GLYC_LASSJ
ID GLYC_LASSJ Reviewed; 491 AA.
AC P08669;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Pre-glycoprotein polyprotein GP complex {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=Pre-GP-C {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Stable signal peptide {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=SSP {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Glycoprotein G1 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=GP1 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Glycoprotein G2 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=GP2 {ECO:0000255|HAMAP-Rule:MF_04084};
GN Name=GPC {ECO:0000255|HAMAP-Rule:MF_04084}; Synonyms=GP-C;
OS Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11622;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10112; Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2916333; DOI=10.1016/0042-6822(89)90287-0;
RA Auperin D.D., McCormick J.B.;
RT "Nucleotide sequence of the Lassa virus (Josiah strain) S genome RNA and
RT amino acid sequence comparison of the N and GPC proteins to other
RT arenaviruses.";
RL Virology 168:421-425(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3750844; DOI=10.1016/0042-6822(86)90438-1;
RA Auperin D.D., Sasso D.R., McCormick J.B.;
RT "Nucleotide sequence of the glycoprotein gene and intergenic region of the
RT Lassa virus S genome RNA.";
RL Virology 154:155-167(1986).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN BY HOST MBTPS1.
RX PubMed=11606739; DOI=10.1073/pnas.221447598;
RA Lenz O., ter Meulen J., Klenk H.D., Seidah N.G., Garten W.;
RT "The Lassa virus glycoprotein precursor GP-C is proteolytically processed
RT by subtilase SKI-1/S1P.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12701-12705(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST DAG1.
RX PubMed=11967329; DOI=10.1128/jvi.76.10.5140-5146.2002;
RA Spiropoulou C.F., Kunz S., Rollin P.E., Campbell K.P., Oldstone M.B.;
RT "New World arenavirus clade C, but not clade A and B viruses, utilizes
RT alpha-dystroglycan as its major receptor.";
RL J. Virol. 76:5140-5146(2002).
RN [5]
RP MUTAGENESIS OF GLY-54; SER-56; THR-58 AND SER-60.
RX PubMed=12633879; DOI=10.1016/s0014-5793(03)00160-1;
RA Eichler R., Lenz O., Strecker T., Garten W.;
RT "Signal peptide of Lassa virus glycoprotein GP-C exhibits an unusual
RT length.";
RL FEBS Lett. 538:203-206(2003).
RN [6]
RP FUNCTION OF STABLE SIGNAL PEPTIDE, AND SUBUNIT.
RX PubMed=14555961; DOI=10.1038/sj.embor.embor7400002;
RA Eichler R., Lenz O., Strecker T., Eickmann M., Klenk H.D., Garten W.;
RT "Identification of Lassa virus glycoprotein signal peptide as a trans-
RT acting maturation factor.";
RL EMBO Rep. 4:1084-1088(2003).
RN [7]
RP TOPOLOGY OF STABLE SIGNAL PEPTIDE.
RX PubMed=14709548; DOI=10.1074/jbc.m312975200;
RA Eichler R., Lenz O., Strecker T., Eickmann M., Klenk H.D., Garten W.;
RT "Lassa virus glycoprotein signal peptide displays a novel topology with an
RT extended endoplasmic reticulum luminal region.";
RL J. Biol. Chem. 279:12293-12299(2004).
RN [8]
RP FUNCTION.
RX PubMed=17761532; DOI=10.1091/mbc.e07-04-0374;
RA Rojek J.M., Campbell K.P., Oldstone M.B., Kunz S.;
RT "Old World arenavirus infection interferes with the expression of
RT functional alpha-dystroglycan in the host cell.";
RL Mol. Biol. Cell 18:4493-4507(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH HOST LAMP1.
RX PubMed=24970085; DOI=10.1126/science.1252480;
RA Jae L.T., Raaben M., Herbert A.S., Kuehne A.I., Wirchnianski A.S.,
RA Soh T.K., Stubbs S.H., Janssen H., Damme M., Saftig P., Whelan S.P.,
RA Dye J.M., Brummelkamp T.R.;
RT "Virus entry. Lassa virus entry requires a trigger-induced receptor
RT switch.";
RL Science 344:1506-1510(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 75-237, INTERACTION WITH HOST
RP LAMP1, GLYCOSYLATION AT ASN-109; ASN-119; ASN-167 AND ASN-224, AND
RP DISULFIDE BONDS.
