ID PDI_YEAST Reviewed; 522 AA. AC P17967; D6VQX3; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 2. DT 27-MAR-2024, entry version 219. DE RecName: Full=Protein disulfide-isomerase; DE Short=PDI; DE EC=5.3.4.1; DE AltName: Full=Thioredoxin-related glycoprotein 1; DE Flags: Precursor; GN Name=PDI1; Synonyms=MFP1, TRG1; OrderedLocusNames=YCL043C; GN ORFNames=YCL313, YCL43C; 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], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 26786 / X2180-1A, and TM5; RX PubMed=1761527; DOI=10.1093/oxfordjournals.jbchem.a123576; RA Tachikawa H., Miura T., Katakura Y., Mizunaga T.; RT "Molecular structure of a yeast gene, PDI1, encoding protein disulfide RT isomerase that is essential for cell growth."; RL J. Biochem. 110:306-313(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2063627; DOI=10.1002/yea.320070212; RA Scherens B., Dubois E., Messenguy F.; RT "Determination of the sequence of the yeast YCL313 gene localized on RT chromosome III. Homology with the protein disulfide isomerase (PDI gene RT product) of other organisms."; RL Yeast 7:185-193(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1840696; DOI=10.1073/pnas.88.10.4453; RA Lamantia M., Miura T., Tachikawa H., Kaplan H.A., Lennarz W.J., RA Mizunaga T.; RT "Glycosylation site binding protein and protein disulfide isomerase are RT identical and essential for cell viability in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4453-4457(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1761554; DOI=10.1016/s0021-9258(18)54265-4; RA Guenther R., Braeuer C., Janetzky B., Foerster H.H., Ehbrecht I.M., RA Lehle L., Kuentzel H.; RT "The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes RT a lumenal endoplasmic reticulum glycoprotein involved in the maturation of RT vacuolar carboxypeptidase."; RL J. Biol. Chem. 266:24557-24563(1991). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1761235; DOI=10.1016/0378-1119(91)90490-3; RA Farquhar R., Honey N., Murant S.J., Bossier P., Schultz L., Montogomery D., RA Ellis R.W., Freedman R.B., Tuite M.F.; RT "Protein disulfide isomerase is essential for viability in Saccharomyces RT cerevisiae."; RL Gene 108:81-89(1991). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1523890; DOI=10.1002/yea.320080709; RA Scherens B., Messenguy F., Gigot D., Dubois E.; RT "The complete sequence of a 9,543 bp segment on the left arm of chromosome RT III reveals five open reading frames including glucokinase and the protein RT disulfide isomerase."; RL Yeast 8:577-586(1992). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1574125; DOI=10.1038/357038a0; RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., RA Richterich P., Roberts A.B., Rodriguez F., Sanz E., RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., RA Sgouros J.G.; RT "The complete DNA sequence of yeast chromosome III."; RL Nature 357:38-46(1992). RN [8] 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 [9] RP FUNCTION, AND INTERACTION WITH EPS1 AND KAR2. RX PubMed=16002399; DOI=10.1074/jbc.m503377200; RA Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T., RA Kikuchi M.; RT "Interactions among yeast protein-disulfide isomerase proteins and RT endoplasmic reticulum chaperone proteins influence their activities."; RL J. Biol. Chem. 280:31438-31441(2005). RN [10] RP FUNCTION, AND INTERACTION WITH MNL1. RX PubMed=19124653; DOI=10.1083/jcb.200809198; RA Clerc S., Hirsch C., Oggier D.M., Deprez P., Jakob C., Sommer T., Aebi M.; RT "Htm1 protein generates the N-glycan signal for glycoprotein degradation in RT the endoplasmic reticulum."; RL J. Cell Biol. 184:159-172(2009). RN [11] RP FUNCTION, AND INTERACTION WITH MNL1. RX PubMed=21700223; DOI=10.1016/j.molcel.2011.04.027; RA Gauss R., Kanehara K., Carvalho P., Ng D.T., Aebi M.; RT "A complex of Pdi1p and the mannosidase Htm1p initiates clearance of RT unfolded glycoproteins from the endoplasmic reticulum."; RL Mol. Cell 42:782-793(2011). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-522, AND DISULFIDE BONDS. RX PubMed=16413482; DOI=10.1016/j.cell.2005.10.044; RA Tian G., Xiang S., Noiva R., Lennarz W.J., Schindelin H.; RT "The crystal structure of yeast protein disulfide isomerase suggests RT cooperativity between its active sites."; RL Cell 124:61-73(2006). CC -!- FUNCTION: Protein disulfide isomerase of ER lumen required for CC formation of disulfide bonds in secretory and cell-surface proteins and CC which unscrambles non-native disulfide bonds. Forms a complex with MNL1 CC to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to CC Man7GlcNAc2, promoting degradation in unfolded protein response. CC {ECO:0000269|PubMed:16002399, ECO:0000269|PubMed:19124653, CC ECO:0000269|PubMed:21700223}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; CC EC=5.3.4.1; CC -!