ID GP_HANTV Reviewed; 1135 AA. AC P08668; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 24-JAN-2024, entry version 129. DE RecName: Full=Envelopment polyprotein; DE AltName: Full=Glycoprotein precursor {ECO:0000305|PubMed:24070985}; DE AltName: Full=M polyprotein; DE Contains: DE RecName: Full=Glycoprotein N {ECO:0000305|PubMed:24070985}; DE Short=Gn; DE AltName: Full=Glycoprotein G1; DE Contains: DE RecName: Full=Glycoprotein C {ECO:0000305|PubMed:24070985}; DE Short=Gc; DE AltName: Full=Glycoprotein G2; DE Flags: Precursor; GN Name=GP; OS Hantaan virus (strain 76-118) (Korean hemorrhagic fever virus). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae; OC Orthohantavirus; Orthohantavirus hantanense. OX NCBI_TaxID=11602; OH NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse). OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=3103329; DOI=10.1016/0042-6822(87)90310-2; RA Schmaljohn C.S., Schmaljohn A.L., Dalrymple J.M.; RT "Hantaan virus M RNA: coding strategy, nucleotide sequence, and gene RT order."; RL Virology 157:31-39(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=3114716; DOI=10.1093/nar/15.15.6299; RA Yoo D., Kang C.Y.; RT "Nucleotide sequence of the M segment of the genomic RNA of Hantaan virus RT 76-118."; RL Nucleic Acids Res. 15:6299-6299(1987). RN [3] RP CLEAVAGE BY SIGNAL PEPTIDASE (ENVELOPMENT POLYPROTEIN). RX PubMed=11689045; DOI=10.1006/viro.2001.1171; RA Loeber C., Anheier B., Lindow S., Klenk H.-D., Feldmann H.; RT "The Hantaan virus glycoprotein precursor is cleaved at the conserved RT pentapeptide WAASA."; RL Virology 289:224-229(2001). RN [4] RP FUNCTION (GLYCOPROTEIN N). RX PubMed=11886265; DOI=10.1006/viro.2001.1303; RA Jin M., Park J., Lee S., Park B., Shin J., Song K.J., Ahn T.I., Hwang S.Y., RA Ahn B.Y., Ahn K.; RT "Hantaan virus enters cells by clathrin-dependent receptor-mediated RT endocytosis."; RL Virology 294:60-69(2002). RN [5] RP REVIEW. RX PubMed=24755564; DOI=10.3390/v6041801; RA Cifuentes-Munoz N., Salazar-Quiroz N., Tischler N.D.; RT "Hantavirus Gn and Gc envelope glycoproteins: key structural units for RT virus cell entry and virus assembly."; RL Viruses 6:1801-1822(2014). RN [6] RP FUNCTION (GLYCOPROTEIN C), SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND RP SUBCELLULAR LOCATION (GLYCOPROTEIN C). RX PubMed=15367644; DOI=10.1128/jvi.78.19.10776-10782.2004; RA Ogino M., Yoshimatsu K., Ebihara H., Araki K., Lee B.H., Okumura M., RA Arikawa J.; RT "Cell fusion activities of Hantaan virus envelope glycoproteins."; RL J. Virol. 78:10776-10782(2004). RN [7] RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C). RX PubMed=15657120; DOI=10.1073/pnas.0406743102; RA Raymond T., Gorbunova E., Gavrilovskaya I.N., Mackow E.R.; RT "Pathogenic hantaviruses bind plexin-semaphorin-integrin domains present at RT the apex of inactive, bent alphavbeta3 integrin conformers."; RL Proc. Natl. Acad. Sci. U.S.A. 102:1163-1168(2005). RN [8] RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C). RX PubMed=16310165; DOI=10.1016/j.bbrc.2005.11.049; RA Mou D.L., Wang Y.P., Huang C.X., Li G.Y., Pan L., Yang W.S., Bai X.F.; RT "Cellular entry of Hantaan virus A9 strain: specific interactions with RT beta3 integrins and a novel 70kDa protein."; RL Biochem. Biophys. Res. Commun. 339:611-617(2006). RN [9] RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C). RX PubMed=18834607; DOI=10.1016/j.virol.2008.08.035; RA Choi Y., Kwon Y.C., Kim S.I., Park J.M., Lee K.H., Ahn B.Y.; RT "A hantavirus causing hemorrhagic fever with renal syndrome requires RT gC1qR/p32 for efficient cell binding and infection."; RL Virology 381:178-183(2008). RN [10] RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION RP (GLYCOPROTEIN C). RX PubMed=24070985; DOI=10.1016/j.virusres.2013.09.022; RA Shimizu K., Yoshimatsu K., Koma T., Yasuda S.P., Arikawa J.; RT "Role of nucleocapsid protein of hantaviruses in intracellular traffic of RT viral glycoproteins."; RL Virus Res. 178:349-356(2013). RN [11] RP SUBUNIT (GLYCOPROTEIN C). RX PubMed=28835498; DOI=10.1128/jvi.00378-17; RA Rissanen I., Stass R., Zeltina A., Li S., Hepojoki J., Harlos K., RA Gilbert R.J.C., Huiskonen J.T., Bowden T.A.; RT "Structural Transitions of the Conserved and Metastable Hantaviral RT Glycoprotein Envelope."; RL J. Virol. 