ID   OSTB_YEAST              Reviewed;         430 AA.
AC   P33767; D3DLP5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1;
DE            Short=Oligosaccharyl transferase subunit WBP1;
DE   AltName: Full=Oligosaccharyl transferase subunit beta;
DE   Flags: Precursor;
GN   Name=WBP1; OrderedLocusNames=YEL002C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=1724755;
RA   Te Heesen S., Rauhut R., Aebersold R., Abelson J., Aebi M., Clark M.W.;
RT   "An essential 45 kDa yeast transmembrane protein reacts with anti-nuclear
RT   pore antibodies: purification of the protein, immunolocalization and
RT   cloning of the gene.";
RL   Eur. J. Cell Biol. 56:8-18(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-40.
RX   PubMed=7703229; DOI=10.1021/bi00013a005;
RA   Pathak R., Hendrickson T.L., Imperiali B.;
RT   "Sulfhydryl modification of the yeast Wbp1p inhibits oligosaccharyl
RT   transferase activity.";
RL   Biochemistry 34:4179-4185(1995).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=1600939; DOI=10.1002/j.1460-2075.1992.tb05265.x;
RA   Te Heesen S., Janetzky B., Lehle L., Aebi M.;
RT   "The yeast WBP1 is essential for oligosaccharyl transferase activity in
RT   vivo and in vitro.";
RL   EMBO J. 11:2071-2075(1992).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8181570; DOI=10.1016/0014-5793(94)00356-4;
RA   Knauer R., Lehle L.;
RT   "The N-oligosaccharyltransferase complex from yeast.";
RL   FEBS Lett. 344:83-86(1994).
RN   [7]
RP   IDENTIFICATION IN THE OLIGOSACCHARYL TRANSFERASE COMPLEX.
RX   PubMed=8175708; DOI=10.1016/s0021-9258(18)99962-x;
RA   Kelleher D.J., Gilmore R.;
RT   "The Saccharomyces cerevisiae oligosaccharyltransferase is a protein
RT   complex composed of Wbp1p, Swp1p, and four additional polypeptides.";
RL   J. Biol. Chem. 269:12908-12917(1994).
RN   [8]
RP   IDENTIFICATION IN THE OLIGOSACCHARYL TRANSFERASE COMPLEX.
RX   PubMed=9405463; DOI=10.1074/jbc.272.51.32513;
RA   Karaoglu D., Kelleher D.J., Gilmore R.;
RT   "The highly conserved Stt3 protein is a subunit of the yeast
RT   oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p.";
RL   J. Biol. Chem. 272:32513-32520(1997).
RN   [9]
RP   REVIEW ON OLIGOSACCHARYL TRANSFERASE.
RX   PubMed=9878773; DOI=10.1016/s0304-4165(98)00128-7;
RA   Knauer R., Lehle L.;
RT   "The oligosaccharyltransferase complex from yeast.";
RL   Biochim. Biophys. Acta 1426:259-273(1999).
RN   [10]
RP   FUNCTION.
RX   PubMed=11580295; DOI=10.1021/bi0111911;
RA   Karaoglu D., Kelleher D.J., Gilmore R.;
RT   "Allosteric regulation provides a molecular mechanism for preferential
RT   utilization of the fully assembled dolichol-linked oligosaccharide by the
RT   yeast oligosaccharyltransferase.";
RL   Biochemistry 40:12193-12206(2001).
RN   [11]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [12]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [13]
RP   COMPOSITION OF OLIGOSACCHARYL TRANSFERASE COMPLEXES.
RX   PubMed=16297388; DOI=10.1016/j.febslet.2005.10.063;
RA   Schwarz M., Knauer R., Lehle L.;
RT   "Yeast oligosaccharyltransferase consists of two functionally distinct sub-
RT   complexes, specified by either the Ost3p or Ost6p subunit.";
RL   FEBS Lett. 579:6564-6568(2005).
RN   [14]
RP   COMPOSITION OF OLIGOSACCHARYL TRANSFERASE COMPLEXES.
RX   PubMed=16096346; DOI=10.1093/glycob/cwj025;
RA   Spirig U., Bodmer D., Wacker M., Burda P., Aebi M.;
RT   "The 3.4-kDa Ost4 protein is required for the assembly of two distinct
RT   oligosaccharyltransferase complexes in yeast.";
RL   Glycobiology 15:1396-1406(2005).
RN   [15]
RP   COMPOSITION OF OLIGOSACCHARYL TRANSFERASE COMPLEXES.
RX   PubMed=16096345; DOI=10.1093/glycob/cwj026;
RA   Yan A., Lennarz W.J.;
RT   "Two oligosaccharyl transferase complexes exist in yeast and associate with
RT   two different translocons.";
RL   Glycobiology 15:1407-1415(2005).
RN   [16]
RP   INTERACTION WITH SEC61; SBH1 AND SSS1.
