ID   CDH1_YEAST              Reviewed;         566 AA.
AC   P53197; D6VUD5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=APC/C activator protein CDH1;
DE   AltName: Full=CDC20 homolog 1;
DE   AltName: Full=Homolog of CDC twenty 1;
GN   Name=CDH1; Synonyms=HCT1; OrderedLocusNames=YGL003C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   ASSOCIATION WITH THE APC/C COMPLEX, PHOSPHORYLATION BY CDC28, AND
RP   MUTAGENESIS OF THR-12; SER-16; SER-42; THR-157; SER-169; THR-173; THR-176;
RP   SER-227 AND SER-239.
RX   PubMed=9831566; DOI=10.1126/science.282.5394.1721;
RA   Zachariae W., Schwab M., Nasmyth K., Seufert W.;
RT   "Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the
RT   anaphase promoting complex.";
RL   Science 282:1721-1724(1998).
RN   [5]
RP   DEPHOSPHORYLATION BY CDC14.
RX   PubMed=10074450; DOI=10.1016/s0960-9822(99)80111-0;
RA   Jaspersen S.L., Charles J.F., Morgan D.O.;
RT   "Inhibitory phosphorylation of the APC regulator Hct1 is controlled by the
RT   kinase Cdc28 and the phosphatase Cdc14.";
RL   Curr. Biol. 9:227-236(1999).
RN   [6]
RP   FUNCTION AS SPINDLE CHECKPOINT TARGET.
RX   PubMed=10329618; DOI=10.1093/emboj/18.10.2707;
RA   Alexandru G., Zachariae W., Schleiffer A., Nasmyth K.;
RT   "Sister chromatid separation and chromosome re-duplication are regulated by
RT   different mechanisms in response to spindle damage.";
RL   EMBO J. 18:2707-2721(1999).
RN   [7]
RP   FUNCTION, INTERACTION WITH CLB2; CLB3 AND CDC5, AND DOMAIN C-BOX MOTIF.
RX   PubMed=11566880; DOI=10.1093/emboj/20.18.5165;
RA   Schwab M., Neutzner M., Moecker D., Seufert W.;
RT   "Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the
RT   ubiquitin ligase APC.";
RL   EMBO J. 20:5165-5175(2001).
RN   [8]
RP   INTERACTION WITH HSL1.
RX   PubMed=11562348; DOI=10.1101/gad.917901;
RA   Burton J.L., Solomon M.J.;
RT   "D box and KEN box motifs in budding yeast Hsl1p are required for APC-
RT   mediated degradation and direct binding to Cdc20p and Cdh1p.";
RL   Genes Dev. 15:2381-2395(2001).
RN   [9]
RP   FUNCTION IN ASE1 AND CDC20 DEGRADATION.
RX   PubMed=11448992; DOI=10.1083/jcb.200102007;
RA   Huang J.N., Park I., Ellingson E., Littlepage L.E., Pellman D.;
RT   "Activity of the APC(Cdh1) form of the anaphase-promoting complex persists
RT   until S phase and prevents the premature expression of Cdc20p.";
RL   J. Cell Biol. 154:85-94(2001).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MSN5 AND PSE1.
RX   PubMed=12456658; DOI=10.1093/emboj/cdf634;
RA   Jaquenoud M., van Drogen F., Peter M.;
RT   "Cell cycle-dependent nuclear export of Cdh1p may contribute to the
RT   inactivation of APC/C(Cdh1).";
RL   EMBO J. 21:6515-6526(2002).
RN   [11]
RP   PHOSPHORYLATION BY CDC28.
RX   PubMed=14574415; DOI=10.1038/nature02062;
RA   Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA   Shokat K.M., Morgan D.O.;
RT   "Targets of the cyclin-dependent kinase Cdk1.";
RL   Nature 425:859-864(2003).
RN   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Activator protein that regulates the ubiquitin ligase
CC       activity and substrate specificity of the anaphase promoting
CC       complex/cyclosome (APC/C). During telophase and in the subsequent G1
CC       phase of the cell cycle, recognizes and binds proteins containing a
CC       destruction box (D-box) and an additional degradation signal termed the
CC       KEN box including ASE1, CDC20, the B-type cyclins CLB2 and CLB3, the
CC       polo-like kinase CDC5 and HSL1, and recruits them in a C-box-dependent
CC       manner to the APC/C for ubiquitination and subsequent proteolysis.
