GP_ANDV
ID GP_ANDV Reviewed; 1138 AA.
AC Q9E006; Q99BV0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=Glycoprotein precursor {ECO:0000250|UniProtKB:P08668};
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P08668};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
GN ORFNames=ADT63_77597gpM {ECO:0000312|EMBL:QDI78308.1},
GN ADT63_77598gpM {ECO:0000312|EMBL:QDI78311.1};
OS Andes orthohantavirus (ANDV) (Andes virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980456;
OH NCBI_TaxID=29094; Abrothrix longipilis (Long-haired grass mouse) (Akodon longipilis).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=89122; Loxodontomys micropus (Southern big-eared mouse) (Auliscomys micropus).
OH NCBI_TaxID=37015; Oligoryzomys chacoensis (Chacoan pygmy rice rat).
OH NCBI_TaxID=218824; Oligoryzomys flavescens (yellow pygmy rice rat).
OH NCBI_TaxID=137207; Oligoryzomys longicaudatus (Long-tailed pygmy rice rat).
OH NCBI_TaxID=37019; Oligoryzomys sp..
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Chile-9717869;
RX PubMed=11907216; DOI=10.1128/jvi.76.8.3765-3773.2002;
RA Bohlman M.C., Morzunov S.P., Meissner J., Taylor M.B., Ishibashi K.,
RA Rowe J., Levis S., Enria D., St Jeor S.C.;
RT "Analysis of hantavirus genetic diversity in Argentina: S segment-derived
RT phylogeny.";
RL J. Virol. 76:3765-3773(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Chile-9717869;
RX PubMed=12367756; DOI=10.1016/s0168-1702(02)00129-6;
RA Meissner J.D., Rowe J.E., Borucki M.K., St Jeor S.C.;
RT "Complete nucleotide sequence of a Chilean hantavirus.";
RL Virus Res. 89:131-143(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AH-1;
RX PubMed=12185264; DOI=10.1099/0022-1317-83-9-2117;
RA Padula P.J., Sanchez A.J., Edelstein A., Nichol S.T.;
RT "Complete nucleotide sequence of the M RNA segment of Andes virus and
RT analysis of the variability of the termini of the virus S, M and L RNA
RT segments.";
RL J. Gen. Virol. 83:2117-2122(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ANDV/Oligoryzomys longicaudatus/CHL/9717869_01/2002
RC {ECO:0000312|EMBL:QDI78308.1}, and
RC Isolate ANDV/Oligoryzomys longicaudatus/CHL/9717869_02/2002
RC {ECO:0000312|EMBL:QDI78311.1};
RA Tan G., Fedorova N., Amedeo P., Hu L., Christensen J., Miller J.,
RA Durbin A., Williams T., Cadiz C., Duehr J., Krammer F.;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Chile-9717869 {ECO:0000312|EMBL:QRY27109.1};
RA Warner B.M., Sloan A., Deschambault Y., Dowhanik S., Tierney K., Audet J.,
RA Stein D.R., Lung O., Buchanan C., Sroga P., Griffin B.D., Siragam V.,
RA Frost K.L., Booth S., Kobasa D., Safronetz D.;
RT "Differential pathogenesis between Andes virus strains CHI-7913 and Chile-
RT 9717869 in Syrian hamsters.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DOMAIN (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN N).
RX PubMed=16973572; DOI=10.1128/jvi.00508-06;
RA Alff P.J., Gavrilovskaya I.N., Gorbunova E., Endriss K., Chong Y.,
RA Geimonen E., Sen N., Reich N.C., Mackow E.R.;
RT "The pathogenic NY-1 hantavirus G1 cytoplasmic tail inhibits RIG-I- and
RT TBK-1-directed interferon responses.";
RL J. Virol. 80:9676-9686(2006).
RN [7]
RP FUNCTION (GLYCOPROTEIN N), AND INTERACTION WITH HOST TRAF3 (GLYCOPROTEIN
RP N).
RX PubMed=24390324; DOI=10.1128/jvi.02647-13;
RA Matthys V.S., Cimica V., Dalrymple N.A., Glennon N.B., Bianco C.,
RA Mackow E.R.;
RT "Hantavirus GnT elements mediate TRAF3 binding and inhibit RIG-I/TBK1-
RT directed beta interferon transcription by blocking IRF3 phosphorylation.";
RL J. Virol. 88:2246-2259(2014).
RN [8]
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 [9]
RP SUBUNIT (GLYCOPROTEIN C).
RX PubMed=26310672; DOI=10.1099/jgv.0.000269;
RA Acuna R., Bignon E.A., Mancini R., Lozach P.Y., Tischler N.D.;
RT "Acidification triggers Andes hantavirus membrane fusion and rearrangement
RT of Gc into a stable post-fusion homotrimer.";
RL J. Gen. Virol. 96:3192-3197(2015).
