GP_UUKS
ID GP_UUKS Reviewed; 1008 AA.
AC P09613;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE AltName: Full=p110 {ECO:0000303|PubMed:8985341};
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 Uukuniemi virus (strain S23) (UUKV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX NCBI_TaxID=487099;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=34613; Ixodes ricinus (Common tick) (Acarus ricinus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PROTEIN SEQUENCE OF 18-29 AND
RP 514-525.
RX PubMed=3629974; DOI=10.1016/0042-6822(87)90060-2;
RA Ronnholm R., Pettersson R.F.;
RT "Complete nucleotide sequence of the M RNA segment of Uukuniemi virus
RT encoding the membrane glycoproteins G1 and G2.";
RL Virology 160:191-202(1987).
RN [2]
RP SUBUNIT (GLYCOPROTEIN N), SUBUNIT (GLYCOPROTEIN C), SUBCELLULAR LOCATION
RP (GLYCOPROTEIN N), SUBCELLULAR LOCATION (GLYCOPROTEIN C), FUNCTION
RP (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=1988460; DOI=10.1083/jcb.112.2.257;
RA Persson R., Pettersson R.F.;
RT "Formation and intracellular transport of a heterodimeric viral spike
RT protein complex.";
RL J. Cell Biol. 112:257-266(1991).
RN [3]
RP SUBUNIT (GLYCOPROTEIN N), SUBUNIT (GLYCOPROTEIN C), SUBCELLULAR LOCATION
RP (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION (GLYCOPROTEIN C).
RX PubMed=1602557; DOI=10.1128/jvi.66.7.4525-4531.1992;
RA Roennholm R.;
RT "Localization to the Golgi complex of Uukuniemi virus glycoproteins G1 and
RT G2 expressed from cloned cDNAs.";
RL J. Virol. 66:4525-4531(1992).
RN [4]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND SUBCELLULAR LOCATION
RP (GLYCOPROTEIN C).
RX PubMed=7625126; DOI=10.1016/0168-1702(95)00006-c;
RA Melin L., Persson R., Andersson A., Bergstroem A., Roennholm R.,
RA Pettersson R.F.;
RT "The membrane glycoprotein G1 of Uukuniemi virus contains a signal for
RT localization to the Golgi complex.";
RL Virus Res. 36:49-66(1995).
RN [5]
RP SUBUNIT (GLYCOPROTEIN N).
RX PubMed=7645217; DOI=10.1006/viro.1995.1397;
RA Roenkae H., Hilden P., Von Bonsdorff C.H., Kuismanen E.;
RT "Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi
RT virus.";
RL Virology 211:241-250(1995).
RN [6]
RP PALMITOYLATION (GLYCOPROTEIN N), PALMITOYLATION (GLYCOPROTEIN C), TOPOLOGY
RP (ENVELOPMENT POLYPROTEIN), AND PROTEOLYTIC CLEAVAGE (ENVELOPMENT
RP POLYPROTEIN).
RX PubMed=8985341; DOI=10.1128/jvi.71.1.218-225.1997;
RA Andersson A.M., Melin L., Persson R., Raschperger E., Wikstrom L.,
RA Pettersson R.F.;
RT "Processing and membrane topology of the spike proteins G1 and G2 of
RT Uukuniemi virus.";
RL J. Virol. 71:218-225(1997).
RN [7]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), PALMITOYLATION (GLYCOPROTEIN N),
RP MUTAGENESIS OF CYS-440 AND CYS-443, AND DOMAIN (GLYCOPROTEIN N).
RX PubMed=9151865; DOI=10.1128/jvi.71.6.4717-4727.1997;
RA Andersson A.M., Melin L., Bean A., Pettersson R.F.;
RT "A retention signal necessary and sufficient for Golgi localization maps to
RT the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane
RT glycoprotein.";
RL J. Virol. 71:4717-4727(1997).
RN [8]
RP SUBCELLULAR LOCATION (GLYCOPROTEIN N), AND DOMAIN (GLYCOPROTEIN N).
RX PubMed=9811692; DOI=10.1128/jvi.72.12.9585-9596.1998;
RA Andersson A.M., Pettersson R.F.;
RT "Targeting of a short peptide derived from the cytoplasmic tail of the G1
RT membrane glycoprotein of Uukuniemi virus (Bunyaviridae) to the Golgi
RT complex.";
RL J. Virol. 72:9585-9596(1998).
RN [9]
RP DOMAIN (GLYCOPROTEIN N), SUBUNIT, SUBCELLULAR LOCATION (GLYCOPROTEIN N),
RP SUBCELLULAR LOCATION (GLYCOPROTEIN C), MUTAGENESIS OF LEU-438; LEU-439 AND
RP LYS-1006, AND FUNCTION (GLYCOPROTEIN N).
