GP_RVFV
ID GP_RVFV Reviewed; 1206 AA.
AC P03518; Q86494; Q86495;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=NSm-Gn protein {ECO:0000250|UniProtKB:P21401};
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P21401};
DE Short=Gn;
DE AltName: Full=Glycoprotein G1;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P21401};
DE Short=Gc;
DE AltName: Full=Glycoprotein G2;
DE Flags: Precursor;
GN Name=GP;
OS Rift valley fever virus (RVFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX NCBI_TaxID=11588;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=297284; Bos taurus x Bison bison (beefalo).
OH NCBI_TaxID=9837; Camelus bactrianus (Bactrian camel).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2998042; DOI=10.1016/0042-6822(85)90320-4;
RA Collett M.S., Purchio A.F., Keegan K., Frazier S., Hays W., Anderson D.K.,
RA Parker M.D., Schmaljohn C.S., Schmidt J., Dalrymple J.M.;
RT "Complete nucleotide sequence of the M RNA segment of Rift Valley fever
RT virus.";
RL Virology 144:228-245(1985).
RN [2]
RP FUNCTION (ISOFORM NSM PROTEIN).
RX PubMed=24551252; DOI=10.1371/journal.pntd.0002670;
RA Kading R.C., Crabtree M.B., Bird B.H., Nichol S.T., Erickson B.R.,
RA Horiuchi K., Biggerstaff B.J., Miller B.R.;
RT "Deletion of the NSm virulence gene of Rift Valley fever virus inhibits
RT virus replication in and dissemination from the midgut of Aedes aegypti
RT mosquitoes.";
RL PLoS Negl. Trop. Dis. 8:e2670-e2670(2014).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (22.0 ANGSTROMS) OF THE VIRAL PARTICLE,
RP SUBUNIT (GLYCOPROTEIN N), SUBUNIT (GLYCOPROTEIN C), FUNCTION (GLYCOPROTEIN
RP N), AND FUNCTION (GLYCOPROTEIN C).
RC STRAIN=Clone 13 {ECO:0000305};
RX PubMed=19193794; DOI=10.1128/jvi.02483-08;
RA Huiskonen J.T., Overby A.K., Weber F., Gruenewald K.;
RT "Electron cryo-microscopy and single-particle averaging of Rift Valley
RT fever virus: evidence for GN-GC glycoprotein heterodimers.";
RL J. Virol. 83:3762-3769(2009).
RN [4] {ECO:0007744|PDB:4HJ1, ECO:0007744|PDB:4HJC}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 691-1119, AND GLYCOSYLATION AT
RP ASN-794 AND ASN-1035.
RX PubMed=23319635; DOI=10.1073/pnas.1217780110;
RA Dessau M., Modis Y.;
RT "Crystal structure of glycoprotein C from Rift Valley fever virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1696-1701(2013).
RN [5] {ECO:0007744|PDB:5Y0W, ECO:0007744|PDB:5Y0Y}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 154-469, AND DISULFIDE BONDS.
RX PubMed=28827346; DOI=10.1073/pnas.1705176114;
RA Wu Y., Zhu Y., Gao F., Jiao Y., Oladejo B.O., Chai Y., Bi Y., Lu S.,
RA Dong M., Zhang C., Huang G., Wong G., Li N., Zhang Y., Li Y., Feng W.H.,
RA Shi Y., Liang M., Zhang R., Qi J., Gao G.F.;
RT "Structures of phlebovirus glycoprotein Gn and identification of a
RT neutralizing antibody epitope.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7564-E7573(2017).
RN [6] {ECO:0007744|PDB:6EGT, ECO:0007744|PDB:6EGU}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 691-1158, FUNCTION (GLYCOPROTEIN
RP C), AND SUBUNIT (GLYCOPROTEIN C).
RX PubMed=29097548; DOI=10.1126/science.aal2712;
RA Guardado-Calvo P., Atkovska K., Jeffers S.A., Grau N., Backovic M.,
RA Perez-Vargas J., de Boer S.M., Tortorici M.A., Pehau-Arnaudet G.,
RA Lepault J., England P., Rottier P.J., Bosch B.J., Hub J.S., Rey F.A.;
RT "A glycerophospholipid-specific pocket in the RVFV class II fusion protein
RT drives target membrane insertion.";
RL Science 358:663-667(2017).
RN [7] {ECO:0007744|PDB:6IEA, ECO:0007744|PDB:6IEB, ECO:0007744|PDB:6IEC, ECO:0007744|PDB:6IEK}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 154-469.
