GP_HANTV
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 03-AUG-2022, entry version 124.
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.
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 iPTMnet; P08668; -.
DR PRIDE; 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:0016021; C:integral component of 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: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; IDA:UniProtKB.
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:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
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 InterPro; IPR016402; Envelope_glycoprot_Hantavirus.
DR InterPro; IPR002532; Hanta_Gc.
DR InterPro; IPR002534; Hanta_Gn.
DR InterPro; IPR012316; ITAM_motif_hantavir-typ.
DR Pfam; PF01567; Hanta_G1; 1.
DR Pfam; PF01561; Hanta_G2; 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
