ID   VP35_MABVM              Reviewed;         329 AA.
AC   P35259; Q38L44; Q6T6U2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-NOV-2023, entry version 77.
DE   RecName: Full=Polymerase cofactor VP35;
DE   AltName: Full=Marburg VP35 {ECO:0000303|PubMed:30044983};
DE            Short=mVP35 {ECO:0000303|PubMed:30044983};
GN   Name=VP35;
OS   Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain
OS   Kenya/Musoke/1980)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthomarburgvirus;
OC   Orthomarburgvirus marburgense.
OX   NCBI_TaxID=33727;
OH   NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1626422; DOI=10.1016/0168-1702(92)90027-7;
RA   Feldmann H., Muehlberger E., Randolf A., Will C., Kiley M.P., Sanchez A.,
RA   Klenk H.-D.;
RT   "Marburg virus, a filovirus: messenger RNAs, gene order, and regulatory
RT   elements of the replication cycle.";
RL   Virus Res. 24:1-19(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
RA   Chain P.S.G., Malfatti S.A., Hajjaj A., Vergez L.M., Do L.H., Smith K.L.,
RA   McCready P.M.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
RA   Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L., Hevey M.,
RA   Schmaljohn A.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Enterlein;
RX   PubMed=16379005; DOI=10.1128/jvi.80.2.1038-1043.2006;
RA   Enterlein S., Volchkov V., Weik M., Kolesnikova L., Volchkova V.,
RA   Klenk H.-D., Muehlberger E.;
RT   "Rescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid
RT   protein VP30.";
RL   J. Virol. 80:1038-1043(2006).
RN   [5]
RP   SUBUNIT, COILED-COIL DOMAIN, MUTAGENESIS OF LEU-90 AND LEU-104, AND
RP   FUNCTION.
RX   PubMed=16282487; DOI=10.1128/jvi.79.23.14876-14886.2005;
RA   Moeller P., Pariente N., Klenk H.-D., Becker S.;
RT   "Homo-oligomerization of Marburgvirus VP35 is essential for its function in
RT   replication and transcription.";
RL   J. Virol. 79:14876-14886(2005).
RN   [6]
RP   INTERACTION WITH THE NUCLEOPROTEIN, AND COILED-COIL DOMAIN.
RX   PubMed=17958906; DOI=10.1186/1743-422x-4-105;
RA   Dicarlo A., Moeller P., Lander A., Kolesnikova L., Becker S.;
RT   "Nucleocapsid formation and RNA synthesis of Marburg virus is dependent on
RT   two coiled coil motifs in the nucleoprotein.";
RL   Virol. J. 4:105-105(2007).
RN   [7]
RP   FUNCTION, AND NOMENCLATURE.
RX   PubMed=30044983; DOI=10.1016/j.celrep.2018.06.045;
RA   Edwards M.R., Liu H., Shabman R.S., Ginell G.M., Luthra P., Ramanan P.,
RA   Keefe L.J., Koellner B., Amarasinghe G.K., Taylor D.J., Leung D.W.,
RA   Basler C.F.;
RT   "Conservation of Structure and Immune Antagonist Functions of Filoviral
RT   VP35 Homologs Present in Microbat Genomes.";
RL   Cell Rep. 24:861-872(2018).
RN   [8] {ECO:0007744|PDB:4GH9, ECO:0007744|PDB:4GHA}
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 204-329, AND FUNCTION.
RX   PubMed=23028316; DOI=10.1371/journal.ppat.1002916;
RA   Bale S., Julien J.P., Bornholdt Z.A., Kimberlin C.R., Halfmann P.,
RA   Zandonatti M.A., Kunert J., Kroon G.J., Kawaoka Y., MacRae I.J.,
RA   Wilson I.A., Saphire E.O.;
RT   "Marburg virus VP35 can both fully coat the backbone and cap the ends of
RT   dsRNA for interferon antagonism.";
RL   PLoS Pathog. 8:e1002916-e1002916(2012).
RN   [9] {ECO:0007744|PDB:5TOH, ECO:0007744|PDB:5TOI}
RP   X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 60-130.
RX   PubMed=27847355; DOI=10.1128/jvi.01085-16;
RA   Bruhn J.F., Kirchdoerfer R.N., Urata S.M., Li S., Tickle I.J., Bricogne G.,
RA   Saphire E.O.;
RT   "Crystal Structure of the Marburg Virus VP35 Oligomerization Domain.";
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:0000269|PubMed:16282487, ECO:0000269|PubMed:23028316,
CC       ECO:0000269|PubMed:30044983}.
