CSG_HALVD
ID CSG_HALVD Reviewed; 827 AA.
AC P25062; D4GU85; Q7M554;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cell surface glycoprotein;
DE AltName: Full=S-layer glycoprotein;
DE Flags: Precursor;
GN Name=csg; Synonyms=cwd; OrderedLocusNames=HVO_2072;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-51; 153-164;
RP 278-292; 297-330; 348-360; 461-467; 494-504; 652-679 AND 737-757,
RP GLYCOSYLATION AT ASN-47; ASN-308 AND ASN-313, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=2123862; DOI=10.1128/jb.172.12.7111-7118.1990;
RA Sumper M., Berg E., Mengele R., Strobel I.;
RT "Primary structure and glycosylation of the S-layer protein of Haloferax
RT volcanii.";
RL J. Bacteriol. 172:7111-7118(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP PROTEIN SEQUENCE OF 37-48; 297-326 AND 505-549, GLYCOSYLATION AT ASN-47;
RP ASN-308; ASN-313 AND ASN-532, GLYCAN COMPOSITION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=1569073; DOI=10.1016/s0021-9258(18)42424-6;
RA Mengele R., Sumper M.;
RT "Drastic differences in glycosylation of related S-layer glycoproteins from
RT moderate and extreme halophiles.";
RL J. Biol. Chem. 267:8182-8185(1992).
RN [4]
RP FUNCTION, AND STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=16453843; DOI=10.1002/j.1460-2075.1988.tb02974.x;
RA Kessel M., Wildhaber I., Cohen S., Baumeister W.;
RT "Three-dimensional structure of the regular surface glycoprotein layer of
RT Halobacterium volcanii from the Dead Sea.";
RL EMBO J. 7:1549-1554(1988).
RN [5]
RP LIPIDATION.
RX PubMed=12069685; DOI=10.1042/bj20020757;
RA Konrad Z., Eichler J.;
RT "Lipid modification of proteins in Archaea: attachment of a mevalonic acid-
RT based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii
RT follows protein translocation.";
RL Biochem. J. 366:959-964(2002).
RN [6]
RP GLYCOSYLATION AT ASN-47 AND ASN-117.
RX PubMed=17996897; DOI=10.1016/j.jmb.2007.10.042;
RA Abu-Qarn M., Yurist-Doutsch S., Giordana A., Trauner A., Morris H.R.,
RA Hitchen P., Medalia O., Dell A., Eichler J.;
RT "Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-
RT layer glycoprotein and proper assembly of the surface layer.";
RL J. Mol. Biol. 374:1224-1236(2007).
RN [7]
RP GLYCOSYLATION AT ASN-47.
RX PubMed=20802039; DOI=10.1128/jb.00705-10;
RA Kaminski L., Abu-Qarn M., Guan Z., Naparstek S., Ventura V.V., Raetz C.R.,
RA Hitchen P.G., Dell A., Eichler J.;
RT "AglJ adds the first sugar of the N-linked pentasaccharide decorating the
RT Haloferax volcanii S-layer glycoprotein.";
RL J. Bacteriol. 192:5572-5579(2010).
RN [8]
RP GLYCOSYLATION AT ASN-47 AND ASN-117.
RX PubMed=20149102; DOI=10.1111/j.1365-2958.2010.07090.x;
RA Magidovich H., Yurist-Doutsch S., Konrad Z., Ventura V.V., Dell A.,
RA Hitchen P.G., Eichler J.;
RT "AglP is a S-adenosyl-L-methionine-dependent methyltransferase that
RT participates in the N-glycosylation pathway of Haloferax volcanii.";
RL Mol. Microbiol. 76:190-199(2010).
RN [9]
RP GLYCOSYLATION.
RX PubMed=21091511; DOI=10.1111/j.1365-2958.2010.07405.x;
RA Guan Z., Naparstek S., Kaminski L., Konrad Z., Eichler J.;
RT "Distinct glycan-charged phosphodolichol carriers are required for the
RT assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer
RT glycoprotein.";
RL Mol. Microbiol. 78:1294-1303(2010).