RN [10]
RP FUNCTION (GLYCOPROTEIN C).
RX PubMed=27414047; DOI=10.1371/journal.pntd.0004799;
RA Barriga G.P., Villalon-Letelier F., Marquez C.L., Bignon E.A., Acuna R.,
RA Ross B.H., Monasterio O., Mardones G.A., Vidal S.E., Tischler N.D.;
RT "Inhibition of the Hantavirus Fusion Process by Predicted Domain III and
RT Stem Peptides from Glycoprotein Gc.";
RL PLoS Negl. Trop. Dis. 10:e0004799-e0004799(2016).
RN [11]
RP SUBUNIT (GLYCOPROTEIN C), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=31180319; DOI=10.7554/elife.46028;
RA Bignon E.A., Albornoz A., Guardado-Calvo P., Rey F.A., Tischler N.D.;
RT "Molecular organization and dynamics of the fusion protein Gc at the
RT hantavirus surface.";
RL Elife 8:0-0(2019).
RN [12] {ECO:0007744|PDB:2K9H}
RP STRUCTURE BY NMR OF 543-599 IN COMPLEX WITH ZINC, AND DOMAIN (GLYCOPROTEIN
RP N).
RC STRAIN=23;
RX PubMed=19179334; DOI=10.1074/jbc.m808081200;
RA Estrada D.F., Boudreaux D.M., Zhong D., St Jeor S.C., De Guzman R.N.;
RT "The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc
RT Fingers.";
RL J. Biol. Chem. 284:8654-8660(2009).
RN [13]
RP STRUCTURE BY NMR OF 534-610, AND DOMAIN (GLYCOPROTEIN N).
RX PubMed=22203819; DOI=10.3389/fmicb.2011.00251;
RA Estrada D.F., Conner M., Jeor S.C., Guzman R.N.;
RT "The Structure of the Hantavirus Zinc Finger Domain is Conserved and
RT Represents the Only Natively Folded Region of the Gn Cytoplasmic Tail.";
RL Front. Microbiol. 2:251-251(2011).
RN [14] {ECO:0007744|PDB:6Y5F, ECO:0007744|PDB:6Y5W, ECO:0007744|PDB:6Y6Q, ECO:0007744|PDB:6YRB, ECO:0007744|PDB:6YRQ, ECO:0007744|PDB:6ZJM}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 375-484, DISULFIDE BONDS, SUBUNIT
RP (GLYCOPROTEIN N), AND SUBUNIT (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 (By similarity). Attaches the virion to host
CC cell receptors including integrin ITGAV/ITGB3 (By similarity). This
CC attachment induces virion internalization possibly through clathrin-
CC dependent endocytosis and dynamin-independent macropinocytosis
CC (Probable). Mediates the assembly and budding of infectious virus
CC particles through its interaction with the nucleocapsid protein and the
CC viral genome (By similarity). May dysregulate normal immune and
CC endothelial cell responses through an ITAM motif (By similarity).
CC Translocates to mitochondria, binds to host TUFM and recruits MAP1LC3B
CC (By similarity). These interactions induce mitochondrial autophagy and
CC therefore destruction of host MAVS leading to inhibition of type I
CC interferon (IFN) responses (By similarity). Concomitant breakdown of
CC glycoprotein N is apparently prevented by the nucleoprotein that may
CC inhibit Gn-stimulated autophagosome-lysosome fusion (By similarity).
CC Interacts with the viral genomic RNA (By similarity). Inhibits the host
CC RIG-I/TBK1 pathway by disrupting the formation of TBK1-TRAF3 complexes
CC and downstream signaling responses required for IFN-beta transcription
CC (PubMed:24390324, PubMed:16973572). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312, ECO:0000269|PubMed:16973572,
CC ECO:0000269|PubMed:24390324, ECO:0000305}.
CC -!- FUNCTION: [Glycoprotein C]: Forms homotetramers with glycoprotein N at
CC the surface of the virion. Attaches the virion to host cell receptors
CC including integrin ITGAV/ITGB3. This attachment induces virion
CC internalization predominantly through clathrin-dependent endocytosis
CC (By similarity). Class II fusion protein that promotes fusion of viral
CC membrane with host endosomal membrane after endocytosis of the virion
CC (PubMed:31180319, PubMed:27414047). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000269|PubMed:27414047, ECO:0000269|PubMed:31180319}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer (PubMed:32937107). Homotetramer;
CC forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation
CC (PubMed:32937107). Interacts (via C-terminus) with the nucleoprotein
CC (By similarity). Interacts with host TUFM; this interaction contributes
CC to the virus-induced degradation of mitochondria by autophagy, which
CC leads to degradation of host MAVS and inhibition of type I interferon
CC (IFN) responses (By similarity). Interacts with host MAP1LC3B; 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 (By similarity).