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 (PubMed:16282487). Interacts
CC       with NP (By similarity). Disrupts innate immune signaling in infected
CC       host cell (PubMed:30044983, PubMed:23028316).
CC       {ECO:0000250|UniProtKB:Q6UY68, ECO:0000269|PubMed:16282487,
CC       ECO:0000269|PubMed:23028316, ECO:0000269|PubMed:30044983}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the filoviridae polymerase cofactor VP35 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01071, ECO:0000305}.
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DR   EMBL; Z12132; CAA78115.1; -; mRNA.
DR   EMBL; AY430365; AAR85461.1; -; Genomic_RNA.
DR   EMBL; AY430366; AAR85454.1; -; Genomic_RNA.
DR   EMBL; DQ217792; ABA87125.1; -; Genomic_RNA.
DR   RefSeq; YP_001531154.1; NC_001608.3.
DR   PDB; 4GH9; X-ray; 1.65 A; A=204-329.
DR   PDB; 4GHA; X-ray; 2.50 A; A/C/E/G=204-329.
DR   PDB; 5TOH; X-ray; 2.01 A; A/B/C=60-130.
DR   PDB; 5TOI; X-ray; 2.19 A; A/B/C=60-130.
DR   PDBsum; 4GH9; -.
DR   PDBsum; 4GHA; -.
DR   PDBsum; 5TOH; -.
DR   PDBsum; 5TOI; -.
DR   SMR; P35259; -.
DR   DIP; DIP-60094N; -.
DR   DNASU; 920948; -.
DR   GeneID; 920948; -.
DR   KEGG; vg:920948; -.
DR   Proteomes; UP000007771; Genome.
DR   Proteomes; UP000137266; Genome.
DR   Proteomes; UP000160614; Genome.
DR   Proteomes; UP000180448; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IDA:CACAO.
DR   CDD; cd21030; V35-RBD_P-protein-C_like; 1.
DR   Gene3D; 2.10.10.70; Filoviridae VP35, C-terminal inhibitory domain, beta-sheet subdomain; 1.
DR   Gene3D; 1.10.8.950; Filoviridae VP35, C-terminal inhibitory domain, helical subdomain; 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_0000222162"
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         31
FT                   /note="E -> K (in strain: pp3/guinea pig lethal and
FT                   pp4/guinea pig nonlethal)"
FT   VARIANT         296
FT                   /note="S -> C (in strain: pp3/guinea pig lethal, pp4/guinea
FT                   pig nonlethal and Isolate Enterlein)"
FT   MUTAGEN         90
FT                   /note="L->A: Complete loss of homo-oligomerization; when
FT                   associated with A-104."
FT                   /evidence="ECO:0000269|PubMed:16282487"
FT   MUTAGEN         104
FT                   /note="L->A: Complete loss of homo-oligomerization; when
FT                   associated with A-90."
FT                   /evidence="ECO:0000269|PubMed:16282487"
FT   HELIX           61..75
FT                   /evidence="ECO:0007829|PDB:5TOH"
FT   HELIX           77..105
FT                   /evidence="ECO:0007829|PDB:5TOH"
FT   HELIX           111..127
FT                   /evidence="ECO:0007829|PDB:5TOH"
FT   HELIX           210..218
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   STRAND          222..225
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           227..241
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           245..257
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           262..272
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   STRAND          283..285
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           294..299
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:4GH9"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:4GH9"
SQ   SEQUENCE   329 AA;  36143 MW;  300EDE165A40938E CRC64;
     MWDSSYMQQV SEGLMTGKVP IDQVFGANPL EKLYKRRKPK GTVGLQCSPC LMSKATSTDD
     IIWDQLIVKR TLADLLIPIN RQISDIQSTL SEVTTRVHEI ERQLHEITPV LKMGRTLEAI
     SKGMSEMLAK YDHLVISTGR TTAPAAAFDA YLNEHGVPPP QPAIFKDLGV AQQACSKGTM
     VKNATTDAAD KMSKVLELSE ETFSKPNLSA KDLALLLFTH LPGNNTPFHI LAQVLSKIAY
     KSGKSGAFLD AFHQILSEGE NAQAALTRLS RTFDAFLGVV PPVIRVKNFQ TVPRPSQKSL
     RAVPPNPTID KGWVCVYSSE QGETRALKI
//