RN [10]
RP GLYCOSYLATION AT ASN-532, AND LACK OF GLYCOSYLATION AT ASN-404.
RX PubMed=22029420; DOI=10.1111/j.1462-2920.2011.02625.x;
RA Guan Z., Naparstek S., Calo D., Eichler J.;
RT "Protein glycosylation as an adaptive response in Archaea: growth at
RT different salt concentrations leads to alterations in Haloferax volcanii S-
RT layer glycoprotein N-glycosylation.";
RL Environ. Microbiol. 14:743-753(2012).
RN [11]
RP GLYCOSYLATION AT ASN-532.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=24194539; DOI=10.1128/mbio.00716-13;
RA Kaminski L., Guan Z., Yurist-Doutsch S., Eichler J.;
RT "Two distinct N-glycosylation pathways process the Haloferax volcanii S-
RT layer glycoprotein upon changes in environmental salinity.";
RL MBio 4:E00716-E00716(2013).
RN [12]
RP PROTEOLYTIC PROCESSING.
RX PubMed=23651326; DOI=10.1111/mmi.12248;
RA Abdul Halim M.F., Pfeiffer F., Zou J., Frisch A., Haft D., Wu S., Tolic N.,
RA Brewer H., Payne S.H., Pasa-Tolic L., Pohlschroder M.;
RT "Haloferax volcanii archaeosortase is required for motility, mating, and C-
RT terminal processing of the S-layer glycoprotein.";
RL Mol. Microbiol. 88:1164-1175(2013).
RN [13]
RP SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, LIPIDATION, AND MUTAGENESIS
RP OF 805-GLY-PHE-806.
RX PubMed=26712937; DOI=10.1128/jb.00849-15;
RA Abdul Halim M.F., Karch K.R., Zhou Y., Haft D.H., Garcia B.A.,
RA Pohlschroder M.;
RT "Permuting the PGF signature motif blocks both archaeosortase-dependent C-
RT terminal cleavage and prenyl lipid attachment for the Haloferax volcanii S-
RT layer glycoprotein.";
RL J. Bacteriol. 198:808-815(2015).
CC -!- FUNCTION: S-layer protein. The S-layer is a paracrystalline mono-
CC layered assembly of proteins which coat the surface of the cell.
CC {ECO:0000269|PubMed:16453843, ECO:0000269|PubMed:2123862}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer
CC {ECO:0000269|PubMed:1569073, ECO:0000269|PubMed:2123862}. Cell membrane
CC {ECO:0000269|PubMed:1569073, ECO:0000269|PubMed:2123862}. Note=This
CC archaeon is covered by an S-layer with hexagonal symmetry. S-layer
CC glycoproteins are anchored to the plasma membrane as well as being
CC surface-exposed (PubMed:2123862, PubMed:1569073). Bound to the membrane
CC via a covalent lipid-mediated ArtA-dependent anchoring mechanism
CC (PubMed:26712937). {ECO:0000269|PubMed:1569073,
CC ECO:0000269|PubMed:2123862, ECO:0000269|PubMed:26712937}.
CC -!- DOMAIN: The glycoprotein is arranged on a p6 lattice with a lattice
CC constant of 16.8 nm. It forms 4.5 nm high, dome-shaped, morphological
CC complexes with a narrow pore at the apex opening into a 'funnel'
CC towards the cell membrane (PubMed:16453843).
CC {ECO:0000269|PubMed:16453843}.
CC -!- PTM: O-glycosylated on 4 to 6 threonine residues; glycans consist of
CC Glc-Gal disaccharides. {ECO:0000269|PubMed:2123862}.
CC -!- PTM: The N-terminus is not blocked.