RX PubMed=17670814; DOI=10.1128/jvi.00767-07;
RA Overby A.K., Popov V.L., Pettersson R.F., Neve E.P.;
RT "The cytoplasmic tails of Uukuniemi Virus (Bunyaviridae) G(N) and G(C)
RT glycoproteins are important for intracellular targeting and the budding of
RT virus-like particles.";
RL J. Virol. 81:11381-11391(2007).
RN [10]
RP DOMAIN (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN N).
RX PubMed=17229712; DOI=10.1128/jvi.02655-06;
RA Overby A.K., Pettersson R.F., Neve E.P.;
RT "The glycoprotein cytoplasmic tail of Uukuniemi virus (Bunyaviridae)
RT interacts with ribonucleoproteins and is critical for genome packaging.";
RL J. Virol. 81:3198-3205(2007).
RN [11]
RP STRUCTURE BY ELECTRON CRYOMICROSCOPY OF THE VIRAL PARTICLE, AND FUNCTION
RP (GLCOPROTEIN C).
RX PubMed=18272496; DOI=10.1073/pnas.0708738105;
RA Overby A.K., Pettersson R.F., Gruenewald K., Huiskonen J.T.;
RT "Insights into bunyavirus architecture from electron cryotomography of
RT Uukuniemi virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2375-2379(2008).
RN [12]
RP FUNCTION (GLYCOPROTEIN C).
RX PubMed=20542252; DOI=10.1016/j.chom.2010.05.007;
RA Lozach P.Y., Mancini R., Bitto D., Meier R., Oestereich L., Overby A.K.,
RA Pettersson R.F., Helenius A.;
RT "Entry of bunyaviruses into mammalian cells.";
RL Cell Host Microbe 7:488-499(2010).
RN [13]
RP FUNCTION (GLYCOPROTEIN N), AND FUNCTION (GLYCOPROTEIN C).
RX PubMed=21767814; DOI=10.1016/j.chom.2011.06.007;
RA Lozach P.Y., Kuehbacher A., Meier R., Mancini R., Bitto D., Bouloy M.,
RA Helenius A.;
RT "DC-SIGN as a receptor for phleboviruses.";
RL Cell Host Microbe 10:75-88(2011).
RN [14]
RP GLYCOSYLATION (GLYCOPROTEIN N), AND GLYCOSYLATION (GLYCOPROTEIN C).
RX PubMed=24942574; DOI=10.1128/jvi.01662-14;
RA Crispin M., Harvey D.J., Bitto D., Halldorsson S., Bonomelli C.,
RA Edgeworth M., Scrivens J.H., Huiskonen J.T., Bowden T.A.;
RT "Uukuniemi Phlebovirus assembly and secretion leave a functional imprint on
RT the virion glycome.";
RL J. Virol. 88:10244-10251(2014).
CC -!- FUNCTION: [Glycoprotein N]: Structural component of the virion that
CC interacts with glycoprotein C (PubMed:1988460). 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:18272496). They
CC are able to attach the virion to the host cell receptor CD209/DC-SIGN
CC and to promote fusion of membranes with the late endosome after
CC endocytosis of the virion (PubMed:20542252). Plays a role in the
CC packaging of ribonucleoproteins during virus assembly (PubMed:17670814,
CC PubMed:17229712). {ECO:0000250|UniProtKB:P21401,
CC ECO:0000269|PubMed:17229712, ECO:0000269|PubMed:17670814,
CC ECO:0000269|PubMed:18272496, ECO:0000269|PubMed:1988460,
CC ECO:0000269|PubMed:20542252}.
CC -!- FUNCTION: [Glycoprotein C]: Structural component of the virion that
CC interacts with glycoprotein N (PubMed:1988460). Acts as a class II
CC fusion protein that is activated upon acidification and subsequent
CC repositioning of the glycoprotein N (By similarity). The glycoprotein
CC protrusions are arranged on an icosahedral lattice, with T=12
CC triangulation (PubMed:18272496). They are able to attach the virion to
CC the host cell receptor CD209/DC-SIGN and to promote fusion of membranes
CC with the late endosome after endocytosis of the virion
CC (PubMed:20542252). {ECO:0000250|UniProtKB:P21401,
CC ECO:0000269|PubMed:18272496, ECO:0000269|PubMed:1988460,
CC ECO:0000269|PubMed:20542252}.
CC -!- SUBUNIT: [Glycoprotein N]: Homodimer (PubMed:7645217). Heterodimer with
CC glycoprotein C (PubMed:1988460, PubMed:1602557, PubMed:17670814).
