ID   PEP5_YEAST              Reviewed;        1029 AA.
AC   P12868; D6W057;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=E3 ubiquitin-protein ligase PEP5 {ECO:0000305|PubMed:22570702};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:22570702};
DE   AltName: Full=Carboxypeptidase Y-deficient protein 5 {ECO:0000303|PubMed:3062374};
DE   AltName: Full=Histone E3 ligase PEP5 {ECO:0000303|PubMed:22570702};
DE   AltName: Full=RING-type E3 ubiquitin transferase PEP5 {ECO:0000305};
DE   AltName: Full=Vacuolar biogenesis protein END1 {ECO:0000303|PubMed:3524852};
DE   AltName: Full=Vacuolar morphogenesis protein 1 {ECO:0000303|PubMed:1526998};
DE   AltName: Full=Vacuolar protein sorting-associated protein 11 {ECO:0000303|PubMed:3062374};
DE   AltName: Full=Vacuolar protein-targeting protein 11 {ECO:0000303|PubMed:3062374};
GN   Name=PEP5 {ECO:0000303|PubMed:3062374};
GN   Synonyms=END1 {ECO:0000303|PubMed:3524852}, VAM1
GN   {ECO:0000303|PubMed:1526998}, VPL9 {ECO:0000303|PubMed:2676511}, VPS11
GN   {ECO:0000303|PubMed:3062374}, VPT11 {ECO:0000303|PubMed:3062374};
GN   OrderedLocusNames=YMR231W; ORFNames=YM9959.13;
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].
RX   PubMed=2204580; DOI=10.1093/genetics/125.4.739;
RA   Woolford C.A., Dixon C.K., Manolson M.F., Wright R., Jones E.W.;
RT   "Isolation and characterization of PEP5, a gene essential for vacuolar
RT   biogenesis in Saccharomyces cerevisiae.";
RL   Genetics 125:739-752(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2670552; DOI=10.1002/j.1460-2075.1989.tb03515.x;
RA   Dulic V., Riezman H.;
RT   "Characterization of the END1 gene required for vacuole biogenesis and
RT   gluconeogenic growth of budding yeast.";
RL   EMBO J. 8:1349-1359(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
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   [5]
RP   IDENTIFICATION.
RX   PubMed=320092; DOI=10.1093/genetics/85.1.23;
RA   Jones E.W.;
RT   "Proteinase mutants of Saccharomyces cerevisiae.";
RL   Genetics 85:23-33(1977).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=3524852; DOI=10.1016/0092-8674(86)90656-2;
RA   Chvatchko Y., Howald I., Riezman H.;
RT   "Two yeast mutants defective in endocytosis are defective in pheromone
RT   response.";
RL   Cell 46:355-364(1986).
RN   [7]
RP   FUNCTION.
RX   PubMed=3062374; DOI=10.1128/mcb.8.11.4936-4948.1988;
RA   Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.;
RT   "Protein sorting in Saccharomyces cerevisiae: isolation of mutants
RT   defective in the delivery and processing of multiple vacuolar hydrolases.";
RL   Mol. Cell. Biol. 8:4936-4948(1988).
RN   [8]
RP   IDENTIFICATION.
RX   PubMed=2676511; DOI=10.1002/j.1460-2075.1989.tb03614.x;
RA   Rothman J.H., Howald I., Stevens T.H.;
RT   "Characterization of genes required for protein sorting and vacuolar
RT   function in the yeast Saccharomyces cerevisiae.";
RL   EMBO J. 8:2057-2065(1989).
RN   [9]
RP   IDENTIFICATION.
RX   PubMed=1526998; DOI=10.1016/s0021-9258(19)37012-7;
RA   Wada Y., Ohsumi Y., Anraku Y.;
RT   "Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I.
RT   Isolation and characterization of two classes of vam mutants.";
RL   J. Biol. Chem. 267:18665-18670(1992).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH PEP3 AND PEP7.
