GP_NYV
ID GP_NYV Reviewed; 1140 AA.
AC Q83887; Q83886; Q83888;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Envelopment polyprotein;
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;
OS New York virus (NYV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus; unclassified Orthohantavirus.
OX NCBI_TaxID=44755;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10041; Peromyscus leucopus (White-footed mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate New York-1, Isolate New York-2, and Isolate Rhode Island-1;
RX PubMed=7494337; DOI=10.1128/jvi.69.12.8137-8141.1995;
RA Hjelle B., Lee S.-W., Song W., Torrez-Martinez N., Song J.-W.,
RA Yanagihara R., Gavrilovskaya I.N., Mackow E.R.;
RT "Molecular linkage of hantavirus pulmonary syndrome to the white-footed
RT mouse, Peromyscus leucopus: genetic characterization of the M genome of New
RT York virus.";
RL J. Virol. 69:8137-8141(1995).
RN [2]
RP INTERACTION WITH HUMAN LYN; HUMAN SYK AND HUMAN ZAP70.
RX PubMed=12502882; DOI=10.1128/jvi.77.2.1638-1643.2003;
RA Geimonen E., LaMonica R., Springer K., Farooqui Y., Gavrilovskaya I.N.,
RA Mackow E.R.;
RT "Hantavirus pulmonary syndrome-associated hantaviruses contain conserved
RT and functional ITAM signaling elements.";
RL J. Virol. 77:1638-1643(2003).
RN [3]
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 [4]
RP FUNCTION (GLYCOPROTEIN N), AND DOMAIN (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 [5]
RP FUNCTION (GLYCOPROTEIN N), INTERACTION WITH HOST TRAF3 (GLYCOPROTEIN N),
RP AND DOMAIN (GLYCOPROTEIN N).
RX PubMed=18614628; DOI=10.1128/jvi.00290-08;
RA Alff P.J., Sen N., Gorbunova E., Gavrilovskaya I.N., Mackow E.R.;
RT "The NY-1 hantavirus Gn cytoplasmic tail coprecipitates TRAF3 and inhibits
RT cellular interferon responses by disrupting TBK1-TRAF3 complex formation.";
RL J. Virol. 82:9115-9122(2008).
RN [6]
RP FUNCTION (GLYCOPROTEIN N), MUTAGENESIS OF TYR-619; TYR-627; SER-629;
RP ARG-630 AND TYR-632, INTERACTION WITH HOST TRAF3 (GLYCOPROTEIN N), AND
RP DOMAIN (GLYCOPROTEIN 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 [7]
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).
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 (PubMed:15657120). This
CC attachment induces virion internalization predominantly through
CC clathrin-dependent endocytosis (By similarity). Mediates the assembly
CC and budding of infectious virus particles through its interaction with
CC the nucleocapsid protein and the viral genome (By similarity). May
CC dysregulate normal immune and endothelial cell responses through an
CC ITAM motif. Translocates to mitochondria, binds to host TUFM and
CC recruits MAP1LC3B (By similarity). These interactions induce
CC mitochondrial autophagy and therefore destruction of host MAVS leading
CC to inhibition of type I interferon (IFN) responses (By similarity).
CC Concomitant breakdown of glycoprotein N is apparently prevented by the
CC nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome
CC fusion (By similarity). Interacts with the viral genomic RNA (By
CC similarity). Inhibits the host RIG-I/TBK1 pathway by disrupting the
CC formation of TBK1-TRAF3 complexes and downstream signaling responses
CC required for IFN-beta transcription (PubMed:16973572, PubMed:24390324,
CC PubMed:18614628). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312, ECO:0000269|PubMed:15657120,
CC ECO:0000269|PubMed:16973572, ECO:0000269|PubMed:18614628,
CC ECO:0000269|PubMed:24390324}.
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 (PubMed:15657120). This attachment
CC induces virion internalization predominantly through clathrin-dependent
CC endocytosis. Class II fusion protein that promotes fusion of viral
CC membrane with host endosomal membrane after endocytosis of the virion
CC (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000269|PubMed:15657120}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer (By similarity). Homotetramer;
CC forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By
CC similarity). Interacts (via C-terminus) with the nucleoprotein (By
CC similarity). Interacts with host TUFM; this interaction contributes to
CC the virus-induced degradation of mitochondria by autophagy, which leads
CC to degradation of host MAVS and inhibition of type I interferon (IFN)
CC 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 (via N-terminus); this
CC interaction inhibits the formation of TRAF3-TBK1 complexes
CC (PubMed:24390324, PubMed:18614628). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P0DTJ1, ECO:0000269|PubMed:18614628,
CC ECO:0000269|PubMed:24390324}.