CC Homotrimer (postfusion) (By similarity). {ECO:0000250|UniProtKB:P03518,
CC ECO:0000269|PubMed:1602557, ECO:0000269|PubMed:17670814,
CC ECO:0000269|PubMed:1988460, ECO:0000269|PubMed:7645217}.
CC -!- SUBUNIT: [Glycoprotein C]: Heterodimer with glycoprotein N
CC (PubMed:1988460, PubMed:1602557, PubMed:17670814). Homotrimer
CC (postfusion) (By similarity). {ECO:0000250|UniProtKB:J3WAX0,
CC ECO:0000269|PubMed:1602557, ECO:0000269|PubMed:17670814,
CC ECO:0000269|PubMed:1988460}.
CC -!- INTERACTION:
CC P09613; Q92538: GBF1; Xeno; NbExp=2; IntAct=EBI-21497244, EBI-359050;
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC {ECO:0000305|PubMed:1988460}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8985341}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:17670814, ECO:0000269|PubMed:9151865,
CC ECO:0000269|PubMed:9811692, ECO:0000305|PubMed:1602557,
CC ECO:0000305|PubMed:7625126}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8985341}. Host endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:1988460, ECO:0000305|PubMed:7625126}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:8985341}. Note=Interaction
CC between Glycoprotein N and Glycoprotein C is essential for proper
CC targeting of Glycoprotein C to the Golgi complex, where virion budding
CC occurs. {ECO:0000269|PubMed:1602557, ECO:0000269|PubMed:7625126}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC {ECO:0000305|PubMed:1988460}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8985341}. Host Golgi apparatus membrane
CC {ECO:0000269|PubMed:17670814, ECO:0000305|PubMed:1602557,
CC ECO:0000305|PubMed:7625126}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8985341}. Host endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:1988460, ECO:0000305|PubMed:7625126}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:8985341}. Note=Interaction
CC between Glycoprotein N and Glycoprotein C is essential for proper
CC targeting of Glycoprotein C to the Golgi complex, where virion budding
CC occurs. {ECO:0000269|PubMed:1602557, ECO:0000269|PubMed:7625126}.
CC -!- DOMAIN: [Glycoprotein N]: Contains a Golgi retention signal on its C-
CC terminus (PubMed:17670814, PubMed:9151865, PubMed:9811692). The
CC cytoplasmic tail specifically interacts with the ribonucleoproteins and
CC is critical for genome packaging (PubMed:17670814, PubMed:17229712).
CC {ECO:0000269|PubMed:17229712, ECO:0000269|PubMed:17670814,
CC ECO:0000269|PubMed:9151865, ECO:0000269|PubMed:9811692}.
CC -!- PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo
CC yield mature proteins including glycoprotein C and glycoprotein N.
CC {ECO:0000269|PubMed:8985341}.
CC -!- PTM: [Glycoprotein N]: The cytoplasmic tail is Palmitoylated.
CC {ECO:0000269|PubMed:8985341, ECO:0000269|PubMed:9151865}.
CC -!- PTM: [Glycoprotein N]: Glycosylated. Contains principally poly-N-
CC acetyllactosamine glycans. {ECO:0000269|PubMed:24942574}.
CC -!- PTM: [Glycoprotein C]: Glycosylated. Contains principally oligomannose-
CC type glycans that can attach to host CD209/DC-SIGN.
CC {ECO:0000269|PubMed:24942574}.
CC -!- PTM: [Glycoprotein C]: Palmitoylated. {ECO:0000269|PubMed:8985341}.
CC -!- SIMILARITY: Belongs to the phlebovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M17417; AAA79512.1; -; Genomic_RNA.
DR PIR; A28502; GNVUUK.
DR SMR; P09613; -.
DR IntAct; P09613; 40.
DR Proteomes; UP000008595; 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: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:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR043603; Phlebo_G2_C.
DR InterPro; IPR010826; Phlebovirus_G1.
DR InterPro; IPR009878; Phlebovirus_G2_fusion.
DR Pfam; PF19019; Phlebo_G2_C; 1.
DR Pfam; PF07243; Phlebovirus_G1; 1.