RX   PubMed=10978279; DOI=10.1093/genetics/156.1.105;
RA   Srivastava A., Woolford C.A., Jones E.W.;
RT   "Pep3p/Pep5p complex: a putative docking factor at multiple steps of
RT   vesicular transport to the vacuole of Saccharomyces cerevisiae.";
RL   Genetics 156:105-122(2000).
RN   [11]
RP   IDENTIFICATION IN THE HOPS COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=10944212; DOI=10.1073/pnas.97.17.9402;
RA   Seals D.F., Eitzen G., Margolis N., Wickner W.T., Price A.;
RT   "A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required
RT   for homotypic vacuole fusion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9402-9407(2000).
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   IDENTIFICATION IN THE HOPS COMPLEX, FUNCTION OF THE HOPS COMPLEX, AND
RP   INTERACTION WITH VAM7.
RX   PubMed=16601699; DOI=10.1038/sj.emboj.7601051;
RA   Stroupe C., Collins K.M., Fratti R.A., Wickner W.;
RT   "Purification of active HOPS complex reveals its affinities for
RT   phosphoinositides and the SNARE Vam7p.";
RL   EMBO J. 25:1579-1589(2006).
RN   [14]
RP   IDENTIFICATION IN THE CORVET COMPLEX.
RX   PubMed=17488625; DOI=10.1016/j.devcel.2007.03.006;
RA   Peplowska K., Markgraf D.F., Ostrowicz C.W., Bange G., Ungermann C.;
RT   "The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21
RT   and is involved in endo-lysosomal biogenesis.";
RL   Dev. Cell 12:739-750(2007).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [17]
RP   FUNCTION, INTERACTION WITH UBC4, AND INTERACTION WITH HISTONES H3 AND H4.
RX   PubMed=22570702; DOI=10.1371/journal.pone.0036295;
RA   Singh R.K., Gonzalez M., Kabbaj M.H., Gunjan A.;
RT   "Novel E3 ubiquitin ligases that regulate histone protein levels in the
RT   budding yeast Saccharomyces cerevisiae.";
RL   PLoS ONE 7:E36295-E36295(2012).
CC   -!- FUNCTION: Required for vacuolar biogenesis and for trafficking of
CC       hydrolase precursors to the vacuole. Mediates transport at the vacuolar
CC       membrane where it may be responsible for tethering transport vesicles
CC       on the target membranes. It is required for gluconeogenic growth of
CC       yeast. Acts as a component of the HOPS complex that acts during the
CC       docking stage of vacuole fusion. HOPS is an effector for the vacuolar
CC       Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It
CC       remains bound to SNARE complexes after vacuole fusion (PubMed:3062374,
CC       PubMed:10978279, PubMed:10944212, PubMed:16601699). Acts as a component
CC       of the CORVET complex that is required for transport between endosome
CC       and vacuole. CORVET is an effector for the endosomal Rab GTPase VPS21
CC       (PubMed:17488625). Probable ubiquitin-protein ligase involved in the
CC       degradation-related ubiquitination of histones. Contributes to the
CC       post-translational regulation of histone protein levels by
CC       polyubiquitination of excess histones for subsequent degradation
CC       (PubMed:22570702). {ECO:0000269|PubMed:10944212,
CC       ECO:0000269|PubMed:10978279, ECO:0000269|PubMed:16601699,
CC       ECO:0000269|PubMed:17488625, ECO:0000269|PubMed:22570702,
CC       ECO:0000269|PubMed:3062374}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:22570702};
CC   -!- SUBUNIT: Component of the homotypic vacuole fusion and vacuole protein
CC       sorting (HOPS) complex, which is composed of a core of the 4 class C
CC       Vps proteins PEP5/VPS11, PEP3/VPS18, VPS16, VPS33 associated to
CC       VAM6/VPS39 and VPS41/VAM2. HOPS associates with phosphoinositides and
CC       the PX domain of VAM7. Component of the class C core vacuole/endosome
CC       tethering (CORVET) complex, which is composed of a core of the 4 class
CC       C Vps proteins PEP5/VPS11, PEP3/VPS18, VPS16, VPS33 associated to
CC       VPS3/PEP6 and VPS8. Interacts with PEP3, PEP7 and VAM7. Interacts with
CC       the E2 ubiquitin-conjugating enzyme UBC4 and histones H3 and H4.
