ID   VP35_MABVP              Reviewed;         329 AA.
AC   Q03039;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Polymerase cofactor VP35;
DE   AltName: Full=Marburg VP35;
DE            Short=mVP35;
GN   Name=VP35;
OS   Lake Victoria marburgvirus (strain Popp-67) (MARV) (Marburg virus (strain
OS   West Germany/Popp/1967)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX   NCBI_TaxID=33728;
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].
RX   PubMed=8482365; DOI=10.1016/0014-5793(93)81107-b;
RA   Bukreyev A.A., Volchkov V.E., Blinov V.M., Netesov S.V.;
RT   "The VP35 and VP40 proteins of filoviruses. Homology between Marburg and
RT   Ebola viruses.";
RL   FEBS Lett. 322:41-46(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7487490; DOI=10.1007/bf01322532;
RA   Bukreyev A.A., Volchkov V.E., Blinov V.M., Dryga S.A., Netesov S.V.;
RT   "The complete nucleotide sequence of the Popp (1967) strain of Marburg
RT   virus: a comparison with the Musoke (1980) strain.";
RL   Arch. Virol. 140:1589-1600(1995).
RN   [3] {ECO:0007744|PDB:4GHL}
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 200-329, AND FUNCTION.
RX   PubMed=23185024; DOI=10.1073/pnas.1213559109;
RA   Ramanan P., Edwards M.R., Shabman R.S., Leung D.W., Endlich-Frazier A.C.,
RA   Borek D.M., Otwinowski Z., Liu G., Huh J., Basler C.F., Amarasinghe G.K.;
RT   "Structural basis for Marburg virus VP35-mediated immune evasion
RT   mechanisms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20661-20666(2012).
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:23185024}.
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 (By similarity). Disrupts innate immune signaling in infected
CC       host cell (By similarity). {ECO:0000250|UniProtKB:P35259,
CC       ECO:0000250|UniProtKB:Q6UY68}.
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; X64406; CAA45748.1; -; Genomic_RNA.
DR   EMBL; Z29337; CAA82537.1; -; Genomic_RNA.
DR   PIR; S32582; S32582.
DR   PDB; 4GHL; X-ray; 2.02 A; A/B/C/D=200-329.
DR   PDB; 6OTC; X-ray; 1.70 A; A=204-329.
DR   PDBsum; 4GHL; -.
DR   PDBsum; 6OTC; -.
DR   SMR; Q03039; -.
DR   ABCD; Q03039; 5 sequenced antibodies.
DR   Proteomes; UP000007772; 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; Transcription;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..329
FT                   /note="Polymerase cofactor VP35"
FT                   /id="PRO_0000222163"
FT   DOMAIN          204..329
FT                   /note="VP35 IID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01071"
FT   COILED          70..120
FT                   /evidence="ECO:0000255"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:4GHL"
FT   HELIX           210..218
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   HELIX           227..241
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   HELIX           245..257
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   HELIX           262..272
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   STRAND          283..285
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:4GHL"
FT   HELIX           294..297
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:6OTC"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:6OTC"
SQ   SEQUENCE   329 AA;  36150 MW;  1EC1333756F22C14 CRC64;
     MWDSSYMQQV SEGLMTGKVP IDQVFGANPS EKLHKRRKPK GTVGLQCSPC LMSKATSTDD
     IVWDQLIVKK TLADLLIPIN RQISDIQSTL NEVTTRVHEI ERQLHEITPV LKMGRTLEAI
     SKGMSEMLAK YDHLVISTGR TTAPAAAFDA YLNEHGVPPP QPAIFKDLGV AQQACSKGTM
     VKNETTDAAD KMSKVLELSE ETFSKPNLSA KDLALLLFTH LPGNNTPFHI LAQVLSKIAY
     KSGKSGAFLD AFHQILSEGE NAQAALTRLS RTFDAFLGVV PPVIRVKNFQ TVPRPCQKSL
     RAVPPNPTID KGWVCVYSSE QGETRALKI