- SUBUNIT: Interacts with EPS1, KAR2 and MNL1. CC {ECO:0000269|PubMed:16002399, ECO:0000269|PubMed:19124653, CC ECO:0000269|PubMed:21700223}. CC -!- INTERACTION: CC P17967; P38888: MNL1; NbExp=4; IntAct=EBI-13012, EBI-24256; CC P17967; P61823: RNASE1; Xeno; NbExp=2; IntAct=EBI-13012, EBI-908364; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138}. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D00842; BAA00723.1; -; Genomic_DNA. DR EMBL; X57712; CAA40883.1; -; Genomic_DNA. DR EMBL; M62815; AAA34848.1; -; Genomic_DNA. DR EMBL; X52313; CAA36550.1; -; Genomic_DNA. DR EMBL; M76982; AAA35169.1; -; Genomic_DNA. DR EMBL; X54535; CAA38402.1; -; Genomic_DNA. DR EMBL; X59720; CAA42373.1; -; Genomic_DNA. DR EMBL; BK006937; DAA07442.1; -; Genomic_DNA. DR PIR; JX0182; ISBYSS. DR RefSeq; NP_009887.1; NM_001178688.1. DR PDB; 2B5E; X-ray; 2.40 A; A=23-522. DR PDB; 3BOA; X-ray; 3.70 A; A=23-522. DR PDBsum; 2B5E; -. DR PDBsum; 3BOA; -. DR AlphaFoldDB; P17967; -. DR SMR; P17967; -. DR BioGRID; 30941; 393. DR ComplexPortal; CPX-1283; HTM1-PDI1 exomannosidase complex. DR DIP; DIP-4978N; -. DR IntAct; P17967; 22. DR MINT; P17967; -. DR STRING; 4932.YCL043C; -. DR GlyCosmos; P17967; 5 sites, No reported glycans. DR GlyGen; P17967; 5 sites. DR iPTMnet; P17967; -. DR MaxQB; P17967; -. DR PaxDb; 4932-YCL043C; -. DR PeptideAtlas; P17967; -. DR EnsemblFungi; YCL043C_mRNA; YCL043C; YCL043C. DR GeneID; 850314; -. DR KEGG; sce:YCL043C; -. DR AGR; SGD:S000000548; -. DR SGD; S000000548; PDI1. DR VEuPathDB; FungiDB:YCL043C; -. DR eggNOG; KOG0190; Eukaryota. DR GeneTree; ENSGT00940000168753; -. DR HOGENOM; CLU_025879_5_0_1; -. DR InParanoid; P17967; -. DR OMA; FFGMKKD; -. DR OrthoDB; 5399045at2759; -. DR BioCyc; YEAST:YCL043C-MONOMER; -. DR BRENDA; 5.3.4.1; 984. DR Reactome; R-SCE-264876; Insulin processing. DR Reactome; R-SCE-901042; Calnexin/calreticulin cycle. DR BioGRID-ORCS; 850314; 10 hits in 10 CRISPR screens. DR ChiTaRS; PDI1; yeast. DR EvolutionaryTrace; P17967; -. DR PRO; PR:P17967; -. DR Proteomes; UP000002311; Chromosome III. DR RNAct; P17967; Protein. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:SGD. DR GO; GO:0106055; C:mannosyl-oligosaccharide 1,2-alpha-mannosidase complex; IPI:ComplexPortal. DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:SGD. DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:SGD. DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD. DR GO; GO:1904382; P:mannose trimming involved in glycoprotein ERAD pathway; IDA:SGD. DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IDA:ComplexPortal. DR GO; GO:0036508; P:protein alpha-1,2-demannosylation; IDA:SGD. DR GO; GO:0006457; P:protein folding; IMP:SGD. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central. DR CDD; cd02961; PDI_a_family; 1. DR CDD; cd02995; PDI_a_PDI_a'_C; 1. DR CDD; cd02982; PDI_b'_family; 1. DR CDD; cd02981; PDI_b_family; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 4. DR InterPro; IPR005792; Prot_disulphide_isomerase. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR01130; ER_PDI_fam; 1. DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1. DR PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1. DR Pfam; PF00085; Thioredoxin; 2. DR Pfam; PF13848; Thioredoxin_6; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 4. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 2. DR PROSITE; PS51352; THIOREDOXIN_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Isomerase; Redox-active center; KW Reference proteome; Repeat; Signal. FT SIGNAL 1..28 FT /note="Or 22" FT /evidence="ECO:0000255" FT CHAIN 29..522 FT /note="Protein disulfide-isomerase" FT /id="PRO_0000034218" FT DOMAIN 29..141 FT /note="Thioredoxin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT DOMAIN 356..485 FT /note="Thioredoxin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT REGION 497..522 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 519..522 FT /note="Prevents secretion from ER" FT COMPBIAS 501..522 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 61 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 64 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 406 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 409 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT SITE 62 FT /note="Contributes to redox potential value" FT /evidence="ECO:0000250" FT SITE 63 FT /note="Contributes to redox potential value" FT /evidence="ECO:0000250" FT SITE 126 FT /note="Lowers pKa of C-terminal Cys of first active site" FT /evidence="ECO:0000250" FT SITE 407 FT /note="Contributes to redox potential value" FT /evidence="ECO:0000250" FT SITE 408 FT /note="Contributes to redox potential value" FT /evidence="ECO:0000250" FT SITE 471 FT /note="Lowers pKa of C-terminal Cys of second active site" FT /evidence="ECO:0000250" FT CARBOHYD 82 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 117 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 155 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 174 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 425 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 61..64 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691, FT ECO:0000269|PubMed:16413482" FT DISULFID 406..409 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691, FT ECO:0000269|PubMed:16413482" FT CONFLICT 33..52 FT /note="AVVKLATDSFNEYIQSHDLV -> LSLSWPPTLSMNTFSRTTWW (in FT Ref. 3; AAA34848)" FT /evidence="ECO:0000305" FT CONFLICT 83 FT /note="I -> V (in Ref. 4; CAA36550/AAA35169)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="S -> R (in Ref. 5; CAA38402)" FT /evidence="ECO:0000305" FT CONFLICT 143 FT /note="V -> S (in Ref. 4)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="Missing (in Ref. 4)" FT /evidence="ECO:0000305" FT CONFLICT 168 FT /note="K -> E (in Ref. 4; CAA36550/AAA35169)" FT /evidence="ECO:0000305" FT CONFLICT 197 FT /note="D -> E (in Ref. 3; AAA34848)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="V -> R (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 226 FT /note="A -> V (in Ref. 4; CAA36550/AAA35169)" FT /evidence="ECO:0000305" FT CONFLICT 333 FT /note="E -> S (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="S -> P (in Ref. 3; AAA34848)" FT /evidence="ECO:0000305" FT CONFLICT 455 FT /note="L -> F (in Ref. 3; AAA34848)" FT /evidence="ECO:0000305" FT CONFLICT 458 FT /note="G -> S (in Ref. 4; CAA36550/AAA35169)" FT /evidence="ECO:0000305" FT CONFLICT 505 FT /note="A -> AEADAEAEA (in Ref. 4 and 5)" FT /evidence="ECO:0000305" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 42..46 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 50..57 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 62..77 FT /evidence="ECO:0007829|PDB:2B5E" FT TURN 78..82 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:2B5E" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 94..99 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 104..112 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 128..138 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 149..155 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 171..183 FT /evidence="ECO:0007829|PDB:2B5E" FT TURN 184..187 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 189..194 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 220..223 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 226..236 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 246..254 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 259..266 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 267..283 FT /evidence="ECO:0007829|PDB:2B5E" FT TURN 284..287 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 301..304 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 311..318 FT /evidence="ECO:0007829|PDB:2B5E" FT TURN 319..322 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 332..336 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 346..358 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 377..381 FT /evidence="ECO:0007829|PDB:2B5E" FT TURN 383..385 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 386..391 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 397..402 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 407..426 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 431..436 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 437..439 FT /evidence="ECO:0007829|PDB:2B5E" FT STRAND 448..456 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 473..483 FT /evidence="ECO:0007829|PDB:2B5E" FT HELIX 490..501 FT /evidence="ECO:0007829|PDB:2B5E" SQ SEQUENCE 522 AA; 58227 MW; 69CF3E05D7F74C94 CRC64; MKFSAGAVLS WSSLLLASSV FAQQEAVAPE DSAVVKLATD SFNEYIQSHD LVLAEFFAPW CGHCKNMAPE YVKAAETLVE KNITLAQIDC TENQDLCMEH NIPGFPSLKI FKNSDVNNSI DYEGPRTAEA IVQFMIKQSQ PAVAVVADLP AYLANETFVT PVIVQSGKID ADFNATFYSM ANKHFNDYDF VSAENADDDF KLSIYLPSAM DEPVVYNGKK ADIADADVFE KWLQVEALPY FGEIDGSVFA QYVESGLPLG YLFYNDEEEL EEYKPLFTEL AKKNRGLMNF VSIDARKFGR HAGNLNMKEQ FPLFAIHDMT EDLKYGLPQL SEEAFDELSD KIVLESKAIE SLVKDFLKGD ASPIVKSQEI FENQDSSVFQ LVGKNHDEIV NDPKKDVLVL YYAPWCGHCK RLAPTYQELA DTYANATSDV LIAKLDHTEN DVRGVVIEGY PTIVLYPGGK KSESVVYQGS RSLDSLFDFI KENGHFDVDG KALYEEAQEK AAEEADADAE LADEEDAIHD EL //