CC -!- PTM: Cleaved by the archaeosortase ArtA at the C-terminus, with removal
CC of a short hydrophobic segment. {ECO:0000269|PubMed:23651326,
CC ECO:0000269|PubMed:26712937}.
CC -!- PTM: Lipidation: Following protein translocation across the membrane,
CC the protein is modified by a derivative of mevalonic acid
CC (PubMed:12069685, PubMed:26712937). Lipid modification is ArtA-
CC dependent and requires the conserved C-terminal PGF motif
CC (PubMed:26712937). {ECO:0000269|PubMed:12069685,
CC ECO:0000269|PubMed:26712937}.
CC -!- PTM: Asn-47 and Asn-117 are glycosylated by a pentasaccharide
CC comprising a hexose, 2 hexuronic acids, a methyl ester of a hexuronic
CC acid and mannose (PubMed:17996897, PubMed:20802039, PubMed:20149102).
CC The pentasaccharide is produced in 2 steps: first, a tetrasaccharide is
CC built on dolichol-P and then transferred to the S-layer glycoprotein.
CC Then, the mannose fifth sugar is attached to a distinct molecule of
CC dolichol-P and is transferred to the protein already carrying the
CC tetrasaccharide (PubMed:21091511). The pentasaccharide on Asn-47 was
CC initially thought to contain mannose, galactose, glucose and idose with
CC a relative ratio of 1/3/3/0.2 (PubMed:1569073). However, it was later
CC shown that it is not the case (PubMed:17996897). Under low-salt
CC conditions (1.75 M instead of 3.4 M), a tetrasaccharide consisting of a
CC sulfated hexose, 2 hexoses and rhamnose is attached to Asn-532
CC (PubMed:22029420). {ECO:0000269|PubMed:1569073,
CC ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:20149102,
CC ECO:0000269|PubMed:20802039, ECO:0000269|PubMed:21091511,
CC ECO:0000269|PubMed:2123862, ECO:0000269|PubMed:22029420,
CC ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the halobacterial S-layer protein family.
CC {ECO:0000305}.
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DR EMBL; M62816; AAA72996.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE05144.1; -; Genomic_DNA.
DR PIR; A37849; A37849.
DR PIR; A38085; A38085.
DR PDB; 7PTP; EM; 11.58 A; A/B/C/D/E=35-827.
DR PDB; 7PTR; EM; 3.46 A; A/B/C/D/E/F=35-827.
DR PDB; 7PTT; EM; 7.97 A; A/B/C/D/E/F=35-827.
DR PDB; 7PTU; EM; 3.87 A; A/B/C/D/E=35-827.
DR PDBsum; 7PTP; -.
DR PDBsum; 7PTR; -.
DR PDBsum; 7PTT; -.
DR PDBsum; 7PTU; -.
DR AlphaFoldDB; P25062; -.
DR SMR; P25062; -.
DR TCDB; 9.B.324.4.1; the pore-forming s-layer protein (s-layer) family.
DR GlyConnect; 81; 1 N-Linked glycan, 1 O-Linked glycan.
DR iPTMnet; P25062; -.
DR EnsemblBacteria; ADE05144; ADE05144; HVO_2072.
DR KEGG; hvo:HVO_2072; -.
DR eggNOG; arCOG03906; Archaea.
DR HOGENOM; CLU_015552_0_0_2; -.
DR OMA; YARDNND; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR026458; Major_cell_surface_glycoprot.
DR InterPro; IPR026371; PGF_CTERM.
DR InterPro; IPR026452; Surf_glycop_sig_pep.
DR TIGRFAMs; TIGR04207; halo_sig_pep; 1.
DR TIGRFAMs; TIGR04216; halo_surf_glyco; 1.
DR TIGRFAMs; TIGR04126; PGF_CTERM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane;
KW Reference proteome; S-layer; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:2123862"
FT CHAIN 35..?
