSSYMQQV SEGLMTGKVP IDQVFGANPL EKLYKRRKPK GTVGLQCSPC LMSKATSTDD
IIWDQLIVKK TLADLLIPIN RQISDIQSTL SEVTTRVHEI ERQLHEITPV LKMGRTLEAI
SKGMSEMLAK YDHLVISTGR TTAPAAAFDA YLNEHGVPPP QPAIFKDLGV AQQACSKGTM
VKNATTDAAD KMSKVLELSE ETFSKPNLSA KDLALLLFTH LPGNNTPFHI LAQVLSKIAY
KSGKSGAFLD AFHQILSEGE NAQAALTRLS RTFDAFLGVV PPVIRVKNFQ TVPRPCQKSL
RAVPPNPTID KGWVCVYSSE QGETRALKI