CC Interacts (via C-terminus) with host TRAF3; this interaction inhibits
CC the formation of TRAF3-TBK1 complexes (PubMed:24390324).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1,
CC ECO:0000269|PubMed:24390324, ECO:0000269|PubMed:32937107}.
CC -!- SUBUNIT: [Glycoprotein C]: Homodimer (PubMed:31180319,
CC PubMed:32937107). Homotetramer; forms heterotetrameric Gn-Gc spikes in
CC the pre-fusion conformation (PubMed:32937107). Homotrimer; forms
CC homotrimer in the post-fusion conformation at acidic pH
CC (PubMed:26310672, PubMed:32937107). Interacts (via C-terminus) with the
CC nucleoprotein (By similarity). {ECO:0000250|UniProtKB:P27312,
CC ECO:0000269|PubMed:26310672, ECO:0000269|PubMed:31180319,
CC ECO:0000269|PubMed:32937107}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC {ECO:0000305}. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P08668}. Host mitochondrion
CC {ECO:0000250|UniProtKB:P08668}. Note=Interaction between glycoprotein N
CC and glycoprotein C is essential for proper targeting of glycoprotein N
CC to the host Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P27312}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P08668}; Single-pass type I membrane protein
CC {ECO:0000305}. Host cell surface {ECO:0000250|UniProtKB:P08668}. Host
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:P08668}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:P08668}. Host
CC endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08668}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:P08668}.
CC Note=Budding probably takes place at the host Golgi (Probable).
CC Glycoprotein C cytoplasmic tail is important for efficient Golgi
CC localization (By similarity). {ECO:0000250|UniProtKB:P08668,
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 (By similarity). The cytoplasmic
CC tail is involved in the inhibition of the host innate immune response
CC (PubMed:16973572). The C-terminus of the cytoplasmic tail is involved
CC in binding to the viral genome and the nucleocapsid (By similarity).
CC Contains 2 contiguous zinc-fingers (PubMed:22203819, PubMed:19179334).
CC {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P27312,
CC ECO:0000269|PubMed:16973572, ECO:0000269|PubMed:19179334,
CC ECO:0000269|PubMed:22203819}.
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]: Envelope polyprotein precursor is
CC quickly cleaved in vivo just after synthesis, presumably by host signal
CC peptidase. {ECO:0000250|UniProtKB:P08668}.
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; AF291703; AAG22532.1; -; Genomic_RNA.
DR EMBL; MN095801; QDI78308.1; -; Viral_cRNA.
DR EMBL; MN095804; QDI78311.1; -; Viral_cRNA.
DR EMBL; AF324901; AAK14322.1; -; Viral_cRNA.
DR EMBL; MT956623; QRY27109.1; -; Viral_cRNA.
DR PDB; 2K9H; NMR; -; A=543-599.
DR PDB; 6Y5F; X-ray; 3.20 A; A/B=21-374, A/B=652-1107.
DR PDB; 6Y5W; X-ray; 2.55 A; A/B=21-374, A/B=652-1107.
DR PDB; 6Y6Q; X-ray; 2.70 A; A=652-1107.
DR PDB; 6YRB; X-ray; 2.35 A; A/B=375-484.
DR PDB; 6YRQ; X-ray; 1.90 A; A/B/C/D=375-484.
DR PDB; 6ZJM; EM; 11.40 A; A/B/C/D/E/F/G/H=21-1107.
DR PDBsum; 2K9H; -.
DR PDBsum; 6Y5F; -.
DR PDBsum; 6Y5W; -.
DR PDBsum; 6Y6Q; -.
DR PDBsum; 6YRB; -.
DR PDBsum; 6YRQ; -.
DR PDBsum; 6ZJM; -.
DR SMR; Q9E006; -.
DR EvolutionaryTrace; Q9E006; -.
DR Proteomes; UP000204348; 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; IEA:UniProtKB-KW.
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:0039547; P:suppression by virus of host TRAF activity; 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; IEA:UniProtKB-KW.