91:0-0(2017). RN [12] RP FUNCTION (GLYCOPROTEIN N), INTERACTION WITH HOST TUFM (GLYCOPROTEIN N), RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), INTERACTION WITH HOST MAP1LC3B RP (GLYCOPROTEIN N), DOMAIN (GLYCOPROTEIN N), AND MUTAGENESIS OF TYR-615 AND RP LEU-618. RC STRAIN=76-118; RX PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061; RA Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L., RA Zhang F.; RT "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate RT Autophagy Flux to Restrain Host Innate Immune Responses."; RL Cell Rep. 27:2075-2091.e5(2019). RN [13] RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C). RX PubMed=31054291; DOI=10.1016/j.virusres.2019.04.009; RA Mueller A., Baum ann A., Essbauer S., Radosa L., Krueger D.H., RA Witkowski P.T., Zeier M., Krautkraemer E.; RT "Analysis of the integrin beta3 receptor for pathogenic orthohantaviruses RT in rodent host species."; RL Virus Res. 267:36-40(2019). RN [14] RP STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS), SUBUNIT (GLYCOPROTEIN N), RP SUBUNIT (GLYCOPROTEIN C), SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND RP SUBCELLULAR LOCATION (GLYCOPROTEIN C). RX PubMed=21068243; DOI=10.1128/jvi.01847-10; RA Battisti A.J., Chu Y.K., Chipman P.R., Kaufmann B., Jonsson C.B., RA Rossmann M.G.; RT "Structural studies of Hantaan virus."; RL J. Virol. 85:835-841(2011). RN [15] {ECO:0007744|PDB:5LJX, ECO:0007744|PDB:5LJY, ECO:0007744|PDB:5LJZ, ECO:0007744|PDB:5LK0, ECO:0007744|PDB:5LK1, ECO:0007744|PDB:5LK2, ECO:0007744|PDB:5LK3} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 649-1105, GLYCOSYLATION AT RP ASN-928, DISULFIDE BOND, FUNCTION (GLYCOPROTEIN C), AND SUBUNIT RP (GLYCOPROTEIN C). RX PubMed=27783711; DOI=10.1371/journal.ppat.1005813; RA Guardado-Calvo P., Bignon E.A., Stettner E., Jeffers S.A., Perez-Vargas J., RA Pehau-Arnaudet G., Tortorici M.A., Jestin J.L., England P., Tischler N.D., RA Rey F.A.; RT "Mechanistic Insight into Bunyavirus-Induced Membrane Fusion from RT Structure-Function Analyses of the Hantavirus Envelope Glycoprotein Gc."; RL PLoS Pathog. 12:E1005813-E1005813(2016). RN [16] {ECO:0007744|PDB:6Y6P} RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 20-371, SUBUNIT (GLYCOPROTEIN N), RP SUBUNIT (GLYCOPROTEIN C), AND FUNCTION (GLYCOPROTEIN C). RX PubMed=32937107; DOI=10.1016/j.cell.2020.08.023; RA Serris A., Stass R., Bignon E.A., Muena N.A., Manuguerra J.C., Jangra R.K., RA Li S., Chandran K., Tischler N.D., Huiskonen J.T., Rey F.A., RA Guardado-Calvo P.; RT "The Hantavirus Surface Glycoprotein Lattice and Its Fusion Control RT Mechanism."; RL Cell 183:442-456.e16(2020). CC -!- FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at CC the surface of the virion. Attaches the virion to host cell receptors CC including integrin ITGAV/ITGB3 (PubMed:16310165, PubMed:31054291, CC PubMed:15657120). This attachment induces virion internalization CC predominantly through clathrin-dependent endocytosis (PubMed:11886265). CC May also bind to host C1QBP for virus entry into the host cell CC (PubMed:18834607). Mediates the assembly and budding of infectious CC virus particles through its interaction with the nucleocapsid protein CC and the viral genome (By similarity). May dysregulate normal immune and CC endothelial cell responses through an ITAM motif. Translocates to CC mitochondria, binds to host TUFM and recruits MAP1LC3B CC (PubMed:31091447). These interactions induce mitochondrial autophagy CC and therefore destruction of host MAVS leading to inhibition of type I CC interferon (IFN) responses (PubMed:31091447). Concomitant breakdown of CC glycoprotein N is apparently prevented by the nucleoprotein that may CC inhibit Gn-stimulated autophagosome-lysosome fusion (PubMed:31091447). CC Interacts with the viral genomic RNA (By similarity). CC {ECO:0000250|UniProtKB:P27312, ECO:0000269|PubMed:11886265, CC ECO:0000269|PubMed:15657120, ECO:0000269|PubMed:16310165, CC ECO:0000269|PubMed:18834607, ECO:0000269|PubMed:31054291, CC ECO:0000269|PubMed:31091447}. CC -!