ID P0C6V4; PN Non-structural protein 11; GN 1a; OS 160235; 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: P0C6V4; DR UNIPROT: Q91QT2; 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: No; 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 MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKIT SQ PGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMR SQ RLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAG SQ TCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQK SQ ADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTA SQ LKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVC SQ KAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIH SQ SLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDD SQ GKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEV SQ DTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEA SQ EECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKV SQ VDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVD SQ EFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIV SQ NAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLV SQ DGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSL SQ GQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAI SQ VLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSY SQ ELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYT SQ QAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNI SQ YESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVE SQ GNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIG SQ KAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVW SQ FVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIF SQ NWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYC SQ KDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPT SQ AYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKN SQ AAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCH SQ NHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRF SQ FITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEG SQ FKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKP SQ WYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLI SQ VPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYM SQ QLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMH SQ CWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKF SQ EAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVS SQ YRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKF SQ IKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYG SQ GYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGV SQ DVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVP SQ LKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMF SQ LPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKC SQ AKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFST SQ NILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFC SQ IDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLA SQ VQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPD SQ PETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHG SQ VKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYF SQ IKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAIT SQ SKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSL SQ RQPKSSVQSVAGASDFDKNYLNGYGVAVRLG //