PDI_YEAST
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 03-AUG-2022, entry version 211.
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}.
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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; 308.
DR ComplexPortal; CPX-1283; HTM1-PDI1 exomannosidase complex.
DR DIP; DIP-4978N; -.
DR IntAct; P17967; 22.
DR MINT; P17967; -.
DR STRING; 4932.YCL043C; -.
DR iPTMnet; P17967; -.
DR MaxQB; P17967; -.
DR PaxDb; P17967; -.
DR PRIDE; P17967; -.
DR EnsemblFungi; YCL043C_mRNA; YCL043C; YCL043C.
DR GeneID; 850314; -.
DR KEGG; sce:YCL043C; -.
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; YIAKHAT; -.
DR BioCyc; YEAST:YCL043C-MON; -.
DR BRENDA; 5.3.4.1; 984.
DR Reactome; R-SCE-901042; Calnexin/calreticulin cycle.
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:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
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:1904380; P:endoplasmic reticulum mannose trimming; IDA:ComplexPortal.
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 InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
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
