GLYC_JUNIN
ID GLYC_JUNIN Reviewed; 485 AA.
AC P26313;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 106.
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 Junin mammarenavirus (JUNV) (Junn mammarenavirus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=2169991;
OH NCBI_TaxID=29095; Akodon azarae (Azara's grass mouse).
OH NCBI_TaxID=10080; Bolomys.
OH NCBI_TaxID=56211; Calomys laucha (Small vesper mouse).
OH NCBI_TaxID=56212; Calomys musculinus (Drylands vesper mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MC2;
RX PubMed=1654373; DOI=10.1099/0022-1317-72-9-2129;
RA Ghiringhelli P.D., Rivera-Pomar R.V., Lozano M.E., Grau O., Romanowski V.;
RT "Molecular organization of Junin virus S RNA: complete nucleotide sequence,
RT relationship with other members of the Arenaviridae and unusual secondary
RT structures.";
RL J. Gen. Virol. 72:2129-2141(1991).
RN [2]
RP SEQUENCE REVISION TO 43-51; 58-80 AND 143.
RA Romanowski V.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=15367645; DOI=10.1128/jvi.78.19.10783-10792.2004;
RA York J., Romanowski V., Lu M., Nunberg J.H.;
RT "The signal peptide of the Junin arenavirus envelope glycoprotein is
RT myristoylated and forms an essential subunit of the mature G1-G2 complex.";
RL J. Virol. 78:10783-10792(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 476-LYS-LYS-477 AND
RP 482-ARG-ARG-483.
RX PubMed=16698999; DOI=10.1128/jvi.00208-06;
RA Agnihothram S.S., York J., Nunberg J.H.;
RT "Role of the stable signal peptide and cytoplasmic domain of G2 in
RT regulating intracellular transport of the Junin virus envelope glycoprotein
RT complex.";
RL J. Virol. 80:5189-5198(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST TFRC.
RX PubMed=17287727; DOI=10.1038/nature05539;
RA Radoshitzky S.R., Abraham J., Spiropoulou C.F., Kuhn J.H., Nguyen D.,
RA Li W., Nagel J., Schmidt P.J., Nunberg J.H., Andrews N.C., Farzan M.,
RA Choe H.;
RT "Transferrin receptor 1 is a cellular receptor for New World haemorrhagic
RT fever arenaviruses.";
RL Nature 446:92-96(2007).
RN [6]
RP CLEAVAGE BY HOST MBTPS1/SKI-1.
RX PubMed=18400865; DOI=10.1128/jvi.02392-07;
RA Rojek J.M., Lee A.M., Nguyen N., Spiropoulou C.F., Kunz S.;
RT "Site 1 protease is required for proteolytic processing of the
RT glycoproteins of the South American hemorrhagic fever viruses Junin,
RT Machupo, and Guanarito.";
RL J. Virol. 82:6045-6051(2008).
RN [7]
RP FUNCTION.
RX PubMed=19548229; DOI=10.1002/biot.200800357;
RA Martinez M.G., Forlenza M.B., Candurra N.A.;
RT "Involvement of cellular proteins in Junin arenavirus entry.";
RL Biotechnol. J. 4:866-870(2009).
RN [8]
RP STRUCTURE BY NMR OF 445-485 IN COMPLEX WITH ZINC, AND DOMAIN.
RX PubMed=21068387; DOI=10.1074/jbc.m110.166025;
RA Briknarova K., Thomas C.J., York J., Nunberg J.H.;
RT "Structure of a zinc-binding domain in the Junin virus envelope
RT glycoprotein.";
RL J. Biol. Chem. 286:1528-1536(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 87-227, GLYCOSYLATION AT ASN-105;
RP ASN-166 AND ASN-178, AND DISULFIDE BOND.
RX PubMed=26651946; DOI=10.1016/j.chom.2015.11.005;
RA Mahmutovic S., Clark L., Levis S.C., Briggiler A.M., Enria D.A.,
RA Harrison S.C., Abraham J.;
RT "Molecular Basis for Antibody-Mediated Neutralization of New World
RT Hemorrhagic Fever Mammarenaviruses.";
RL Cell Host Microbe 18:705-713(2015).
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 -!- FUNCTION: [Glycoprotein G1]: Interacts with the host receptor (By
CC similarity). Mediates virus attachment to host TFRC. This attachment
CC induces virion internalization predominantly through clathrin-mediated
CC endocytosis (PubMed:17287727). {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:19548229}.
CC -!- SUBUNIT: [Glycoprotein G1]: Homotetramer; disulfide-linked (By
CC similarity). Interacts with host TFRC (PubMed:17287727).