RX PubMed=25972533; DOI=10.1128/jvi.00651-15;
RA Cohen-Dvashi H., Cohen N., Israeli H., Diskin R.;
RT "Molecular Mechanism for LAMP1 Recognition by Lassa Virus.";
RL J. Virol. 89:7584-7592(2015).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (16.40 ANGSTROMS) OF 75-237, GLYCOSYLATION
RP AT ASN-109; ASN-119; ASN-167 AND ASN-224, AND DISULFIDE BONDS.
RX PubMed=26849049; DOI=10.1371/journal.ppat.1005418;
RA Li S., Sun Z., Pryce R., Parsy M.L., Fehling S.K., Schlie K., Siebert C.A.,
RA Garten W., Bowden T.A., Strecker T., Huiskonen J.T.;
RT "Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus
RT Glycoprotein Spike.";
RL PLoS Pathog. 12:E1005418-E1005418(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-259, GLYCOSYLATION AT ASN-79;
RP ASN-89; ASN-99; ASN-109; ASN-119; ASN-167; ASN-224; ASN-365; ASN-373;
RP ASN-390 AND ASN-395, AND DISULFIDE BONDS.
RX PubMed=28572385; DOI=10.1126/science.aam7260;
RA Hastie K.M., Zandonatti M.A., Kleinfelter L.M., Heinrich M.L.,
RA Rowland M.M., Chandran K., Branco L.M., Robinson J.E., Garry R.F.,
RA Saphire E.O.;
RT "Structural basis for antibody-mediated neutralization of Lassa virus.";
RL Science 356:923-928(2017).
CC -!- FUNCTION: [Glycoprotein G1]: Interacts with the host receptor (By
CC similarity). Mediates virus attachment to host receptor alpha-
CC dystroglycan DAG1. This attachment induces virion internalization
CC predominantly through clathrin- and caveolin-independent endocytosis
CC (PubMed:11967329). {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:11967329}.
CC -!- FUNCTION: [Glycoprotein G2]: Class I viral fusion protein that directs
CC fusion of viral and host endosomal membranes, leading to delivery of
CC the nucleocapsid into the cytoplasm. Membrane fusion is mediated by
CC irreversible conformational changes induced upon acidification in the
CC endosome. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- FUNCTION: Stable signal peptide (SSP): cleaved and functions as a
CC signal peptide. In addition, it is also retained as the third component
CC of the GP complex. The SSP is required for efficient glycoprotein
CC expression, post-translational maturation cleavage of GP1 and GP2,
CC glycoprotein transport to the cell surface plasma membrane, formation
CC of infectious virus particles, and acid pH-dependent glycoprotein-
CC mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:24970085}.
CC -!- SUBUNIT: [Glycoprotein G1]: Homotetramer; disulfide-linked (By
CC similarity). Interacts with host DAG1 (PubMed:11967329).
CC {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:11967329}.
CC -!- SUBUNIT: [Glycoprotein G2]: Homotetramer. GP2 homotetramers bind
CC through ionic interactions with GP1 homotetramers to form the GP
CC complex together with the stable signal peptide. The GP-C polyprotein
CC interacts with the host protease MBTPS1/SKI-1 resulting in the
CC polyprotein processing. {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:14555961, ECO:0000269|PubMed:24970085,
CC ECO:0000269|PubMed:25972533}.
CC -!- INTERACTION:
CC P08669; P11279: LAMP1; Xeno; NbExp=4; IntAct=EBI-8411266, EBI-2805407;
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal
CC peptide masks endogenous ER localization signals in the cytoplasmic
CC domain of G2 to ensure that only the fully assembled, tripartite GP
CC complex is transported for virion assembly. {ECO:0000255|HAMAP-
CC Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- DOMAIN: The cytoplasmic domain of GP2 plays a role in ER location. It
CC also contains a zinc-binding domain that allows SSP retention in the
CC GPC complex by accepting a cysteine from SSP as the fourth ligand.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C
CC polyprotein is cleaved in the endoplasmic reticulum by the host
CC protease MBTPS1. Only cleaved glycoprotein is incorporated into
CC virions. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- PTM: The SSP remains stably associated with the GP complex following
CC cleavage by signal peptidase and plays crucial roles in the trafficking
CC of GP through the secretory pathway. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SIMILARITY: Belongs to the arenaviridae GPC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
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DR EMBL; M15076; AAA46283.1; -; Genomic_RNA.
DR EMBL; J04324; AAA46286.1; -; Genomic_RNA.
DR PIR; A24296; VGXPLV.
DR RefSeq; NP_694870.1; NC_004296.1.
DR PDB; 4ZJF; X-ray; 2.60 A; A/B/C/D=75-237.
DR PDB; 5FT2; EM; 16.40 A; B=75-237.
