ID  P0C6V5;
PN  Non-structural protein 11;
GN  1a;
OS  11127;
SL  Nucleus Position: SL-0382;
SL  Comments: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles (By similarity). Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER) (By similarity). {ECO:0000250|UniProtKB:P0C6U8, ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}. [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6U8}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
DR  UNIPROT: P0C6V5;
DR  UNIPROT: Q0GNB9;
DR  PDB: 3EWO;
DR  PDB: 3EWP;
DR  PDB: 3LD1;
DR  Pfam: PF09401;
DR  Pfam: PF19218;
DR  Pfam: PF16348;
DR  Pfam: PF19217;
DR  Pfam: PF19213;
DR  Pfam: PF08716;
DR  Pfam: PF08717;
DR  Pfam: PF08710;
DR  Pfam: PF08715;
DR  Pfam: PF01661;
DR  Pfam: PF17896;
DR  Pfam: PF05409;
DR  PROSITE: PS51952;
DR  PROSITE: PS51992;
DR  PROSITE: PS51943;
DR  PROSITE: PS51944;
DR  PROSITE: PS51946;
DR  PROSITE: PS51949;
DR  PROSITE: PS51950;
DR  PROSITE: PS51951;
DR  PROSITE: PS51442;
DR  PROSITE: PS51154;
DR  PROSITE: PS51124;
DE  Function: [Isoform Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6U8}. [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|- [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln- CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6U8}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6U8}.
DE  Reference Proteome: Yes;
GO  GO:0044167;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0004197;
GO  GO:0016829;
GO  GO:0008242;
GO  GO:0003723;
GO  GO:0016740;
GO  GO:0008270;
GO  GO:0039520;
GO  GO:0006508;
GO  GO:0019079;
GO  GO:0019082;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MASSLKQGVSPKLRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRNLQTGKQFKFETVCGLFLLKGVDKIT
SQ  PGVPAKVLKATSKLADLEDIFGVSPFARKYRELLKTACQWSLTVETLDARAQTLDEIFDPTEILWLQVAAKIQVSAMAMR
SQ  RLVGEVTAKVMDALGSNMSALFQIFKQQIVRIFQKALAIFENVSELPQRIAALKMAFAKCAKSITVVVMERTLVVREFAG
SQ  TCLASINGAVAKFFEELPNGFMGAKIFTTLAFFREAAVKIVDNIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK
SQ  AEIPVESEGWSAILGGHLCYVFKSGDRFYAAPLSGNFALHDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVAELVAA
SQ  IKRGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLKLFQSARVKVEDVWSSLTEKSFEFWRLAYGKVRNLEEFVKTCFC
SQ  KAQMAIVILATVLGEGIWHLVSQVIYKVGGLFTKVVDFCEKYWKGFCAQLKRAKLIVTETLCVLKGVAQHCFQLLLDAIQ
SQ  FMYKSFKKCALGRIHGDLLFWKGGVHKIIQEGDEIWFDAIDSIDVEDLGVVQEKLIDFDVCDNVTLPENQPGHMVQIEDD
SQ  GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVFIKVSIECCGEPWNTIFKKAYKEPIEV
SQ  ETDLTVEQLLSVVYEKMCDDLKLFPEAPEPPPFENVTLVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGDA
SQ  EECDTNLECEEEDEDTKVLALIQDPASNKYPLPLDDDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKALPQKV
SQ  IDVLGDWGEAVDAQEQLCQQESTRVISEKSVEGFTGSCDAMAEQAIVEEQEIVPVVEQSQDVVVFTPADLEVVKETAEEV
SQ  DEFILISAVPKEEVVSQEKEEPQVEQEPTLVVKAQREKKAKKFKVKPATCEKPKFLEYKTCVGDLAVVIAKALDEFKEFC
SQ  IVNAANEHMSHGGGVAKAIADFCGPDFVEYCADYVKKHGPQQKLVTPSFVKGIQCVNNVVGPRHGDSNLREKLVAAYKSV
SQ  LVGGVVNYVVPVLSSGIFGVDFKISIDAMREAFKGCAIRVLLFSLSQEHIDYFDATCKQKTIYLTEDGVKYRSVVLKPGD