CC       Required for exit from mitosis, cytokinesis and formation of
CC       prereplicative complexes in G1. Probably is the target of a BUB2-
CC       dependent spindle checkpoint pathway. {ECO:0000269|PubMed:10329618,
CC       ECO:0000269|PubMed:11448992, ECO:0000269|PubMed:11566880}.
CC   -!- SUBUNIT: Associates with the APC/C complex. Interacts with CLB2, CLB3,
CC       CDC5, HSL1, MSN5 and PSE1. {ECO:0000269|PubMed:11562348,
CC       ECO:0000269|PubMed:11566880, ECO:0000269|PubMed:12456658}.
CC   -!- INTERACTION:
CC       P53197; Q08981: ACM1; NbExp=8; IntAct=EBI-23684, EBI-2345174;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12456658}. Nucleus
CC       {ECO:0000269|PubMed:12456658}. Note=Nuclear import and export are
CC       mediated by the importin PSE1 and the exportin MSN5.
CC   -!- DOMAIN: The C-box is required for the association with the APC/C
CC       complex. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at multiple sites by CDC28, probably in its CLB5
CC       bound form, in S, G2 and M phase of the cell cycle, thereby blocking
CC       the association of CDH1 to the APC/C and promoting nuclear export of
CC       CDH1 by MSN5. Dephosphorylated and activated by CDC14 in late anaphase,
CC       which may be necessary for PSE1-dependent nuclear localization.
CC       {ECO:0000269|PubMed:14574415, ECO:0000269|PubMed:9831566}.
CC   -!- SIMILARITY: Belongs to the WD repeat CDC20/Fizzy family. {ECO:0000305}.
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DR   EMBL; Z72525; CAA96703.1; -; Genomic_DNA.
DR   EMBL; AY693078; AAT93097.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08096.1; -; Genomic_DNA.
DR   PIR; S64005; S64005.
DR   RefSeq; NP_011512.1; NM_001180868.1.
DR   PDB; 4BH6; X-ray; 2.90 A; A/B/C/D/E/F/G/H=241-548.
DR   PDB; 5A31; EM; 4.30 A; R=246-546.
DR   PDB; 8A3T; EM; 3.50 A; B=1-566.
DR   PDBsum; 4BH6; -.
DR   PDBsum; 5A31; -.
DR   PDBsum; 8A3T; -.
DR   AlphaFoldDB; P53197; -.
DR   EMDB; EMD-2925; -.
DR   SMR; P53197; -.
DR   BioGRID; 33242; 361.
DR   ComplexPortal; CPX-761; Anaphase-Promoting Complex, CDH1 variant.
DR   DIP; DIP-5915N; -.
DR   ELM; P53197; -.
DR   IntAct; P53197; 22.
DR   MINT; P53197; -.
DR   STRING; 4932.YGL003C; -.
DR   iPTMnet; P53197; -.
DR   MaxQB; P53197; -.
DR   PaxDb; 4932-YGL003C; -.
DR   PeptideAtlas; P53197; -.
DR   EnsemblFungi; YGL003C_mRNA; YGL003C; YGL003C.
DR   GeneID; 852881; -.
DR   KEGG; sce:YGL003C; -.
DR   AGR; SGD:S000002971; -.
DR   SGD; S000002971; CDH1.
DR   VEuPathDB; FungiDB:YGL003C; -.
DR   eggNOG; KOG0305; Eukaryota.
DR   GeneTree; ENSGT00950000183104; -.
DR   HOGENOM; CLU_014831_4_1_1; -.
DR   InParanoid; P53197; -.
DR   OMA; WSKNTDE; -.
DR   OrthoDB; 20041at2759; -.
DR   BioCyc; YEAST:G3O-30527-MONOMER; -.
DR   Reactome; R-SCE-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 852881; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P53197; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53197; Protein.
DR   GO; GO:0005680; C:anaphase-promoting complex; IPI:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR   GO; GO:0030332; F:cyclin binding; IDA:SGD.
DR   GO; GO:1990757; F:ubiquitin ligase activator activity; IDA:SGD.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:SGD.
DR   GO; GO:0010697; P:negative regulation of mitotic spindle pole body separation; IMP:SGD.
DR   GO; GO:1905786; P:positive regulation of anaphase-promoting complex-dependent catabolic process; IMP:SGD.