CC       {ECO:0000269|PubMed:10944212, ECO:0000269|PubMed:10978279,
CC       ECO:0000269|PubMed:16601699, ECO:0000269|PubMed:17488625,
CC       ECO:0000269|PubMed:22570702}.
CC   -!- INTERACTION:
CC       P12868; P27801: PEP3; NbExp=6; IntAct=EBI-6450, EBI-13130;
CC       P12868; P20795: VPS33; NbExp=5; IntAct=EBI-6450, EBI-20395;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10944212};
CC       Peripheral membrane protein {ECO:0000269|PubMed:10944212}; Cytoplasmic
CC       side {ECO:0000269|PubMed:10944212}.
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VPS11 family. {ECO:0000305}.
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DR   EMBL; X54466; CAA38348.1; -; Genomic_DNA.
DR   EMBL; X15355; CAA33413.1; -; Genomic_DNA.
DR   EMBL; Z49939; CAA90202.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10131.1; -; Genomic_DNA.
DR   PIR; S57598; S57598.
DR   RefSeq; NP_013958.1; NM_001182738.1.
DR   PDB; 7ZU0; EM; 4.40 A; A=1-1029.
DR   PDB; 8CUK; X-ray; 2.22 A; A/B/C=1-350.
DR   PDBsum; 7ZU0; -.
DR   PDBsum; 8CUK; -.
DR   EMDB; EMD-14964; -.
DR   EMDB; EMD-2280; -.
DR   SMR; P12868; -.
DR   BioGRID; 35409; 92.
DR   ComplexPortal; CPX-1625; HOPS complex.
DR   ComplexPortal; CPX-1626; CORVET complex.
DR   DIP; DIP-4409N; -.
DR   IntAct; P12868; 14.
DR   MINT; P12868; -.
DR   STRING; 4932.YMR231W; -.
DR   iPTMnet; P12868; -.
DR   MaxQB; P12868; -.
DR   PaxDb; 4932-YMR231W; -.
DR   PeptideAtlas; P12868; -.
DR   EnsemblFungi; YMR231W_mRNA; YMR231W; YMR231W.
DR   GeneID; 855271; -.
DR   KEGG; sce:YMR231W; -.
DR   AGR; SGD:S000004844; -.
DR   SGD; S000004844; PEP5.
DR   VEuPathDB; FungiDB:YMR231W; -.
DR   eggNOG; KOG2114; Eukaryota.
DR   GeneTree; ENSGT00940000153635; -.
DR   HOGENOM; CLU_001287_0_0_1; -.
DR   InParanoid; P12868; -.
DR   OMA; ENECPAC; -.
DR   OrthoDB; 5491867at2759; -.
DR   BioCyc; YEAST:G3O-32912-MONOMER; -.
DR   BioGRID-ORCS; 855271; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P12868; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P12868; Protein.
DR   GO; GO:0033263; C:CORVET complex; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0030897; C:HOPS complex; IPI:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; IGI:SGD.
DR   GO; GO:0036205; P:histone catabolic process; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IGI:SGD.
DR   GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR   GO; GO:0035542; P:regulation of SNARE complex assembly; IDA:SGD.
DR   GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:ComplexPortal.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR   GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   GO; GO:0099022; P:vesicle tethering; IDA:SGD.
DR   CDD; cd16688; RING-H2_Vps11; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR016528; VPS11.
DR   InterPro; IPR024763; VPS11_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR   Pfam; PF12451; VPS11_C; 1.