RX PubMed=30936489; DOI=10.1038/s41564-019-0411-z;
RA Wang Q., Ma T., Wu Y., Chen Z., Zeng H., Tong Z., Gao F., Qi J., Zhao Z.,
RA Chai Y., Yang H., Wong G., Bi Y., Wu L., Shi R., Yang M., Song J.,
RA Jiang H., An Z., Wang J., Yilma T.D., Shi Y., Liu W.J., Liang M., Qin C.,
RA Gao G.F., Yan J.;
RT "Neutralization mechanism of human monoclonal antibodies against Rift
RT Valley fever virus.";
RL Nat. Microbiol. 4:1231-1241(2019).
CC -!- FUNCTION: [Glycoprotein N]: Structural component of the virion that
CC interacts with glycoprotein C (By similarity). It shields the
CC hydrophobic fusion loops of the glycoprotein C, preventing premature
CC fusion (By similarity). The glycoprotein protrusions are arranged on an
CC icosahedral lattice, with T=12 triangulation (PubMed:19193794,
CC PubMed:23319635). They are able to attach the virion to the host cell
CC receptor CD209/DC-SIGN and to promote fusion of membranes with the late
CC endosome after endocytosis of the virion (By similarity). Plays a role
CC in the packaging of ribonucleoproteins and polymerase during virus
CC assembly (By similarity). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000250|UniProtKB:P21401, ECO:0000269|PubMed:19193794,
CC ECO:0000269|PubMed:23319635}.
CC -!- FUNCTION: [Glycoprotein C]: Structural component of the virion that
CC interacts with glycoprotein N (By similarity). Acts as a class II
CC fusion protein that is activated upon acidification and subsequent
CC repositioning of the glycoprotein N (PubMed:23319635, PubMed:29097548).
CC The glycoprotein protrusions are arranged on an icosahedral lattice,
CC with T=12 triangulation (PubMed:19193794, PubMed:23319635). They are
CC able to attach the virion to the host cell receptor CD209/DC-SIGN and
CC to promote fusion of membranes with the late endosome after endocytosis
CC of the virion (By similarity). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000269|PubMed:19193794, ECO:0000269|PubMed:23319635,
CC ECO:0000269|PubMed:29097548}.
CC -!- FUNCTION: [Isoform NSm protein]: Plays a role for virus dissemination
CC in the mosquito. {ECO:0000250|UniProtKB:P21401,
CC ECO:0000269|PubMed:24551252}.
CC -!- FUNCTION: [NSm-Gn protein]: Plays a role for virus dissemination in
CC mosquitoes. {ECO:0000250|UniProtKB:P21401}.
CC -!- SUBUNIT: [Glycoprotein N]: Heterodimer with glycoprotein C
CC (PubMed:19193794, PubMed:28827346). Interacts with nucleocapsid protein
CC N and with the polymerase L in order to package them into virus
CC particles (By similarity). {ECO:0000250|UniProtKB:P21401,
CC ECO:0000269|PubMed:19193794, ECO:0000269|PubMed:28827346}.
CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein C
CC (PubMed:19193794, PubMed:28827346). Homotrimer (postfusion)
CC (PubMed:29097548). Interacts with nucleocapsid protein N and with the
CC polymerase L in order to package them into virus particles (By
CC similarity). Interacts with host E3 ubiquitin-protein ligase UBR4; this
CC interaction is important for viral RNA production (By similarity).
CC Interacts with host LRP1; this interaction facilitates virus entry into
CC the host cell (By similarity). {ECO:0000250|UniProtKB:P09613,
CC ECO:0000250|UniProtKB:P21401, ECO:0000269|PubMed:19193794,
CC ECO:0000269|PubMed:28827346, ECO:0000269|PubMed:29097548}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09613}. Note=Interaction between Glycoprotein N
CC and Glycoprotein C is essential for proper targeting of Glycoprotein C
CC to the Golgi complex, where virion budding occurs.
CC {ECO:0000250|UniProtKB:P09613}.
CC -!- SUBCELLULAR LOCATION: [Isoform NSm protein]: Host mitochondrion outer
CC membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:P09613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=P03518-1; Sequence=Displayed;
CC Name=NSm protein {ECO:0000250|UniProtKB:P21401}; Synonyms=P14;
CC IsoId=P03518-2; Sequence=VSP_057986, VSP_057987;
CC Name=NSm' protein {ECO:0000250|UniProtKB:P21401}; Synonyms=P13;
CC IsoId=P03518-3; Sequence=VSP_057985, VSP_057987;
CC -!- DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C-
CC terminus (By similarity). The cytoplasmic tail specifically interacts
CC with the ribonucleoproteins and is critical for genome packaging (By
CC similarity). {ECO:0000250|UniProtKB:P09613}.
CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins including NSm protein, Glycoprotein C, and
CC Glycoprotein N. {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein N]: Glycosylated (By similarity). The glycans can
CC attach to host CD209/DC-SIGN, and may play a role in virus entry into
CC dendritic cells (By similarity). {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein C]: Glycosylated (By similarity). The glycans can
CC attach to host CD209/DC-SIGN, and may play a role in virus entry into
CC dendritic cells (By similarity). {ECO:0000250|UniProtKB:P21401}.
CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000250|UniProtKB:P09613}.
CC -!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M11157; AAA47450.1; -; Genomic_RNA.
DR PIR; A04110; VGVURV.
DR PDB; 4HJ1; X-ray; 1.90 A; A/B/C/D=691-1119.
DR PDB; 4HJC; X-ray; 4.15 A; A=691-1118.
DR PDB; 5Y0W; X-ray; 2.50 A; A=154-469.
DR PDB; 5Y0Y; X-ray; 3.40 A; A=154-469.
DR PDB; 6EGT; X-ray; 2.50 A; A/B/C=691-1158.
DR PDB; 6EGU; X-ray; 2.30 A; A/B/C=691-1158.
DR PDB; 6F9F; EM; 13.30 A; A/C/E/G/I=154-469.
DR PDB; 6IEA; X-ray; 2.00 A; A=154-469.
DR PDB; 6IEB; X-ray; 2.41 A; A/B=154-469.
DR PDB; 6IEC; X-ray; 3.20 A; A/B/E/I=154-469.
DR PDB; 6IEK; X-ray; 2.70 A; A/D=154-469.
DR PDBsum; 4HJ1; -.
DR PDBsum; 4HJC; -.
DR PDBsum; 5Y0W; -.
DR PDBsum; 5Y0Y; -.
DR PDBsum; 6EGT; -.
DR PDBsum; 6EGU; -.
DR PDBsum; 6F9F; -.
DR PDBsum; 6IEA; -.
DR PDBsum; 6IEB; -.
DR PDBsum; 6IEC; -.
DR PDBsum; 6IEK; -.
DR SMR; P03518; -.
DR ABCD; P03518; 10 sequenced antibodies.
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:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR016404; M_polyprot_prcur_phlebovir.
DR InterPro; IPR043603; Phlebo_G2_C.
DR InterPro; IPR010826; Phlebovirus_G1.
DR InterPro; IPR009878; Phlebovirus_G2_fusion.
DR InterPro; IPR009879; Phlebovirus_NSM.
DR Pfam; PF19019; Phlebo_G2_C; 1.
DR Pfam; PF07243; Phlebovirus_G1; 1.
DR Pfam; PF07245; Phlebovirus_G2; 1.
DR Pfam; PF07246; Phlebovirus_NSM; 2.
DR PIRSF; PIRSF003961; M_poly_PhleboV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; 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 mitochondrion outer membrane;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1206
FT /note="Envelopment polyprotein"
FT /id="PRO_0000247009"
FT CHAIN 17..690
FT /note="NSm-Gn protein"
FT /id="PRO_0000036847"
FT CHAIN 154..690
FT /note="Glycoprotein N"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036848"
FT CHAIN 691..1206
FT /note="Glycoprotein C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036849"
FT TOPO_DOM 17..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..582
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..1159
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1160..1180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1181..1206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 131..153
FT /note="Internal signal sequence for glycoprotein N"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 608..650
FT /note="Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 646..650
FT /note="Important for correct targeting of the glycoproteins
FT to the Golgi complex but not for heterodimerization"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 675..690
FT /note="Internal signal sequence for glycoprotein C"
FT /evidence="ECO:0000250|UniProtKB:P09613"
FT REGION 777..783
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT REGION 819..830
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT SITE 153..154
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT SITE 690..691
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:23319635"
FT CARBOHYD 1035
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:23319635"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 179..188
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 229..239
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 250..281
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 271..284
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 304..456
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 322..332
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 374..434
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 402..413
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 420..425
FT /evidence="ECO:0000269|PubMed:28827346"
FT DISULFID 479..482
FT /evidence="ECO:0000303|PubMed:28827346"
FT DISULFID 486..556
FT /evidence="ECO:0000303|PubMed:28827346"
FT DISULFID 506..511
FT /evidence="ECO:0000303|PubMed:28827346"
FT DISULFID 691..731
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 704..713
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 756..852
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 771..965
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 777..825
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 783..832
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 788..814
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 818..823
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 934..947
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1029..1101
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1039..1042