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; Phosphoprotein;
KW 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..1138
FT /note="Envelopment polyprotein"
FT /id="PRO_0000455206"
FT CHAIN 19..651
FT /note="Glycoprotein N"
FT /id="PRO_0000455207"
FT CHAIN 652..1138
FT /note="Glycoprotein C"
FT /id="PRO_0000455208"
FT TOPO_DOM 19..487
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..1107
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1129..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 614..637
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT ZN_FING 548..568
FT /note="CCHC-type 1"
FT /evidence="ECO:0000269|PubMed:19179334,
FT ECO:0000269|PubMed:22203819"
FT ZN_FING 573..594
FT /note="CCHC-type 2"
FT /evidence="ECO:0000269|PubMed:19179334,
FT ECO:0000269|PubMed:22203819"
FT REGION 519..536
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000269|PubMed:22203819"
FT REGION 591..608
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 595..606
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000269|PubMed:22203819"
FT REGION 610..637
FT /note="Interaction with host TRAF3"
FT /evidence="ECO:0000250|UniProtKB:Q83887"
FT REGION 614..628
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 760..780
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT REGION 1124..1138
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT MOTIF 618..621
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT SITE 651..652
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT MOD_RES 618
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 631
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 30..155
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 64..161
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 113..132
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 137..142
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 179..189
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 214..250
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 239..354
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 379..438
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 383..392
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 408..427
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 455..478
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 738..773
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 742..780
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 754..887
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 768..898
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 783..906
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 809..818
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 826..835
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 866..870
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 972..1002
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 995..1047
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 1012..1017
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 1048..1053
FT /evidence="ECO:0000269|PubMed:32937107"
FT DISULFID 1087..1091
FT /evidence="ECO:0000269|PubMed:32937107"
FT VARIANT 8
FT /note="V -> A (in strain: AH-1)"
FT VARIANT 281
FT /note="R -> I (in strain: AH-1)"
FT VARIANT 294
FT /note="H -> Y (in strain: AH-1)"
FT VARIANT 317
FT /note="T -> I (in strain: AH-1)"
FT VARIANT 328
FT /note="L -> F (in strain: AH-1)"
FT VARIANT 346
FT /note="V -> I (in strain: AH-1)"
FT VARIANT 353
FT /note="T -> V (in strain: AH-1)"
FT VARIANT 537
FT /note="I -> V (in strain: AH-1)"
FT VARIANT 913
FT /note="I -> V (in strain: AH-1)"
FT VARIANT 1023
FT /note="T -> A (in strain: AH-1)"
SQ SEQUENCE 1138 AA; 125548 MW; AA2C5221069C4B4D CRC64;
MEGWYLVVLG VCYTLTLAMP KTIYELKMEC PHTVGLGQGY IIGSTELGLI SIEAASDIKL
ESSCNFDLHT TSMAQKSFTQ VEWRKKSDTT DTTNAASTTF EAQTKTVNLR GTCILAPELY
DTLKKVKKTV LCYDLTCNQT HCQPTVYLIA PVLTCMSIRS CMASVFTSRI QVIYEKTHCV
TGQLIEGQCF NPAHTLTLSQ PAHTYDTVTL PISCFFTPKK SEQLKVIKTF EGILTKTGCT
ENALQGYYVC FLGSHSEPLI VPSLEDIRSA EVVSRMLVHP RGEDHDAIQN SQSHLRIVGP
ITAKVPSTSS TDTLKGTAFA GVPMYSSLST LVRNADPEFV FSPGIVPESN HSTCDKKTVP
ITWTGYLPIS GEMEKVTGCT VFCTLAGPGA SCEAYSENGI FNISSPTCLV NKVQRFRGSE
QKINFICQRV DQDVVVYCNG QKKVILTKTL VIGQCIYTFT SLFSLMPDVA HSLAVELCVP
GLHGWATVML LSTFCFGWVL IPAVTLIILK CLRVLTFSCS HYTNESKFKF ILEKVKIEYQ
KTMGSMVCDV CHHECETAKE LESHRQSCIN GQCPYCMTIT EATESALQAH YSICKLTGRF
QEALKKSLKK PEVKKGCYRT LGVFRYKSRC YVGLVWCLLL TCEIVIWAAS AETPLMESGW
SDTAHGVGEI PMKTDLELDF SLPSSSSYSY RRKLTNPANK EESIPFHFQM EKQVIHAEIQ
PLGHWMDATF NIKTAFHCYG ACQKYSYPWQ TSKCFFEKDY QYETGWGCNP GDCPGVGTGC
TACGVYLDKL KSVGKAYKII SLKYTRKVCI QLGTEQTCKH IDANDCLVTP SVKVCIVGTV
SKLQPSDTLL FLGPLEQGGI ILKQWCTTSC AFGDPGDIMS TPSGMRCPEH TGSFRKICGF
ATTPVCEYQG NTISGYKRMM ATKDSFQSFN LTEPHITTNK LEWIDPDGNT RDHVNLVLNR
DVSFQDLSDN PCKVDLHTQA IEGAWGSGVG FTLTCTVGLT ECPSFMTSIK ACDLAMCYGS
TVTNLARGSN TVKVVGKGGH SGSSFKCCHD TDCSSEGLLA SAPHLERVTG FNQIDSDKVY
DDGAPPCTFK CWFTKSGEWL LGILNGNWIV VVVLVVILIL SIIMFSVLCP RRGHKKTV