RX   PubMed=15831493; DOI=10.1074/jbc.m502858200;
RA   Chavan M., Yan A., Lennarz W.J.;
RT   "Subunits of the translocon interact with components of the oligosaccharyl
RT   transferase complex.";
RL   J. Biol. Chem. 280:22917-22924(2005).
RN   [17]
RP   INTERACTION WITH OST2; OST3; OST5; OST6; WBP1 AND SWP1.
RX   PubMed=15886282; DOI=10.1073/pnas.0502669102;
RA   Yan A., Wu E., Lennarz W.J.;
RT   "Studies of yeast oligosaccharyl transferase subunits using the split-
RT   ubiquitin system: topological features and in vivo interactions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:7121-7126(2005).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 425-430.
RX   PubMed=23481256; DOI=10.1038/emboj.2013.41;
RA   Ma W., Goldberg J.;
RT   "Rules for the recognition of dilysine retrieval motifs by coatomer.";
RL   EMBO J. 32:926-937(2013).
RN   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-430.
RX   PubMed=29466327; DOI=10.1038/nature25755;
RA   Bai L., Wang T., Zhao G., Kovach A., Li H.;
RT   "The atomic structure of a eukaryotic oligosaccharyltransferase complex.";
RL   Nature 555:328-333(2018).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1-430, AND
RP   GLYCOSYLATION AT ASN-60 AND ASN-332.
RX   PubMed=29301962; DOI=10.1126/science.aar5140;
RA   Wild R., Kowal J., Eyring J., Ngwa E.M., Aebi M., Locher K.P.;
RT   "Structure of the yeast oligosaccharyltransferase complex gives insight
RT   into eukaryotic N-glycosylation.";
RL   Science 359:545-550(2018).
CC   -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC       catalyzes the initial transfer of a defined glycan
CC       (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC       pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC       consensus motif in nascent polypeptide chains, the first step in
CC       protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC       the complex associates with the Sec61 complex at the channel-forming
CC       translocon complex that mediates protein translocation across the
CC       endoplasmic reticulum (ER). All subunits are required for a maximal
CC       enzyme activity. {ECO:0000269|PubMed:11580295,
CC       ECO:0000269|PubMed:1600939}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:9878773}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex,
CC       which appears to exist in two assemblies comprising OST1, OST2, OST4,
CC       OST5, STT3, SWP1, WPB1, and either OST3 or OST6 (PubMed:8175708,
CC       PubMed:16297388, PubMed:16096345, PubMed:15831493, PubMed:15886282,
CC       PubMed:9405463, PubMed:29301962). OST assembly occurs through the
CC       formation of 3 subcomplexes. Subcomplex 1 contains OST1 and OST5,
CC       subcomplex 2 contains STT3, OST3, and OST4, and subcomplex 3 contains
CC       OST2, WBP1, and SWP1 (PubMed:29301962). Interacts with SEC61, SBH1 and
CC       SSS1 (PubMed:15831493). {ECO:0000269|PubMed:15831493,
CC       ECO:0000269|PubMed:15886282, ECO:0000269|PubMed:16096345,
CC       ECO:0000269|PubMed:16297388, ECO:0000269|PubMed:29301962,
CC       ECO:0000269|PubMed:8175708, ECO:0000269|PubMed:9405463}.
CC   -!- INTERACTION:
CC       P33767; P53622: COP1; NbExp=3; IntAct=EBI-12658, EBI-4860;
CC       P33767; Q99380: OST4; NbExp=6; IntAct=EBI-12658, EBI-12689;
CC       P33767; P52870: SBH1; NbExp=2; IntAct=EBI-12658, EBI-16410;
CC       P33767; P32915: SEC61; NbExp=2; IntAct=EBI-12658, EBI-16400;
CC       P33767; P35179: SSS1; NbExp=2; IntAct=EBI-12658, EBI-16406;
CC       P33767; P39007: STT3; NbExp=2; IntAct=EBI-12658, EBI-18447;
CC       P33767; Q02795: SWP1; NbExp=3; IntAct=EBI-12658, EBI-12666;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1724755,
CC       ECO:0000269|PubMed:8181570}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:29301962}.
CC   -!- DOMAIN: The cytoplasmic C-terminal domain contains a functional
CC       dilysine-retrieval motif, which is involved in the retrograde Golgi-to-
CC       ER transport of the protein.
CC   -!- MISCELLANEOUS: Present with 14900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR   EMBL; X61388; CAA43660.1; -; Genomic_DNA.
DR   EMBL; U18530; AAB64479.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07649.1; -; Genomic_DNA.
DR   PIR; S20187; S20187.
DR   RefSeq; NP_010914.3; NM_001178817.3.
DR   PDB; 4J86; X-ray; 1.48 A; C/D=425-430.
DR   PDB; 6C26; EM; 3.50 A; B=1-430.
DR   PDB; 6EZN; EM; 3.30 A; G=1-430.
DR   PDB; 7OCI; EM; 3.46 A; G=1-430.
DR   PDB; 8AGC; EM; 3.10 A; G=1-430.
DR   PDB; 8AGE; EM; 2.80 A; G=1-430.