- FUNCTION: [Glycoprotein C]: Homodimer. Homotetramer; forms CC heterotetrameric Gn-Gc spikes in the pre-fusion conformation CC (Probable). Attaches the virion to host cell receptors including CC integrin ITGAV/ITGB3 (PubMed:16310165, PubMed:15657120, CC PubMed:31054291). This attachment induces virion internalization CC predominantly through clathrin-dependent endocytosis (PubMed:16310165). CC May also bind to host C1QBP for virus entry into the host cell CC (PubMed:18834607). Class II fusion protein that promotes fusion of CC viral membrane with host endosomal membrane after endocytosis of the CC virion (PubMed:15367644, PubMed:27783711, PubMed:32937107). CC {ECO:0000269|PubMed:15367644, ECO:0000269|PubMed:15657120, CC ECO:0000269|PubMed:16310165, ECO:0000269|PubMed:18834607, CC ECO:0000269|PubMed:27783711, ECO:0000269|PubMed:31054291, CC ECO:0000269|PubMed:32937107, ECO:0000305|PubMed:21068243}. CC -!- SUBUNIT: [Glycoprotein N]: Homodimer (Probable) (PubMed:32937107). CC Homotetramer; forms heterotetrameric Gn-Gc spikes in the pre-fusion CC conformation (Probable) (PubMed:32937107). Interacts (via C-terminus) CC with the nucleoprotein (By similarity). Interacts with host TUFM; this CC interaction contributes to the virus-induced degradation of CC mitochondria by autophagy, which leads to degradation of host MAVS and CC inhibition of type I interferon (IFN) responses (PubMed:31091447). CC Interacts with host MAP1LC3B; this interaction contributes to the CC virus-induced degradation of mitochondria by autophagy, which leads to CC degradation of host MAVS and inhibition of type I interferon (IFN) CC responses (PubMed:31091447). {ECO:0000250|UniProtKB:P0DTJ1, CC ECO:0000269|PubMed:31091447, ECO:0000269|PubMed:32937107, CC ECO:0000305|PubMed:21068243}. CC -!- SUBUNIT: [Glycoprotein C]: Homotetramer; forms heterotetrameric Gn-Gc CC spikes in the pre-fusion conformation (PubMed:28835498, CC PubMed:32937107, PubMed:21068243). Homotrimer; forms homotrimer in the CC post-fusion conformation at acidic pH (PubMed:28835498, CC PubMed:27783711). Interacts (via C-terminus) with the nucleoprotein (By CC similarity). {ECO:0000250|UniProtKB:P27312, CC ECO:0000269|PubMed:21068243, ECO:0000269|PubMed:27783711, CC ECO:0000269|PubMed:28835498, ECO:0000269|PubMed:32937107}. CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane CC {ECO:0000269|PubMed:21068243}; Multi-pass membrane protein CC {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:15367644}. Host CC Golgi apparatus membrane {ECO:0000269|PubMed:24070985}; Multi-pass CC membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Host CC mitochondrion {ECO:0000269|PubMed:31091447}. Note=Interaction between CC glycoprotein N and glycoprotein C is essential for proper targeting of CC glycoprotein N to the host Golgi complex, where virion budding occurs. CC {ECO:0000250|UniProtKB:P27312}. CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane CC {ECO:0000269|PubMed:21068243}; Single-pass type I membrane protein CC {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:15367644}. Host CC Golgi apparatus membrane {ECO:0000269|PubMed:24070985}; Single-pass CC type I membrane protein {ECO:0000305}. Host endoplasmic reticulum CC membrane {ECO:0000305}; Single-pass type I membrane protein CC {ECO:0000305}. Note=Budding probably takes place at the host Golgi CC (Probable). Glycoprotein C cytoplasmic tail is important for efficient CC Golgi localization (PubMed:24070985). {ECO:0000269|PubMed:24070985, CC ECO:0000305}. CC -!