CC -!- SUBUNIT: [Glycoprotein C]: Homodimer. Homotetramer; forms
CC heterotetrameric Gn-Gc spikes in the pre-fusion conformation.
CC Homotrimer; forms homotrimer in the post-fusion conformation at acidic
CC pH (By similarity). Interacts (via C-terminus) with the nucleoprotein
CC (By similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312}.
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, PubMed:24390324, PubMed:18614628). The C-terminus of
CC the cytoplasmic tail is involved in binding to the viral genome and the
CC nucleocapsid (By similarity). Contains 2 contiguous zinc-fingers (By
CC similarity). {ECO:0000250|UniProtKB:P08668,
CC ECO:0000250|UniProtKB:P27312, ECO:0000250|UniProtKB:Q9E006,
CC ECO:0000269|PubMed:16973572, ECO:0000269|PubMed:18614628,
CC ECO:0000269|PubMed:24390324}.
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}.
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DR EMBL; U36802; AAC54560.1; -; Genomic_RNA.
DR EMBL; U36801; AAC54559.1; -; Genomic_RNA.
DR EMBL; U36803; AAC54561.1; -; Genomic_RNA.
DR SMR; Q83887; -.
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: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-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; 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 Disulfide bond; 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 RLR pathway by virus; Inhibition of host TRAFs by virus;
KW Membrane; Metal-binding; Phosphoprotein; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW Zinc; Zinc-finger.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1140
FT /note="Envelopment polyprotein"
FT /id="PRO_0000235995"
FT CHAIN 18..652
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000235996"
FT CHAIN 653..1140
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000235997"
FT TOPO_DOM 18..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..1108
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1130..1140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 615..638
FT /note="ITAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT ZN_FING 549..569
FT /note="CCHC-type 1"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT ZN_FING 574..595
FT /note="CCHC-type 2"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 520..537
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 592..609
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 596..607
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT REGION 611..638
FT /note="Interaction with host TRAF3"
FT /evidence="ECO:0000269|PubMed:24390324"
FT REGION 615..629
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT REGION 761..781
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P41266"
FT REGION 1125..1140
FT /note="Binding to the ribonucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P27312"
FT MOTIF 619..622
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT SITE 652..653
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT MOD_RES 619
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT MOD_RES 632
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 30..155
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 64..161
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 113..132
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 137..142
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 179..189
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 214..251
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 380..439
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 384..393
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 409..428
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 456..479
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT DISULFID 739..774
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 743..781
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 755..888
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 769..899
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 784..907
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 810..819
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 827..836
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 867..871
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 973..1003
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 996..1048
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1013..1018
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1049..1054
FT /evidence="ECO:0000250|UniProtKB:P08668"
FT DISULFID 1088..1092
FT /evidence="ECO:0000250|UniProtKB:Q9E006"
FT VARIANT 4
FT /note="W -> F (in strain: Isolate New York-2)"
FT VARIANT 8
FT /note="S -> F (in strain: Isolate New York-2 and Isolate
FT Rhode Island-1)"
FT VARIANT 46
FT /note="E -> G (in strain: Isolate New York-2)"
FT VARIANT 141
FT /note="H -> Y (in strain: Isolate Rhode Island-1)"
FT VARIANT 238
FT /note="S -> G (in strain: Isolate New York-2)"
FT VARIANT 261
FT /note="F -> S (in strain: Isolate Rhode Island-1)"
FT VARIANT 314
FT /note="T -> A (in strain: Isolate New York-2)"
FT VARIANT 325
FT /note="M -> T (in strain: Isolate Rhode Island-1)"
FT VARIANT 359
FT /note="T -> A (in strain: Isolate Rhode Island-1)"
FT VARIANT 394
FT /note="E -> K (in strain: Isolate Rhode Island-1)"
FT VARIANT 452
FT /note="V -> I (in strain: Isolate Rhode Island-1)"
FT VARIANT 489
FT /note="T -> A (in strain: Isolate Rhode Island-1)"
FT VARIANT 551
FT /note="V -> A (in strain: Isolate Rhode Island-1)"
FT VARIANT 589
FT /note="Q -> L (in strain: Isolate Rhode Island-1)"
FT VARIANT 618
FT /note="C -> R (in strain: Isolate Rhode Island-1)"
FT VARIANT 697
FT /note="N -> D (in strain: Isolate New York-2)"
FT VARIANT 794
FT /note="V -> G (in strain: Isolate Rhode Island-1)"
FT VARIANT 1043
FT /note="G -> S (in strain: Isolate Rhode Island-1)"
FT MUTAGEN 619
FT /note="Y->F: No effect on the regulation of RIG-I-directed
FT IRF3 activation."