DR   PDBsum; 4J86; -.
DR   PDBsum; 6C26; -.
DR   PDBsum; 6EZN; -.
DR   PDBsum; 7OCI; -.
DR   PDBsum; 8AGC; -.
DR   PDBsum; 8AGE; -.
DR   AlphaFoldDB; P33767; -.
DR   EMDB; EMD-12808; -.
DR   EMDB; EMD-15419; -.
DR   EMDB; EMD-4161; -.
DR   EMDB; EMD-7336; -.
DR   SMR; P33767; -.
DR   BioGRID; 36729; 487.
DR   ComplexPortal; CPX-1638; Oligosaccharyl transferase complex, OST6 variant.
DR   ComplexPortal; CPX-1639; Oligosaccharyl transferase complex, OST3 variant.
DR   DIP; DIP-676N; -.
DR   ELM; P33767; -.
DR   IntAct; P33767; 44.
DR   MINT; P33767; -.
DR   STRING; 4932.YEL002C; -.
DR   TCDB; 9.B.142.3.14; the integral membrane glycosyltransferase family 39 (gt39) family.
DR   GlyCosmos; P33767; 2 sites, No reported glycans.
DR   GlyGen; P33767; 2 sites.
DR   iPTMnet; P33767; -.
DR   MaxQB; P33767; -.
DR   PaxDb; 4932-YEL002C; -.
DR   PeptideAtlas; P33767; -.
DR   ABCD; P33767; 1 sequenced antibody.
DR   EnsemblFungi; YEL002C_mRNA; YEL002C; YEL002C.
DR   GeneID; 856716; -.
DR   KEGG; sce:YEL002C; -.
DR   AGR; SGD:S000000728; -.
DR   SGD; S000000728; WBP1.
DR   VEuPathDB; FungiDB:YEL002C; -.
DR   eggNOG; KOG2754; Eukaryota.
DR   GeneTree; ENSGT00390000017294; -.
DR   HOGENOM; CLU_031804_1_1_1; -.
DR   InParanoid; P33767; -.
DR   OMA; IDHLHYD; -.
DR   OrthoDB; 1356at2759; -.
DR   BioCyc; MetaCyc:YEL002C-MONOMER; -.
DR   BioCyc; YEAST:YEL002C-MONOMER; -.
DR   BRENDA; 2.4.99.18; 984.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 856716; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P33767; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P33767; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IMP:SGD.
DR   GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:SGD.
DR   GO; GO:0016757; F:glycosyltransferase activity; IDA:SGD.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IDA:ComplexPortal.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR   InterPro; IPR005013; DDOST_48_kDa_subunit.
DR   PANTHER; PTHR10830; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE 48 KDA SUBUNIT; 1.
DR   PANTHER; PTHR10830:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE 48 KDA SUBUNIT; 1.
DR   Pfam; PF03345; DDOST_48kD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:1724755,
FT                   ECO:0000269|PubMed:7703229"
FT   CHAIN           21..430
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit WBP1"
FT                   /id="PRO_0000021961"
FT   TOPO_DOM        24..393
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:29301962"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:29301962"
FT   TOPO_DOM        415..430
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:1724755"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29301962"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29301962"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           41..49
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          54..61
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           88..93
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           96..104
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           121..128
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          199..205
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          216..222
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:8AGC"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            243..245
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           247..256
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          260..276
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          285..287
FT                   /evidence="ECO:0007829|PDB:6EZN"
FT   STRAND          289..299
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          304..306
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          313..326
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          337..345
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          351..359
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          367..376
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           380..382
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           386..388
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   STRAND          389..391
FT                   /evidence="ECO:0007829|PDB:6EZN"
FT   HELIX           392..414
FT                   /evidence="ECO:0007829|PDB:8AGE"
FT   HELIX           426..429
FT                   /evidence="ECO:0007829|PDB:4J86"
SQ   SEQUENCE   430 AA;  49392 MW;  495DA76BE8A9B29A CRC64;
     MRTDWNFFFC ILLQAIFVVG TQTSRTLVLY DQSTEPLEEY SVYLKDLEQR NYKLEYLDIN
     STSTTVDLYD KEQRLFDNII VFPTKGGKNL ARQIPVKQLI KFFENEGNIL CMSSPGAVPN
     TIRLFLNELG IYPSPKGHVI RDYFSPSSEE LVVSSNHLLN KYVYNARKSE DFVFGESSAA
     LLENREQIVP ILNAPRTSFT ESKGKCNSWT SGSQGFLVVG FQNLNNARLV WIGSSDFLKN
     KNQDSNQEFA KELLKWTFNE KSVIKSVHAV HSHADGTSYD EEPYKIKDKV IYSVGFSEWN
     GEEWLPHIAD DIQFELRQVD PYYRLTLSPS GNDSETQYYT TGEFILPDRH GVFTFLTDYR
     KIGLSFTTDK DVKAIRHLAN DEYPRSWEIS NSWVYISAIC GVIVAWIFFV VSFVTTSSVG
     KKLETFKKTN
//