SQ  SLGQFGQVFARNKVVFSADDVEDKEILFIPTTDKTILEYYGLDAQKYVTYLQTLAQKWDVQYRDNFVILEWRDGNCWISS
SQ  AIVLLQAAKIRFKGFLAEAWAKLLGGDPTDFVAWCYASCNAKVGDFSDANWLLANLAEHFDADYTNALLKKCVSCNCGVK
SQ  SYELRGLEACIQPVRAPNLLHFKTQYSNCPTCGASSTDEVIEASLPYLLLFATDGPATVDCDENAVGTVVFIGSTNSGHC
SQ  YTQADGKAFDNLAKDRKFGRKSPYITAMYTRFSLRSENPLLVVEHSKGKAKVVKEDVSNLATSSKASFDDLTDFEQWYDS
SQ  NIYESLKVQETPDNLDEYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFTYKLTPDTDENSKTPVYYPVLDSISLRAIW
SQ  VEGSANFVVGHPNYYSKSLRIPTFWENAESFVKMGYKIDGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKI
SQ  LVKAATYVADKVGDGVVRNITDRIKGLCGFTRGHFEKKMSLQFLKTLVFFFFYFLKASSKSLVSSYKIVLCKVVFATLLI
SQ  VWFIYTSNPVVFTGIRVLDFLFEGSLCGPYNDYGKDSFDVLRYCAGDFTCRVCLHDRDSLHLYKHAYSVEQIYKDAASGI
SQ  NFNWNWLYLVFLILFVKPVAGFVIICYCVKYLVLSSTVLQTGVGFLDWFVKTVFTHFNFMGAGFYFWLFYKIYVQVHHIL
SQ  YCKDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVK
SQ  PTAYAYHVVYEACVVDDFVNLKYKAAIPGKDNASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEA
SQ  KNAAVYYAQYLCKPILILDQALYEQLIVEPVSKSVIDKVCSILSNIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIF
SQ  CHNHEVEYTGDGFTNVIPSYGMDTDKLTPRDRGFLINADASIANLRVKNAPPVVWKFSDLIKLSDSCLKYLISATVKSGG
SQ  RFFITKSGAKQVISCHTQKLLVEKKAGGVINNTFKWFMSCFKWLFVFYILFTACCLGYYYMEMNKSFVHPMYDVNSTLHV
SQ  EGFKVIDKGVIREIVSEDNCFSNKFVNFDAFWGKSYENNKNCPIVTVVIDGDGTVAVGVPGFVSWVMDGVMFVHMTQTDR
SQ  RPWYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVR
SQ  LIVPQQILHTPYIVKFVSDSYCRGSVCEYTKPGYCVSLDSQWVLFNDEYISKPGVFCGSTVRELMFNMVSTFFTGVNPNI
SQ  YIQLATMFLILVVIVLIFAMVIKFQGVFKAYATIVFTIMLVWVINAFVLCVHSYNSVLAVILLVLYCYASMVTSRNTAII
SQ  MHCWLVFTFGLIVPTWLACCYLGFILYMYTPLVFWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGTEFVKLTNEIGD
SQ  KFEAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEVVYTPPRYSIGVSRLQAGFKKLVSPSSAVEKCIVS
SQ  VSYRGNNLNGLWLGDSIYCPRHVLGKFSGDQWGDVLNLANNHEFEVVTQNGVTLNVVSRRLKGAVLILQTAVANAETPKY
SQ  KFVKANCGDSFTIACSYGGTVIGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEF
SQ  YGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSQPKWLESTTVSIEDYNRWASDNGFTPFSTSTAITKLSAIT
SQ  GVDVCKLLRTIMVKSAQWGSDPILGQYNFEDELTPESVFNQVGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTA
SQ  VPLKFYVHAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPW
SQ  MLLPLVLYTAFKCVQGCYMNSFNTSLLMLYQFMKLGFVIYTSSNTLTAYTEGNWELFFELVHTIVLANVSSNSLIGLIVF
SQ  KCAKWMLYYCNATYFNNYVLMAVMVNGIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKVNPPKTVWEVF
SQ  TTNILIQGIGGDRVLPIATVQSKLSDVKCTTVVLMQLLTKLNVEANSKMHAYLVELHNKILASDDVGECMDNLLGMLITL
SQ  FCIDSTIDLGEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKSIYEKVLADSKNGGVTQQELAAYRKAANIAKSVFDRD
SQ  LAVQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQANSGVVPLATVPIVCSNKLTLVI
SQ  PDPETWVKCVEGVHVTYSTVVWNIDCVTDADGTELHPTSTGSGLTYCISGDNIAWPLKVNLTRNGHNKVDVALQNNELMP
SQ  HGVKTKACVAGVDQAHCSVESKCYYTSISGSSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGDKVEVVYL
SQ  YFIKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFA
SQ  ITSKPSPTPDQDSYGGASVCLYCRAHIAHPGGAGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCD
SQ  SLRQPKPSVQSVAVASGFDKNYLNGYGVAVRLG
//