DR PDB; 5OMI; X-ray; 2.56 A; A/B/C=306-419.
DR PDB; 5VK2; X-ray; 3.20 A; A/B/C=1-259, a/b/c=260-423.
DR PDB; 6JGY; X-ray; 3.39 A; A=306-432.
DR PDBsum; 4ZJF; -.
DR PDBsum; 5FT2; -.
DR PDBsum; 5OMI; -.
DR PDBsum; 5VK2; -.
DR PDBsum; 6JGY; -.
DR SMR; P08669; -.
DR IntAct; P08669; 5.
DR MINT; P08669; -.
DR iPTMnet; P08669; -.
DR GeneID; 956585; -.
DR KEGG; vg:956585; -.
DR Proteomes; UP000002473; 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:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.20.28.180; -; 1.
DR HAMAP; MF_04084; ARENA_GPC; 1.
DR InterPro; IPR001535; Arena_glycoprot.
DR InterPro; IPR043015; Arena_glycoprot_zinc-bd.
DR Pfam; PF00798; Arena_glycoprot; 1.
DR PIRSF; PIRSF004028; GPC_ArenaV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endoplasmic reticulum; Host Golgi apparatus;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CHAIN 2..491
FT /note="Pre-glycoprotein polyprotein GP complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353854"
FT CHAIN 2..58
FT /note="Stable signal peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353855"
FT CHAIN 59..259
FT /note="Glycoprotein G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036601"
FT CHAIN 260..491
FT /note="Glycoprotein G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036602"
FT TOPO_DOM 2..17
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 18..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 54..58
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 59..432
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 454..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 58..59
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 259..260
FT /note="Cleavage; by host MBTPS1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT DISULFID 86..231
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT DISULFID 118..155
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT DISULFID 180..212
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:25972533, ECO:0000269|PubMed:26849049,
FT ECO:0000269|PubMed:28572385"
FT DISULFID 279..292
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT DISULFID 301..310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT DISULFID 364..385
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:28572385"
FT MUTAGEN 54
FT /note="G->A: No effect on SSP cleavage."
FT /evidence="ECO:0000269|PubMed:12633879"
FT MUTAGEN 56
FT /note="S->A: Complete loss of SSP cleavage."
FT /evidence="ECO:0000269|PubMed:12633879"
FT MUTAGEN 58
FT /note="T->A: Complete loss of SSP cleavage."
FT /evidence="ECO:0000269|PubMed:12633879"
FT MUTAGEN 60
FT /note="S->A: No effect on SSP cleavage."
FT /evidence="ECO:0000269|PubMed:12633879"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5VK2"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:5VK2"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5VK2"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5VK2"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:4ZJF"
FT HELIX 123..139
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4ZJF"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:4ZJF"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4ZJF"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:4ZJF"
FT TURN 227..231
FT /evidence="ECO:0007829|PDB:4ZJF"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:5VK2"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:5VK2"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5VK2"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:5VK2"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5VK2"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:5VK2"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:5VK2"
FT HELIX 306..354
FT /evidence="ECO:0007829|PDB:5OMI"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:5OMI"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:5OMI"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5VK2"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:5OMI"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5VK2"
FT HELIX 402..417
FT /evidence="ECO:0007829|PDB:5OMI"
SQ SEQUENCE 491 AA; 55813 MW; A291367FC5BC70C8 CRC64;
MGQIVTFFQE VPHVIEEVMN IVLIALSVLA VLKGLYNFAT CGLVGLVTFL LLCGRSCTTS
LYKGVYELQT LELNMETLNM TMPLSCTKNN SHHYIMVGNE TGLELTLTNT SIINHKFCNL
SDAHKKNLYD HALMSIISTF HLSIPNFNQY EAMSCDFNGG KISVQYNLSH SYAGDAANHC
GTVANGVLQT FMRMAWGGSY IALDSGRGNW DCIMTSYQYL IIQNTTWEDH CQFSRPSPIG
YLGLLSQRTR DIYISRRLLG TFTWTLSDSE GKDTPGGYCL TRWMLIEAEL KCFGNTAVAK
CNEKHDEEFC DMLRLFDFNK QAIQRLKAEA QMSIQLINKA VNALINDQLI MKNHLRDIMG
IPYCNYSKYW YLNHTTTGRT SLPKCWLVSN GSYLNETHFS DDIEQQADNM ITEMLQKEYM
ERQGKTPLGL VDLFVFSTSF YLISIFLHLV KIPTHRHIVG KSCPKPHRLN HMGICSCGLY
KQPGVPVKWK R
