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 27-MAR-2024, entry version 229. 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/"; 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; 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; 86. 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 GlyCosmos; P00729; 4 sites, No reported glycans. DR GlyGen; P00729; 4 sites. DR iPTMnet; P00729; -. DR MaxQB; P00729; -. DR PaxDb; 4932-YMR297W; -. DR PeptideAtlas; P00729; -. DR EnsemblFungi; YMR297W_mRNA; YMR297W; YMR297W. DR GeneID; 855343; -. DR KEGG; sce:YMR297W; -. DR AGR; SGD:S000004912; -. 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 OrthoDB; 1647009at2759; -. DR BioCyc; MetaCyc:YMR297W-MONOMER; -. DR BioCyc; YEAST:YMR297W-MONOMER; -. DR BRENDA; 3.4.16.5; 984. DR Reactome; R-SCE-2132295; MHC class II antigen presentation. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 855343; 2 hits in 10 CRISPR screens. 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; 1.10.287.410; -; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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:SF113; CARBOXYPEPTIDASE Y; 1. DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1. DR Pfam; PF05388; Carbpep_Y_N; 1. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 //