- DOMAIN: [Glycoprotein N]: The YxxL motif at the C-terminus is CC indispensable for the interaction with MAP1LC3B and for the Gn-mediated CC induction of mitochondrial autophagy (PubMed:31091447). The cytoplasmic CC tail is involved in the inhibition of the host innate immune response CC (By similarity). The C-terminus of the cytoplasmic tail is involved in CC binding to the viral genome and the nucleocapsid (By similarity). CC Contains 2 contiguous zinc-fingers (By similarity). CC {ECO:0000250|UniProtKB:P0DTJ1, ECO:0000250|UniProtKB:P27312, CC ECO:0000250|UniProtKB:Q9E006, ECO:0000269|PubMed:31091447}. CC -!- DOMAIN: [Glycoprotein C]: The C-terminus is necessary for proper CC localization in the Golgi (By similarity). The cytoplasmic tail is CC involved in binding to the nucleocapsid (By similarity). CC {ECO:0000250|UniProtKB:P27312}. CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavage in vivo CC yield the mature proteins Glycoprotein N and Glycoprotein C. CC {ECO:0000269|PubMed:11689045}. CC -!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M14627; AAA43836.1; -; Genomic_RNA. DR EMBL; Y00386; CAA68456.1; -; mRNA. DR PIR; A26348; GNVUHV. DR PIR; A29382; GNVUH7. DR PDB; 5LJX; X-ray; 1.40 A; A=649-1105. DR PDB; 5LJY; X-ray; 3.00 A; A=649-1105. DR PDB; 5LJZ; X-ray; 1.60 A; A=649-1105. DR PDB; 5LK0; X-ray; 1.80 A; A=649-1105. DR PDB; 5LK1; X-ray; 1.70 A; A=649-1105. DR PDB; 5LK2; X-ray; 1.60 A; A=649-1105. DR PDB; 5LK3; X-ray; 1.50 A; A=649-1105. DR PDB; 6Y6P; X-ray; 1.94 A; A=20-371. DR PDBsum; 5LJX; -. DR PDBsum; 5LJY; -. DR PDBsum; 5LJZ; -. DR PDBsum; 5LK0; -. DR PDBsum; 5LK1; -. DR PDBsum; 5LK2; -. DR PDBsum; 5LK3; -. DR PDBsum; 6Y6P; -. DR SMR; P08668; -. DR TCDB; 1.G.20.1.1; the hantavirus gc envelope fusion glycoprotein (gc-efg) family. DR GlyCosmos; P08668; 5 sites, No reported glycans. DR iPTMnet; P08668; -. DR ABCD; P08668; 2 sequenced antibodies. DR Proteomes; UP000008627; Genome. DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0039527; P:disruption by virus of host TRAF-mediated signal transduction; IEA:UniProtKB-KW. DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IDA:UniProtKB. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0039521; P:suppression by virus of host autophagy; IDA:UniProtKB. DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IDA:UniProtKB. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.8.1320; -; 1. DR InterPro; IPR016402; Envelope_glycoprot_Hantavirus. DR InterPro; IPR048791; Gc_C_bunya. DR InterPro; IPR048790; Gn-B_hanta. DR InterPro; IPR002532; Hanta_Gc_N. DR InterPro; IPR002534; Hanta_Gn-H. DR InterPro; IPR012316; ITAM_motif_hantavir-typ. DR Pfam; PF20682; Hanta_Gc_C; 1. DR Pfam; PF01561; Hanta_Gc_N; 1. DR Pfam; PF20679; Hanta_Gn-B; 1. DR Pfam; PF01567; Hanta_Gn-H; 1. DR Pfam; PF10538; ITAM_Cys-rich; 1. DR PIRSF; PIRSF003945; M_poly_HantaV; 1. DR PROSITE; PS51056; ITAM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activation of host autophagy by virus; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane; KW Host mitochondrion; Host-virus interaction; KW Inhibition of host innate immune response by virus; KW Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus; KW Inhibition of host TRAFs by virus; Membrane; Metal-binding; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; KW Viral attachment to host cell; Viral envelope protein; Viral immunoevasion; KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host; KW Virus entry into host cell; Zinc; Zinc-finger. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..1135 FT /note="Envelopment polyprotein" FT /id="PRO_0000036815" FT CHAIN 19..648 FT /note="Glycoprotein N" FT /id="PRO_0000036816" FT CHAIN 649..1135 FT /note="Glycoprotein C" FT /id="PRO_0000036817" FT TOPO_DOM 19..485 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 486..506 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 507..627 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 628..648 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 649..1105 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 1106..1126 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1127..1135 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 611..634 FT /note="ITAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379" FT ZN_FING 545..565 FT /note="CCHC-type 1" FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT ZN_FING 570..591 FT /note="CCHC-type 2" FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT REGION 516..533 FT /note="Binding to the ribonucleoprotein" FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT REGION 588..605 FT /note="Binding to the ribonucleoprotein" FT /evidence="ECO:0000250|UniProtKB:P27312" FT REGION 592..603 FT /note="Binding to the ribonucleoprotein" FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT REGION 611..625 FT /note="Binding to the ribonucleoprotein" FT /evidence="ECO:0000250|UniProtKB:P27312" FT REGION 757..777 FT /note="Fusion loop" FT /evidence="ECO:0000250|UniProtKB:P41266" FT REGION 1122..1135 FT /note="Binding to the ribonucleoprotein" FT /evidence="ECO:0000250|UniProtKB:P27312" FT MOTIF 615..618 FT /note="YxxL" FT /evidence="ECO:0000269|PubMed:31091447" FT SITE 648..649 FT /note="Cleavage; by host signal peptidase" FT /evidence="ECO:0000269|PubMed:11689045" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 235 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 347 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 399 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 928 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:27783711" FT DISULFID 29..151 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 63..157 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 109..128 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 133..138 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 175..185 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 210..247 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 234..351 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 376..435 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 380..389 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 405..424 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 452..475 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT DISULFID 735..770 FT DISULFID 739..777 FT DISULFID 751..885 FT DISULFID 765..896 FT DISULFID 780..904 FT DISULFID 806..815 FT DISULFID 823..832 FT DISULFID 863..867 FT DISULFID 970..1000 FT DISULFID 993..1045 FT DISULFID 1010..1015 FT DISULFID 1046..1051 FT DISULFID 1085..1089 FT /evidence="ECO:0000250|UniProtKB:Q9E006" FT MUTAGEN 615 FT /note="Y->A: Complete loss of interaction with host FT MAP1LC3B." FT /evidence="ECO:0000269|PubMed:31091447" FT MUTAGEN 618 FT /note="L->A: Complete loss of interaction with host FT MAP1LC3B." FT /evidence="ECO:0000269|PubMed:31091447" FT CONFLICT 37 FT /note="E -> G (in Ref. 2; CAA68456)" FT /evidence="ECO:0000305" FT CONFLICT 64 FT /note="N -> S (in Ref. 2; CAA68456)" FT /evidence="ECO:0000305" FT CONFLICT 173 FT /note="S -> T (in Ref. 2; CAA68456)" FT /evidence="ECO:0000305" FT STRAND 22..29 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 39..45 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 51..56 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 73..81 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 99..109 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 115..122 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 126..133 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 135..147 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 148..152 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 155..161 