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 1049..1083
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform NSm' protein)"
FT /id="VSP_057985"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform NSm protein)"
FT /id="VSP_057986"
FT VAR_SEQ 154..1197
FT /note="Missing (in isoform NSm protein and isoform NSm'
FT protein)"
FT /id="VSP_057987"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:6IEB"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5Y0Y"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6IEA"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6IEA"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6IEA"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:6IEB"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:6IEA"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:6IEA"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:6IEA"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5Y0W"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 336..347
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:6IEA"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5Y0W"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6IEB"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6IEA"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:6IEA"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 455..467
FT /evidence="ECO:0007829|PDB:6IEA"
FT STRAND 691..696
FT /evidence="ECO:0007829|PDB:4HJ1"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 702..709
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 711..722
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 728..735
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 742..764
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 767..776
FT /evidence="ECO:0007829|PDB:4HJ1"
FT TURN 785..790
FT /evidence="ECO:0007829|PDB:4HJ1"
FT HELIX 798..803
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 810..817
FT /evidence="ECO:0007829|PDB:4HJ1"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 826..829
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 831..844
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 847..864
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 870..875
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 880..883
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 886..893
FT /evidence="ECO:0007829|PDB:4HJ1"
FT HELIX 900..902
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 904..908
FT /evidence="ECO:0007829|PDB:4HJ1"
FT TURN 909..911
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 912..918
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 931..936
FT /evidence="ECO:0007829|PDB:4HJ1"
FT HELIX 937..941
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 947..949
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 954..959
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 962..967
FT /evidence="ECO:0007829|PDB:4HJ1"
FT HELIX 972..978
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 980..985
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 988..992
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 994..996
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 999..1003
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1009..1021
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1030..1044
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1046..1056
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1058..1064
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1070..1075
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1077..1086
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1089..1103
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1106..1113
FT /evidence="ECO:0007829|PDB:4HJ1"
FT STRAND 1123..1129
FT /evidence="ECO:0007829|PDB:6EGU"
SQ SEQUENCE 1206 AA; 132053 MW; D2E8017179285924 CRC64;
MYVLLTILIS VLVCEAVIRV SLSSTREETC FGDSTNPEMI EGAWDSLREE EMPEELSCSI
SGIREVKTSS QELYRALKAI IAADGLNNIT CHGKDPEDKI SLIKGPPHKK RVGIVRCERR
RDAKQIGRET MAGIAMTVLP ALAVFALAPV VFAEDPHLRN RPGKGHNYID GMTQEDATCK
PVTYAGACSS FDVLLEKGKF PLFQSYAHHR TLLEAVHDTI IAKADPPSCD LQSAHGNPCM
KEKLVMKTHC PNDYQSAHYL NNDGKMASVK CPPKYGLTED CNFCRQMTGA SLKKGSYPLQ
DLFCQSSEDD GSKLKTKMKG VCEVGVQAHK KCDGQLSTAH EVVPFAVFKN SKKVYLDKLD
LKTEENLLPD SFVCFEHKGQ YKGTMDSGQT KRELKSFDIS QCPKIGGHGS KKCTGDAAFC
SAYECTAQYA NAYCSHANGS GIVQIQVSGV WKKPLCVGYE RVVVKRELSA KPIQRVEPCT
TCITKCEPHG LVVRSTGFKI SSAVACASGV CVTGSQSPST EITLKYPGIS QSSGGDIGVH
MAHDDQSVSS KIVAHCPPQD PCLVHGCIVC AHGLINYQCH TALSAFVVVF VFSSIAIICL
AVLYRVLKCL KIAPRKVLNP LMWITAFIRW IYKKMVARVA HNINQVNREI GWMEGGQLVL
GNPAPIPRHA PIPRYSTYLM LLLIVSYASA CSELIQASSR ITTCSTEGVN TKCRLSGTAL
IRAGSVGAEA CLMLKGVKED QTKFLKIKTV SSELSCREGQ SYWTGSISPK CLSSRRCHLV
GECHVNRCLS WRDNETSAEF SFVGESTTMR ENKCFEQCGG WGCGCFNVNP SCLFVHTYLQ
SVRKEALRVF NCIDWVHKLT LEITDFDGSV STIDLGASSS RFTNWGSVSL SLDAEGISGS
NSFSFIESPS KGYAIVDEPF SEIPRQGFLG EIRCNSESSV LSAHESCLRA PNLISYKPMI
DQLECTTNLI DPFVVFERGS LPQTRNDKTF AASKGNRGVQ AFSKGSVQAD LTLMFDNFEV
DFVGAAVSCD AAFLNLTGCY SCNAGARVCL SITSTGTGSL SAHNKDGSLH IVLPSENGTK
DQCQILHFTV PEVEEEFMYS CDGDERPLLV KGTLIAIDPF DDRREAGGES TVVNPKSGSW
NFFDWFSGLM SWFGGPLKLY SSFACMLHYQ LGSFSSLYIL EEQASLKCGL LPLRRPHRSV
RVKVIC