CC {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:17287727}.
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:18400865}.
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 'Cys-57' from SSP as the fourth ligand.
CC {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387}.
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 ECO:0000269|PubMed:18400865}.
CC -!- SIMILARITY: Belongs to the arenaviridae GPC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
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DR EMBL; D10072; BAA00964.2; -; Genomic_RNA.
DR PIR; JT0978; VGXPJV.
DR PDB; 2L0Z; NMR; -; A=445-485.
DR PDB; 5EN2; X-ray; 1.82 A; C=87-227.
DR PDB; 5W1K; X-ray; 3.99 A; E/J/P/R=87-228.
DR PDBsum; 2L0Z; -.
DR PDBsum; 5EN2; -.
DR PDBsum; 5W1K; -.
DR SMR; P26313; -.
DR TCDB; 1.G.8.1.2; the arenavirus fusion protein (av-fp) family.
DR iPTMnet; P26313; -.
DR ABCD; P26313; 5 sequenced antibodies.
DR EvolutionaryTrace; P26313; -.
DR Proteomes; UP000127886; 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; 2.
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; Transmembrane; Transmembrane helix;
KW 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 ECO:0000269|PubMed:15367645"
FT CHAIN 2..485
FT /note="Pre-glycoprotein polyprotein GP complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353850"
FT CHAIN 2..58
FT /note="Stable signal peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000353851"
FT CHAIN 59..251
FT /note="Glycoprotein G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036597"
FT CHAIN 252..485
FT /note="Glycoprotein G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036598"
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..424
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 446..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT REGION 476..477
FT /note="Involved in ER localization"
FT REGION 482..483
FT /note="Involved in ER localization"
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 ECO:0000269|PubMed:21068387"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:21068387"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:21068387"
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 ECO:0000269|PubMed:21068387"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:21068387"
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 ECO:0000269|PubMed:21068387"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:21068387"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:21068387"
FT SITE 58..59
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 251..252
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 ECO:0000269|PubMed:15367645"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:26651946"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:26651946"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:26651946"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 92..226
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:26651946"
FT DISULFID 135..164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:26651946"
FT DISULFID 207..213
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084,
FT ECO:0000269|PubMed:26651946"
FT DISULFID 271..284
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 293..302
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 356..377
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT MUTAGEN 2
FT /note="G->A: Reduces membrane fusion activity. No effect on
FT GP complex formation."
FT /evidence="ECO:0000269|PubMed:15367645"
FT MUTAGEN 476..477
FT /note="KK->AA: Induces transport to the cell surface in the
FT absence of SSP. No effect on SSP binding."
FT /evidence="ECO:0000269|PubMed:16698999"
FT MUTAGEN 482..483
FT /note="RR->AA: Induces transport to the cell surface in the
FT absence of SSP. No effect on SSP binding."
FT /evidence="ECO:0000269|PubMed:16698999"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:5EN2"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:5EN2"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:5EN2"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:5EN2"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:5EN2"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:5EN2"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5EN2"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:5EN2"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:2L0Z"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:2L0Z"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:2L0Z"
FT TURN 468..471
FT /evidence="ECO:0007829|PDB:2L0Z"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2L0Z"
SQ SEQUENCE 485 AA; 55607 MW; EE57D860FDD17F05 CRC64;
MGQFISFMQE IPTFLQEALN IALVAVSLIA IIKGVVNLYK SGLFQFFVFL ALAGRSCTEE
AFKIGLHTEF QTVSFSMVGL FSNNPHDLPL LCTLNKSHLY IKGGNASFKI SFDDIAVLLP
EYDVIIQHPA DMSWCSKSDD QIWLSQWFMN AVGHDWYLDP PFLCRNRTKT EGFIFQVNTS
KTGINENYAK KFKTGMHHLY REYPDSCLDG KLCLMKAQPT SWPLQCPLDH VNTLHFLTRG
KNIQLPRRSL KAFFSWSLTD SSGKDTPGGY CLEEWMLVAA KMKCFGNTAV AKCNLNHDSE
FCDMLRLFDY NKNAIKTLND ETKKQVNLMG QTINALISDN LLMKNKIREL MSVPYCNYTK
FWYVNHTLSG QHSLPRCWLI KNNSYLNISD FRNDWILESD FLISEMLSKE YSDRQGKTPL
TLVDICFWST VFFTASLFLH LVGIPTHRHI RGEACPLPHR LNSLGGCRCG KYPNLKKPTV
WRRGH