FT /note="Cell surface glycoprotein"
FT /id="PRO_0000032617"
FT PROPEP ?..827
FT /note="Removed by archaeosortase"
FT /evidence="ECO:0000305|PubMed:23651326"
FT /id="PRO_0000444190"
FT TRANSMEM 804..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 73..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 804..806
FT /note="PGF sorting signal"
FT /evidence="ECO:0000305|PubMed:23651326"
FT COMPBIAS 764..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 404
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:22029420"
FT CARBOHYD 47
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1569073,
FT ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:20149102,
FT ECO:0000269|PubMed:20802039, ECO:0000269|PubMed:2123862"
FT CARBOHYD 117
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17996897,
FT ECO:0000269|PubMed:20149102"
FT CARBOHYD 308
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1569073,
FT ECO:0000269|PubMed:2123862"
FT CARBOHYD 313
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1569073,
FT ECO:0000269|PubMed:2123862"
FT CARBOHYD 532
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1569073,
FT ECO:0000269|PubMed:22029420, ECO:0000269|PubMed:24194539"
FT CARBOHYD 766
FT /note="N-linked (Glc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 805..806
FT /note="GF->FG: Loss of ArtA-dependent C-terminal
FT processing. Lack of lipid modification. Forms a thicker S-
FT layer."
FT /evidence="ECO:0000269|PubMed:26712937"
FT CONFLICT 534
FT /note="T -> TA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7PTR"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:7PTR"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:7PTR"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 411..421
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 455..460
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 462..472
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 496..506
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 539..547
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 552..558
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 563..572
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 576..585
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 607..617
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 624..635
FT /evidence="ECO:0007829|PDB:7PTR"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 644..651
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 657..667
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 679..687
FT /evidence="ECO:0007829|PDB:7PTR"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 721..727
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 733..741
FT /evidence="ECO:0007829|PDB:7PTR"
FT STRAND 746..755
FT /evidence="ECO:0007829|PDB:7PTR"
SQ SEQUENCE 827 AA; 85189 MW; B208E96283699974 CRC64;
MTKLKDQTRA ILLATLMVTS VFAGAIAFTG SAAAERGNLD ADSESFNKTI QSGDRVFLGE
EISTDAGLGA SNPLLTGTAG NSEGVSLDLS SPIPQTTENQ PLGTYDVDGS GSATTPNVTL
LAPRITDSEI LTSSGGDVTG SAISSSDAGN LYVNADYNYE SAEKVEVTVE DPSGTDITNE
VLSGTDTFVD DGSIGSTSST GGGVGIDMSD QDAGEYTIIL EGAEDLDFGD ATETMTLTIS
SQDEIGIELD SESVTQGTDV QYTVTNGIDG NEHVVAMDLS DLQNDATTEQ AKEVFRNIGD
TSEVGIANSS ATNTSGSSTG PTVETADIAY AVVEIDGASA VGGIETQYLD DSEVDLEVYD
AGVSATAAVG QDATNDITLT IEEGGTTLSS PTGQYVVGSE VDINGTATSS DSVAIYVRDD
GDWQLLEIGG DNEISVDSDD TFEEEDIALS GLSGDGSSIL SLTGTYRIGV IDASDADVGG
DGSVDDSLTT SEFTSGVSSS NSIRVTDQAL TGQFTTINGQ VAPVETGTVD INGTASGANS
VLVIFVDERG NVNYQEVSVD SDGTYDEDDI TVGLTQGRVT AHILSVGRDS AIGDGSLPSG
PSNGATLNDL TGYLDTLDQN NNNGEQINEL IASETVDETA SDDLIVTETF RLAESSTSID
SIYPDAAEAA GINPVATGET MVIAGSTNLK PDDNTISIEV TNEDGTSVAL EDTDEWNNDG
QWMVEIDTTD FETGTFTVEA DDGDNTDTVN VEVVSEREDT TTSSDNATDT TTTTDGPTET
TTTAEPTETT EEPTEETTTS SNTPGFGIAV ALVALVGAAL LALRREN
