CBPY_YEAST
ID CBPY_YEAST Reviewed; 532 AA.
AC P00729; D6W0C4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Carboxypeptidase Y {ECO:0000303|Ref.4};
DE Short=CPD-Y {ECO:0000303|PubMed:8679540};
DE Short=cpY;
DE EC=3.4.16.5 {ECO:0000269|PubMed:17408619, ECO:0000269|PubMed:8679540};
DE AltName: Full=Carboxypeptidase YSCY;
DE Flags: Precursor;
GN Name=PRC1 {ECO:0000303|PubMed:3028649};
GN OrderedLocusNames=YMR297W {ECO:0000312|SGD:S000004912};
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=3028649; DOI=10.1016/0092-8674(87)90085-7;
RA Valls L.A., Hunter C.P., Rothman J.H., Stevens T.H.;
RT "Protein sorting in yeast: the localization determinant of yeast vacuolar
RT carboxypeptidase Y resides in the propeptide.";
RL Cell 48:887-897(1987).
RN [2]
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 [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 112-532.
RX DOI=10.1007/BF02907793;
RA Martin B.M., Svendsen I., Viswanatha T., Johansen J.T.;
RT "Amino acid sequence of carboxypeptidase Y. I. Peptides from cleavage with
RT cyanogen bromide.";
RL Carlsberg Res. Commun. 47:1-13(1982).
RN [5]
RP SEQUENCE REVISION, AND ACTIVE SITE SER-257.
RX DOI=10.1007/BF02907496;
RA Breddam K., Svendsen I.;
RT "Identification of methionyl and cysteinyl residues in the substrate
RT binding site of carboxypeptidase Y.";
RL Carlsberg Res. Commun. 49:639-645(1984).
RN [6]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=348476; DOI=10.1111/j.1432-1033.1978.tb12275.x;
RA Hasilik A., Tanner W.;
RT "Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y.
RT Conversion of precursor into the enzyme.";
RL Eur. J. Biochem. 85:599-608(1978).
RN [7]
RP ACTIVE SITE HIS-508.
RX PubMed=2639680; DOI=10.1007/bf02904470;
RA Bech L.M., Breddam K.;
RT "Inactivation of carboxypeptidase Y by mutational removal of the putative
RT essential histidyl residue.";
RL Carlsberg Res. Commun. 54:165-171(1989).
RN [8]
RP MUTAGENESIS OF HIS-508.
RX PubMed=7904479; DOI=10.1021/bi00168a016;
RA Mortensen U.H., Remington S.J., Breddam K.;
RT "Site-directed mutagenesis on (serine) carboxypeptidase Y. A hydrogen bond
RT network stabilizes the transition state by interaction with the C-terminal
RT carboxylate group of the substrate.";
RL Biochemistry 33:508-517(1994).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8679540; DOI=10.1021/bi952758e;
RA Stennicke H.R., Mortensen U.H., Breddam K.;
RT "Studies on the hydrolytic properties of (serine) carboxypeptidase Y.";
RL Biochemistry 35:7131-7141(1996).
RN [10]
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 [11]
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 [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=17408619; DOI=10.1016/j.febslet.2007.03.039;
RA Wuenschmann J., Beck A., Meyer L., Letzel T., Grill E., Lendzian K.J.;
RT "Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 581:1681-1687(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19897216; DOI=10.1016/j.phytochem.2009.09.034;
RA Wuenschmann J., Krajewski M., Letzel T., Huber E.M., Ehrmann A., Grill E.,
RA Lendzian K.J.;
RT "Dissection of glutathione conjugate turnover in yeast.";
RL Phytochemistry 71:54-61(2010).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=23708375; DOI=10.1007/s00709-013-0510-2;
RA Matsumoto R., Suzuki K., Ohya Y.;
RT "Organelle acidification is important for localisation of vacuolar proteins
RT in Saccharomyces cerevisiae.";
RL Protoplasma 250:1283-1293(2013).