DR   GO; GO:0120151; P:positive regulation of mitotic actomyosin contractile ring disassembly; IMP:SGD.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:SGD.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:SGD.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:SGD.
DR   GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:SGD.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR033010; Cdc20/Fizzy.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19918; CELL DIVISION CYCLE 20 CDC20 FIZZY -RELATED; 1.
DR   PANTHER; PTHR19918:SF1; FIZZY-RELATED PROTEIN HOMOLOG; 1.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..566
FT                   /note="APC/C activator protein CDH1"
FT                   /id="PRO_0000050904"
FT   REPEAT          258..298
FT                   /note="WD 1"
FT   REPEAT          300..339
FT                   /note="WD 2"
FT   REPEAT          342..379
FT                   /note="WD 3"
FT   REPEAT          383..422
FT                   /note="WD 4"
FT   REPEAT          425..467
FT                   /note="WD 5"
FT   REPEAT          469..510
FT                   /note="WD 6"
FT   REPEAT          513..552
FT                   /note="WD 7"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           55..61
FT                   /note="C-box"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         12
FT                   /note="T->A: Abolishes phosphorylation; when associated
FT                   with A-16; A-42; A-157; A-169; A-173; A-176; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         16
FT                   /note="S->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-42; A-157; A-169; A-173; A-176; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         42
FT                   /note="S->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-157; A-169; A-173; A-176; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         157
FT                   /note="T->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-42; A-169; A-173; A-176; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         169
FT                   /note="S->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-42; A-157; A-173; A-176; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         173
FT                   /note="T->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-42; A-157; A-169; A-176; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         176
FT                   /note="T->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-42; A-157; A-169; A-173; A-227 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         227
FT                   /note="S->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and
FT                   A-239."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   MUTAGEN         239
FT                   /note="S->A: Abolishes phosphorylation; when associated
FT                   with A-12; A-16; A-42; A-157; A-169; A-173; A-176 and
FT                   A-227."
FT                   /evidence="ECO:0000269|PubMed:9831566"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           66..73
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           91..110
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           113..117
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           125..131
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           215..225
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           231..238
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          275..281
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          305..310
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          314..321
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          326..330
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   TURN            331..334
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          335..340
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          347..353
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          356..364
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          366..370
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          373..376
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          378..381
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          388..393
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          395..397
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          399..404
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          409..413
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          420..423
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          430..435
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          437..439
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          442..447
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   TURN            449..451
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          453..458
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   TURN            459..462
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          463..469
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          474..479
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          481..484
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          486..490
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          492..494
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          497..500
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          502..504
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          507..511
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          518..523
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          527..534
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   TURN            535..537
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   STRAND          538..543
FT                   /evidence="ECO:0007829|PDB:4BH6"
FT   HELIX           558..562
FT                   /evidence="ECO:0007829|PDB:8A3T"
SQ   SEQUENCE   566 AA;  62821 MW;  DA6DE5545607906B CRC64;
     MSTNLNPFMN NTPSSSPLKG SESKRVSKRP ISSSSSASLL SSPSRRSRPS TVYGDRYIPS
     RTDIDFNSIV SISSMASVPA LNPSSTEDQV EYQKERQAHE TYNTLLKNEL FGEMLSKDTV
     GSESSIDRIK NTRPSTRGNV HAENTTRHGY ELERVSTPPP EAAGLEEFSP HSTPVTPRRL
     FTSQQDEITR PSSNSVRGAS LLTYQQRKGR RLSAASLLQS QFFDSMSPVR PDSKQLLLSP
     GKQFRQIAKV PYRVLDAPSL ADDFYYSLID WSSTDVLAVA LGKSIFLTDN NTGDVVHLCD
     TENEYTSLSW IGAGSHLAVG QANGLVEIYD VMKRKCIRTL SGHIDRVACL SWNNHVLTSG
     SRDHRILHRD VRMPDPFFET IESHTQEVCG LKWNVADNKL ASGGNDNVVH VYEGTSKSPI
     LTFDEHKAAV KAMAWSPHKR GVLATGGGTA DRRLKIWNVN TSIKMSDIDS GSQICNMVWS
     KNTNELVTSH GYSKYNLTLW DCNSMDPIAI LKGHSFRVLH LTLSNDGTTV VSGAGDETLR
     YWKLFDKPKA KVQPNSLIFD AFNQIR
//