DR Pfam; PF07245; Phlebovirus_G2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; 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-virus interaction; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3629974"
FT CHAIN 18..1008
FT /note="Envelopment polyprotein"
FT /id="PRO_0000232521"
FT CHAIN 18..513
FT /note="Glycoprotein N"
FT /id="PRO_0000036853"
FT CHAIN 514..1008
FT /note="Glycoprotein C"
FT /id="PRO_0000036855"
FT TOPO_DOM 18..394
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8985341,
FT ECO:0000269|PubMed:9151865"
FT TOPO_DOM 514..977
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1008
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8985341"
FT REGION 419..465
FT /note="Golgi retention signal"
FT /evidence="ECO:0000269|PubMed:9151865,
FT ECO:0000269|PubMed:9811692"
FT REGION 461..465
FT /note="Important for correct targeting of the glycoproteins
FT to the Golgi complex but not for heterodimerization"
FT /evidence="ECO:0000269|PubMed:17670814"
FT REGION 497..513
FT /note="Internal signal sequence for glycoprotein C"
FT /evidence="ECO:0000269|PubMed:8985341"
FT REGION 601..607
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT REGION 644..655
FT /note="Fusion loop"
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT SITE 513..514
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000305|PubMed:8985341"
FT SITE 1006
FT /note="Important for glycoprotein C and glycoprotein N
FT subcellular location"
FT /evidence="ECO:0000269|PubMed:17670814"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 138..269
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 156..166
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 206..247
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 216..226
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 233..238
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 292..295
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 299..368
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 319..324
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 514..555
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 527..537
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 580..677
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 595..789
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 601..650
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 607..657
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 612..639
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 643..648
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 728..742
FT /evidence="ECO:0000250|UniProtKB:R4V2Q5"
FT DISULFID 758..771
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 851..924
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT DISULFID 861..864
FT /evidence="ECO:0000250|UniProtKB:P21401"
FT MUTAGEN 438
FT /note="L->A: Loss of budding into the Golgi membrane; no
FT effect on Golgi subcellular location."
FT /evidence="ECO:0000269|PubMed:17670814"
FT MUTAGEN 439
FT /note="L->A: Budding defect; no effect on Golgi subcellular
FT location."
FT /evidence="ECO:0000269|PubMed:17670814"
FT MUTAGEN 440
FT /note="C->A: Decreased palmitoylation."
FT /evidence="ECO:0000269|PubMed:9151865"
FT MUTAGEN 443
FT /note="C->A: Decreased palmitoylation."
FT /evidence="ECO:0000269|PubMed:9151865"
FT MUTAGEN 1006
FT /note="K->A: Mislocalization of glycoprotein C and
FT glycoprotein N to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:17670814"
SQ SEQUENCE 1008 AA; 113589 MW; F557C06D8DB77E32 CRC64;
MVRTYLLLLL LCGPATPFFN HLMDVTRRLL DSSNATWQRD QPDTHRLSRL DAHVMSMLGV
GSHIDEVSVN HSQHLHNFRS YNCEEGRRTL TMMDPKSGKF KRLKCNENQT LSKDCASCIE
KKSSIMKSEH LVYDDAICQS DYSSPEAMPD HETHLCRIGP LHIQHCTHEA KRVQHVSWFW
IDGKLRVYDD FSVSWTEGKF LSLFDCLNET SKDHNCNKAV CLEGRCSGDL QFCTEFTCSY
AKADCNCKRN QVSGVAVVHT KHGSFMPECM GQSLWSVRKP LSKRSVTVQQ PCMDCESDCK
VDHILVIVRH FYPDHYQACL GSTCLTGRAK DKEFKIPFKM ADRLSDSHFE IRIWDKERSN
EYFLESRCES VDACAAITCW FCRANWANIH CFSKEQVLIL VAVSSLCILL LASVLRALKV
IATFTWKIIK PFWWILSLLC RTCSKRLNKR AERLKESIHS LEEGLNNVDE GPREQNNPAR
AVARPNVRQK MFNLTRLSPV VVGMLCLACP VESCSDSISV TASSQRCSTS SDGVNSCFVS
TSSLLQVSPK GQESCLILKG PTGTAVDSIR IKTTDIKLEC VRRDLYWVPR VTHRCIGTRR
CHLMGACKGE ACSEFKINDY SPEWGHEEEL MAQLGWSYCV EQCGGALCQC FNMRPSCFYL
RKTFSHLSQD AFNIYECSEW SYRINVLVST NSTHSNLTLK LGVPDSIPHG LISLSSVSQP
PAIAYSECFG EDLHGTKFHT VCNRRTDYTL GRIGEIQCPT KADALAVSKR CISSDSIIFS
KVHKDSVDCQ SSIIDPMTIR NRNKLPSTVG SVTFWPTETS VEAAIPDLAS ATMLIRLDGY
TIQFRSDSNK CSPRFLSLSG CYNCEAGAKL ELEHVTDFGT ALGILECPSL GYTTYYEVKN
TLEKSIRTMH LNGSHVEAKC YFRCPNSESQ LTIRGELIYL FNDDIRHHNQ TLSPGLSPKS
GSGWDPFGWF KASWLRAIWA ILGGTVSLII GVVIIYMVFT LCLKVKKS