RN [15]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25214228; DOI=10.1007/s10529-014-1667-2;
RA Yu X., Zhai C., Zhong X., Tang W., Wang X., Yang H., Chen W., Ma L.;
RT "High-level expression and characterization of carboxypeptidase Y from
RT Saccharomyces cerevisiae in Pichia pastoris GS115.";
RL Biotechnol. Lett. 37:161-167(2015).
RN [16]
RP GLYCOSYLATION AT ASN-124; ASN-198; ASN-279 AND ASN-479.
RX PubMed=28189789; DOI=10.1016/j.ijbiomac.2017.02.026;
RA Gnanesch Kumar B.S., Surolia A.;
RT "N-glycosylation analysis of yeast carboxypeptidase Y reveals the ultimate
RT removal of phosphate from glycans at Asn(368).";
RL Int. J. Biol. Macromol. 98:582-585(2017).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29514932; DOI=10.1091/mbc.e17-08-0516;
RA Parzych K.R., Ariosa A., Mari M., Klionsky D.J.;
RT "A newly characterized vacuolar serine carboxypeptidase, Atg42/Ybr139w, is
RT required for normal vacuole function and the terminal steps of autophagy in
RT the yeast Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 29:1089-1099(2018).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 112-532, GLYCOSYLATION AT
RP ASN-198; ASN-279 AND ASN-479, AND DISULFIDE BONDS.
RX PubMed=7727362; DOI=10.1021/bi00203a007;
RA Endrizzi J.A., Breddam K., Remington S.J.;
RT "2.8-A structure of yeast serine carboxypeptidase.";
RL Biochemistry 33:11106-11120(1994).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 112-532, GLYCOSYLATION AT
RP ASN-198; ASN-279 AND ASN-479, AND DISULFIDE BONDS.
RX PubMed=15713484; DOI=10.1016/j.jmb.2004.12.051;
RA Mima J., Hayashida M., Fujii T., Narita Y., Hayashi R., Ueda M., Hata Y.;
RT "Structure of the carboxypeptidase Y inhibitor IC in complex with the
RT cognate proteinase reveals a novel mode of the proteinase-protein inhibitor
RT interaction.";
RL J. Mol. Biol. 346:1323-1334(2005).
CC -!- FUNCTION: Vacuolar serine-type carboxypeptidase involved in degradation
CC of small peptides (PubMed:8679540). Digests preferentially peptides
CC containing an aliphatic or hydrophobic residue in P1' position, as well
CC as methionine, leucine or phenylalanine in P1 position of ester
CC substrate (PubMed:8679540). Also plays a role in breakdown of the
CC autophagic body and the autophagosome-dependent protein synthesis
CC (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis
CC from glutathione (GSH) by cleaving the Gly from GSH and form the PC-
CC peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also
CC involved in resistance to xenobiotics via the degradation of
CC glutathione-S-conjugates (PubMed:19897216).
CC {ECO:0000269|PubMed:17408619, ECO:0000269|PubMed:19897216,
CC ECO:0000269|PubMed:29514932, ECO:0000269|PubMed:8679540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity.;
CC EC=3.4.16.5; Evidence={ECO:0000269|PubMed:8679540};
CC -!- ACTIVITY REGULATION: Inhibited by ZPCK.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.021 mM for furylacryloyl-Phe-Leu-OH
CC {ECO:0000269|PubMed:8679540};
CC Note=kcat is 4900 min(-1) with furylacryloyl-Phe-Leu-OH as substrate.
CC {ECO:0000269|PubMed:8679540};
CC pH dependence:
CC Optimum pH is 6.5. Active from pH 4.5 to pH 8.5.