DR   PIRSF; PIRSF007860; VPS11; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Transferase; Transport; Ubl conjugation pathway;
KW   Vacuole; Zinc; Zinc-finger.
FT   CHAIN           1..1029
FT                   /note="E3 ubiquitin-protein ligase PEP5"
FT                   /id="PRO_0000055995"
FT   REPEAT          406..583
FT                   /note="CHCR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   ZN_FING         928..973
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          637..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        37
FT                   /note="A -> R (in Ref. 2; CAA33413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619..625
FT                   /note="VFYSYKT -> MFFTVTKH (in Ref. 2; CAA33413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        769..770
FT                   /note="TK -> KQ (in Ref. 2; CAA33413)"
FT                   /evidence="ECO:0000305"
FT   STRAND          12..18
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   TURN            20..23
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   TURN            50..52
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          76..83
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          97..105
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          117..122
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          140..147
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          165..172
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          188..194
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          213..219
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   TURN            231..234
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          235..239
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          241..248
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          253..257
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          270..280
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          298..305
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   TURN            306..309
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          310..319
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          321..327
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          334..339
FT                   /evidence="ECO:0007829|PDB:8CUK"
FT   STRAND          342..349
FT                   /evidence="ECO:0007829|PDB:8CUK"
SQ   SEQUENCE   1029 AA;  117478 MW;  E5216AD3C285CF34 CRC64;
     MSLSSWRQFQ LFENIPIRDP NFGGDSLLYS DPTLCAATIV DPQTLIIAVN SNIIKVVKLN
     QSQVIHEFQS FPHDFQITFL KVINGEFLVA LAESIGKPSL IRVYKLEKLP NREQLYHSQV
     ELKNGNNTYP ISVVSISNDL SCIVVGFING KIILIRGDIS RDRGSQQRII YEDPSKEPIT
     ALFLNNDATA CFAATTSRIL LFNTTGRNRG RPSLVLNSKN GLDLNCGSFN PATNEFICCL
     SNFIEFFSSS GKKHQFAFDL SLRKRIFCVD KDHILIVTEE TGVPTTSISV NELSPTIINR
     IFIIDAKNKI ISLNFVVSSA IIDIFSTSQS GKNITYLLTS EGVMHRITPK SLENQINIII
     QKELYPFALQ LAKQHSLSPL DVQEIHKKYG DYLFKKGLRK EATDQYIQCL DVVETSEIIS
     KFGVKEVPDP ESMRNLADYL WSLIKNSISQ RDHVTLLLIV LIKLKDVEGI DTFIQHFDRK
     GIWNEGVVMD DMDDVTFFYS DNDFFDLDLI LELMKESDFK RLSYRLAKKY SKDSLIIVDI
     LLNLLHNPVK AIKYIKSLPI DETLRCLVTY SKKLLEESPN ETNALLIEVF TGKFKPSTFE
     VDLDRRDTTG DFSENIRTVF YSYKTFFNYM NSNGTSDAMS ESSEASHEHE EPTYHPPKPS
     IVFSSFVTKP FEFVVFLEAC LACYQQYEGF DEDRQVILTT LYDLYLNLAQ NDVPERIDDW
     RSRATGVLRE SNKLVYSAAS NNTSKRVDNS IMLLISHMDQ SSASAKDKTK IDIASFANDN
     PEMDLLSTFR AMTLNEEPST CLKFLEKYGT EEPKLLQVAL SYFVSNKLIF KEMGGNEVLK
     EKVLRPIIEG ERMPLLDIIK ALSRTNVAHF GLIQDIIIDH VKTEDTEIKR NEKLIESYDK
     ELKEKNKKLK NTINSDQPLH VPLKNQTCFM CRLTLDIPVV FFKCGHIYHQ HCLNEEEDTL
     ESERKLFKCP KCLVDLETSN KLFEAQHEVV EKNDLLNFAL NSEEGSRDRF KVITEFLGRG
     AISYSDITI
//