FT /evidence="ECO:0000269|PubMed:24390324"
FT MUTAGEN 627
FT /note="Y->A,F,S: Complete loss of Gn-dependent regulation
FT of RIG-I-directed IRF3 activation."
FT /evidence="ECO:0000269|PubMed:24390324"
FT MUTAGEN 629
FT /note="S->A: No effect on the regulation of RIG-I-directed
FT IRF3 activation."
FT /evidence="ECO:0000269|PubMed:24390324"
FT MUTAGEN 630
FT /note="R->A: No effect on the regulation of RIG-I-directed
FT IRF3 activation."
FT /evidence="ECO:0000269|PubMed:24390324"
FT MUTAGEN 632
FT /note="Y->F: No effect on the regulation of RIG-I-directed
FT IRF3 activation."
FT /evidence="ECO:0000269|PubMed:24390324"
SQ SEQUENCE 1140 AA; 125619 MW; BD3CCFDB0417AC42 CRC64;
MVGWVCISLV VLATTTAGLT RNLYELKIEC PHTVGLGQGY VTGSVETTPI LLTQVTDLKI
ESSCNFDLHV PSTSIQKYNQ VEWAKKSSTT ESTSAGATTF EAKTKEVSLK GTCNIPVTTF
EAAYKSRKTV ICYDLACNQT HCLPTVHLIA PVQTCMSVRS CMIGLLSSRI QVIYEKTYCV
TGQLVEGLCF IPTHTIALTQ PGHTYDTMTL PITCFLVAKK LGTQLKIAVE LEKLITASGC
TENSFQGYYI CFLGKHSEPL FVPMMDDYRS AELFTRMVLN PRGEDHDPDQ NGQGLMRIAG
PITAKVPSTE TTETMQGIAF AGAPMYSSFS TLVRKADPDY VFSPGIIAES NHSVCDKKTI
PLTWTGFLAV SGEIEKITGC TVFCTLVGPG ASCEAYSETG IFNISSPTCL VNKVQKFRGS
EQRINFMCQR VDQDVIVYCN GQKKVILTKT LVIGQCIYTF TSLFSLIPGV AHSLAVELCV
PGLHGWATTA LLITFCFGWL LIPTITMIIL KILRLLTFSC SHYSTESKFK AILERVKVEY
QKTMGSMVCD VCHHECETAK ELETHKKSCP EGQCPYCMTM TESTESALQA HFSICKLTNR
FQENLKKSLK RPEVKQGCYR TLGVFRYKSR CYVGLVWGVL LTTELIVWAA SADTPLMESG
WSDTAHGVGI VPMKTDLELD FALASSSSYS YRRKLVNPAN KEETLPFHFQ LDKQVVHAEI
QNLGHWMDGT FNIKTAFHCY GECKKYAYPW QTAKCFFEKD YQYETSWGCN PPDCPGVGTG
CTACGVYLDK LRSVGKAYKI VSLKFTRKVC IQLGTEQTCK HIDVNDCLVT PSVKVCLIGT
ISKLQPGDTL LFLGPLEQGG IILKQWCTTS CVFGDPGDIM STTTGMKCPE HTGSFRKICG
FATTPTCEYQ GNTISGFQRM MATRDSFQSF NVTEPHITSN RLEWIDPDSS IKDHINMVLN
RDVSFQDLSD NPCKVDLHTQ SIDGAWGSGV GFTLVCTVGL TECANFITSI KACDSAMCYG
ATVTNLLRGS NTVKVVGKGG HSGSLFKCCH DTDCTEEGLA ASPPHLDRVT GYNQIDSDKV
YDDGAPPCTI KCWFTKSGEW LLGILNGNWV VVAVLIVILI LSILLFSFFC PIRGRKNKSN