CC {ECO:0000269|PubMed:8679540};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:25214228};
CC -!- INTERACTION:
CC P00729; P38307: DER1; NbExp=2; IntAct=EBI-4153, EBI-5761;
CC P00729; Q08109: HRD1; NbExp=11; IntAct=EBI-4153, EBI-37613;
CC P00729; Q05787: HRD3; NbExp=6; IntAct=EBI-4153, EBI-31647;
CC P00729; P32915: SEC61; NbExp=4; IntAct=EBI-4153, EBI-16400;
CC P00729; Q99220: YOS9; NbExp=2; IntAct=EBI-4153, EBI-34938;
CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23708375, ECO:0000269|PubMed:29514932}. Note=The
CC vacuolar sorting receptor VPS10 is required for the delivery of ATG42
CC to the vacuole lumen. {ECO:0000269|PubMed:29514932}.
CC -!- PTM: Enters the endoplasmic reticulum as an inactive zymogen and is
CC modified by four N-linked core oligosaccharides, giving rise to a
CC precursor known as P1 (67 kDa). As P1 transits through the Golgi,
CC extension of its core oligosaccharides leads to the Golgi-modified P2
CC precursor (69 kDa). P2 is sorted away from secretory proteins at or
CC beyond a late Golgi compartment and is subsequently delivered to the
CC vacuole via a prevacuolar endosome-like compartment. Upon arrival in
CC the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar
CC proteases to yield the enzymatically active mature vacuolar form of CPY
CC (61 kDa). {ECO:0000269|PubMed:348476}.
CC -!- PTM: The four high mannose core N-glycans found in mature CPY are
CC Man(11-15)GlcNAc(2) at Asn-124, Man(8-12)GlcNAc(2) at Asn-198, Man(9-
CC 14)GlcNAc(2) at Asn-279 and phosphorylated Man(12-17)GlcNAc(2) as well
CC as Man(11-16)GlcNAc(2) at Asn-479. {ECO:0000269|PubMed:28189789}.
CC -!- DISRUPTION PHENOTYPE: Leads to vacuolar defects as well as defects in
CC the terminal steps of autophagy, when ATG42 is also deleted
CC (PubMed:29514932). The PCR1/ATG42 double deletion abrogates also the
CC production of phytochelatin and the degradation of glutathione-S-
CC conjugates (PubMed:17408619, PubMed:19897216).
CC {ECO:0000269|PubMed:17408619, ECO:0000269|PubMed:19897216,
CC ECO:0000269|PubMed:29514932}.
CC -!- MISCELLANEOUS: Present with 44000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/COY/";
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DR EMBL; M15482; AAA34902.1; -; Genomic_DNA.
DR EMBL; X80836; CAA56806.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10198.1; -; Genomic_DNA.
DR PIR; A26597; CPBYY.
DR RefSeq; NP_014026.1; NM_001182806.1.
DR PDB; 1CPY; X-ray; 2.60 A; A=112-532.
DR PDB; 1WPX; X-ray; 2.70 A; A=112-532.
DR PDB; 1YSC; X-ray; 2.80 A; A=112-532.
DR PDBsum; 1CPY; -.
DR PDBsum; 1WPX; -.
DR PDBsum; 1YSC; -.
DR AlphaFoldDB; P00729; -.
DR SMR; P00729; -.
DR BioGRID; 35477; 80.
DR DIP; DIP-2394N; -.
DR IntAct; P00729; 17.
DR MINT; P00729; -.
DR STRING; 4932.YMR297W; -.
DR ChEMBL; CHEMBL4295562; -.
DR Allergome; 8267; Sac c Carboxypeptidase Y.
DR ESTHER; yeast-cbpy1; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR iPTMnet; P00729; -.
DR MaxQB; P00729; -.
DR PaxDb; P00729; -.
DR PRIDE; P00729; -.
DR EnsemblFungi; YMR297W_mRNA; YMR297W; YMR297W.
DR GeneID; 855343; -.
DR KEGG; sce:YMR297W; -.
DR SGD; S000004912; PRC1.
DR VEuPathDB; FungiDB:YMR297W; -.
DR eggNOG; KOG1282; Eukaryota.