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 164..172 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 202..214 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 222..230 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 243..249 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:6Y6P" FT HELIX 264..275 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 291..300 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 311..319 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 325..328 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 355..370 FT /evidence="ECO:0007829|PDB:6Y6P" FT STRAND 663..665 FT /evidence="ECO:0007829|PDB:5LJX" FT HELIX 668..670 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 673..680 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 685..692 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 694..698 FT /evidence="ECO:0007829|PDB:5LK3" FT STRAND 700..707 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 711..732 FT /evidence="ECO:0007829|PDB:5LJX" FT HELIX 739..741 FT /evidence="ECO:0007829|PDB:5LJZ" FT TURN 745..748 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 750..756 FT /evidence="ECO:0007829|PDB:5LJX" FT HELIX 763..765 FT /evidence="ECO:0007829|PDB:5LJZ" FT STRAND 779..809 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 812..819 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 823..825 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 827..834 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 845..848 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 850..860 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 875..877 FT /evidence="ECO:0007829|PDB:5LJX" FT TURN 878..881 FT /evidence="ECO:0007829|PDB:5LJY" FT STRAND 892..895 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 898..900 FT /evidence="ECO:0007829|PDB:5LJY" FT STRAND 903..906 FT /evidence="ECO:0007829|PDB:5LJX" FT HELIX 913..918 FT /evidence="ECO:0007829|PDB:5LJX" FT HELIX 919..923 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 924..931 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 933..935 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 938..941 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 949..956 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 958..960 FT /evidence="ECO:0007829|PDB:5LJX" FT HELIX 962..965 FT /evidence="ECO:0007829|PDB:5LJY" FT STRAND 971..984 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 989..1011 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 1014..1034 FT /evidence="ECO:0007829|PDB:5LJX" FT STRAND 1043..1047 FT /evidence="ECO:0007829|PDB:5LJX" SQ SEQUENCE 1135 AA; 126421 MW; 8E40B8EA68EA62FA CRC64; MGIWKWLVMA SLVWPVLTLR NVYDMKIECP HTVSFGENSV IGYVELPPVP LADTAQMVPE SSCNMDNHQS LNTITKYTQV SWRGKADQSQ SSQNSFETVS TEVDLKGTCV LKHKMVEESY RSRKSVTCYD LSCNSTYCKP TLYMIVPIHA CNMMKSCLIA LGPYRVQVVY ERSYCMTGVL IEGKCFVPDQ SVVSIIKHGI FDIASVHIVC FFVAVKGNTY KIFEQVKKSF ESTCNDTENK VQGYYICIVG GNSAPIYVPT LDDFRSMEAF TGIFRSPHGE DHDLAGEEIA SYSIVGPANA KVPHSASSDT LSLIAYSGIP SYSSLSILTS STEAKHVFSP GLFPKLNHTN CDKSAIPLIW TGMIDLPGYY EAVHPCTVFC VLSGPGASCE AFSEGGIFNI TSPMCLVSKQ NRFRLTEQQV NFVCQRVDMD IVVYCNGQRK VILTKTLVIG QCIYTITSLF SLLPGVAHSI AVELCVPGFH GWATAALLVT FCFGWVLIPA ITFIILTVLK FIANIFHTSN QENRLKSVLR KIKEEFEKTK GSMVCDVCKY ECETYKELKA HGVSCPQSQC PYCFTHCEPT EAAFQAHYKV CQVTHRFRDD LKKTVTPQNF TPGCYRTLNL FRYKSRCYIF TMWIFLLVLE SILWAASASE TPLTPVWNDN AHGVGSVPMH TDLELDFSLT SSSKYTYRRK LTNPLEEAQS IDLHIEIEEQ TIGVDVHALG HWFDGRLNLK TSFHCYGACT KYEYPWHTAK CHYERDYQYE TSWGCNPSDC PGVGTGCTAC GLYLDQLKPV GSAYKIITIR YSRRVCVQFG EENLCKIIDM NDCFVSRHVK VCIIGTVSKF SQGDTLLFFG PLEGGGLIFK HWCTSTCQFG DPGDIMSPRD KGFLCPEFPG SFRKKCNFAT TPICEYDGNM VSGYKKVMAT IDSFQSFNTS TMHFTDERIE WKDPDGMLRD HINILVTKDI DFDNLGENPC KIGLQTSSIE GAWGSGVGFT LTCLVSLTEC PTFLTSIKAC DKAICYGAES VTLTRGQNTV KVSGKGGHSG STFRCCHGED CSQIGLHAAA PHLDKVNGIS EIENSKVYDD GAPQCGIKCW FVKSGEWISG IFSGNWIVLI VLCVFLLFSL VLLSILCPVR KHKKS //