DR GeneTree; ENSGT00960000189236; -.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; P00729; -.
DR OMA; GDWMKPF; -.
DR BioCyc; MetaCyc:YMR297W-MON; -.
DR BioCyc; YEAST:YMR297W-MON; -.
DR BRENDA; 3.4.16.5; 984.
DR EvolutionaryTrace; P00729; -.
DR PRO; PR:P00729; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P00729; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:CAFA.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:SGD.
DR GO; GO:0016236; P:macroautophagy; IGI:SGD.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IDA:SGD.
DR GO; GO:0031638; P:zymogen activation; IGI:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR008442; Propeptide_carboxypepY.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF05388; Carbpep_Y_N; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Signal; Vacuole;
KW Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..111
FT /note="Mediates translocation across the endoplasmic
FT reticulum, renders the enzyme inactive during transit, and
FT targets the molecule to the vacuole"
FT /evidence="ECO:0000269|Ref.4, ECO:0000305|PubMed:3028649"
FT /id="PRO_0000004293"
FT CHAIN 112..532
FT /note="Carboxypeptidase Y"
FT /id="PRO_0000004294"
FT MOTIF 24..27
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000269|PubMed:3028649"
FT ACT_SITE 257
FT /evidence="ECO:0000269|PubMed:7727362, ECO:0000269|Ref.5"
FT ACT_SITE 449
FT /evidence="ECO:0000305|PubMed:7727362"
FT ACT_SITE 508
FT /evidence="ECO:0000269|PubMed:2639680,
FT ECO:0000305|PubMed:7727362"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.5"
FT BINDING 509
FT /ligand="substrate"
FT /evidence="ECO:0000305|Ref.5"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:28189789"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362"
FT DISULFID 167..409
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:7727362"
FT DISULFID 304..318
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:7727362"
FT DISULFID 328..351
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:7727362"
FT DISULFID 335..344
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:7727362"
FT DISULFID 373..379
FT /evidence="ECO:0000269|PubMed:15713484,
FT ECO:0000269|PubMed:7727362"
FT MUTAGEN 508
FT /note="H->A,R: Inactivates enzyme."
FT /evidence="ECO:0000269|PubMed:7904479"
FT CONFLICT 260..261
FT /note="GH -> HG (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Y -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="G -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1YSC"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 315..338
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 393..398
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1WPX"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 428..436
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 454..463
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:1CPY"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:1CPY"
FT HELIX 515..526
FT /evidence="ECO:0007829|PDB:1CPY"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:1CPY"
SQ SEQUENCE 532 AA; 59802 MW; 7227F3489CBDD952 CRC64;
MKAFTSLLCG LGLSTTLAKA ISLQRPLGLD KDVLLQAAEK FGLDLDLDHL LKELDSNVLD
AWAQIEHLYP NQVMSLETST KPKFPEAIKT KKDWDFVVKN DAIENYQLRV NKIKDPKILG
IDPNVTQYTG YLDVEDEDKH FFFWTFESRN DPAKDPVILW LNGGPGCSSL TGLFFELGPS
SIGPDLKPIG NPYSWNSNAT VIFLDQPVNV GFSYSGSSGV SNTVAAGKDV YNFLELFFDQ
FPEYVNKGQD FHIAGESYAG HYIPVFASEI LSHKDRNFNL TSVLIGNGLT DPLTQYNYYE
PMACGEGGEP SVLPSEECSA MEDSLERCLG LIESCYDSQS VWSCVPATIY CNNAQLAPYQ
RTGRNVYDIR KDCEGGNLCY PTLQDIDDYL NQDYVKEAVG AEVDHYESCN FDINRNFLFA
GDWMKPYHTA VTDLLNQDLP ILVYAGDKDF ICNWLGNKAW TDVLPWKYDE EFASQKVRNW
TASITDEVAG EVKSYKHFTY LRVFNGGHMV PFDVPENALS MVNEWIHGGF SL
