ID   APC1_YEAST              Reviewed;        1748 AA.
AC   P53886; D6W112;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Anaphase-promoting complex subunit 1;
GN   Name=APC1; OrderedLocusNames=YNL172W; ORFNames=N1677;
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=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 1547.
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   FUNCTION, AND SUBUNIT.
RX   PubMed=8895471; DOI=10.1126/science.274.5290.1201;
RA   Zachariae W., Shin T.H., Galova M., Obermaier B., Nasmyth K.;
RT   "Identification of subunits of the anaphase-promoting complex of
RT   Saccharomyces cerevisiae.";
RL   Science 274:1201-1204(1996).
RN   [4]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH MND2.
RX   PubMed=12609981; DOI=10.1074/jbc.m213109200;
RA   Hall M.C., Torres M.P., Schroeder G.K., Borchers C.H.;
RT   "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-
RT   promoting complex.";
RL   J. Biol. Chem. 278:16698-16705(2003).
RN   [5]
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   [6]
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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1462, 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: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC       that controls progression through mitosis and the G1 phase of the cell
CC       cycle. The APC/C is thought to confer substrate specificity and, in the
CC       presence of ubiquitin-conjugating E2 enzymes, it catalyzes the
CC       formation of protein-ubiquitin conjugates that are subsequently
CC       degraded by the 26S proteasome. In early mitosis, the APC/C is
CC       activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5,
CC       and other anaphase inhibitory proteins for proteolysis, thereby
CC       triggering the separation of sister chromatids at the metaphase-to-
CC       anaphase transition. In late mitosis and in G1, degradation of CLB5
CC       allows activation of the APC/C by CDH1, which is needed to destroy
CC       CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and
CC       creating the low CDK state necessary for cytokinesis and for reforming
CC       prereplicative complexes in G1 prior to another round of replication.
CC       {ECO:0000269|PubMed:12609981, ECO:0000269|PubMed:8895471}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 13 subunits that stay
CC       tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5,
CC       APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC1
CC       interacts directly with MND2. {ECO:0000269|PubMed:12609981,
CC       ECO:0000269|PubMed:8895471}.
CC   -!- INTERACTION:
CC       P53886; P53886: APC1; NbExp=2; IntAct=EBI-29017, EBI-29017;
CC       P53886; P53068: DOC1; NbExp=9; IntAct=EBI-29017, EBI-2603;
CC       P53886; P40577: MND2; NbExp=3; IntAct=EBI-29017, EBI-25433;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC       {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 178 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the APC1 family. {ECO:0000305}.
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DR   EMBL; Z71448; CAA96060.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10378.2; -; Genomic_DNA.
DR   PIR; S63127; S63127.
DR   RefSeq; NP_014227.4; NM_001183010.4.
DR   PDB; 8A3T; EM; 3.50 A; C=1-1748.
DR   PDB; 8A5Y; EM; 4.90 A; C=1-1748.
DR   PDB; 8A61; EM; 5.40 A; C=1-1748.
DR   PDBsum; 8A3T; -.
DR   PDBsum; 8A5Y; -.
DR   PDBsum; 8A61; -.
DR   AlphaFoldDB; P53886; -.
DR   EMDB; EMD-15199; -.
DR   SMR; P53886; -.
DR   BioGRID; 35658; 511.
DR   ComplexPortal; CPX-756; Anaphase-Promoting core complex.
DR   ComplexPortal; CPX-760; Anaphase-Promoting Complex, CDC20 variant.
DR   ComplexPortal; CPX-761; Anaphase-Promoting Complex, CDH1 variant.
DR   ComplexPortal; CPX-762; Anaphase-Promoting complex AMA1 variant.
DR   DIP; DIP-970N; -.
DR   IntAct; P53886; 14.
DR   MINT; P53886; -.
DR   STRING; 4932.YNL172W; -.
DR   iPTMnet; P53886; -.
DR   MaxQB; P53886; -.
DR   PaxDb; 4932-YNL172W; -.
DR   PeptideAtlas; P53886; -.
DR   EnsemblFungi; YNL172W_mRNA; YNL172W; YNL172W.
DR   GeneID; 855549; -.
DR   KEGG; sce:YNL172W; -.
DR   AGR; SGD:S000005116; -.
DR   SGD; S000005116; APC1.
DR   VEuPathDB; FungiDB:YNL172W; -.
DR   eggNOG; KOG1858; Eukaryota.
DR   GeneTree; ENSGT00390000016757; -.
DR   HOGENOM; CLU_000746_0_0_1; -.
DR   InParanoid; P53886; -.
DR   OMA; LEEWHVY; -.
DR   OrthoDB; 180933at2759; -.
DR   BioCyc; YEAST:G3O-33185-MONOMER; -.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 855549; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P53886; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53886; Protein.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:SGD.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010458; P:exit from mitosis; IMP:SGD.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; NAS:ComplexPortal.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:ComplexPortal.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR024990; Apc1.
DR   InterPro; IPR011989; ARM-like.
DR   PANTHER; PTHR12827:SF3; ANAPHASE-PROMOTING COMPLEX SUBUNIT 1; 1.
DR   PANTHER; PTHR12827; MEIOTIC CHECKPOINT REGULATOR TSG24 FAMILY MEMBER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW   Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..1748
FT                   /note="Anaphase-promoting complex subunit 1"
FT                   /id="PRO_0000215875"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        1547
FT                   /note="M -> I (in Ref. 1; CAA96060)"
FT                   /evidence="ECO:0000305"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          92..103
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          152..160
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          163..168
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            208..211
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          212..216
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          368..379
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           391..397
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          398..405
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          408..415
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            416..419
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          420..427
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           430..434
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           436..441
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            446..448
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          450..452
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           459..461
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          462..467
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          469..471
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          476..483
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          486..492
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          494..496
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          499..505
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           508..510
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           512..514
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           515..519
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          527..529
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           530..540
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           543..563
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           572..587
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           596..600
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           602..605
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           608..615
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           617..638
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           642..644
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           645..662
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           666..670
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           703..709
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            724..729
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           732..736
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           740..752
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           761..768
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           773..776
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           784..797
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           805..807
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           811..825
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           860..871
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           894..905
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          908..910
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           911..919
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          921..923
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           936..964
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          973..975
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          985..987
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            998..1000
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1004..1020
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1031..1036
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1044..1055
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1064..1071
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1076..1090
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1096..1105
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1107..1109
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1121..1134
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1135..1137
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1141..1152
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1155..1157
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1160..1162
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1165..1178
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1179..1181
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1212..1229
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1237..1239
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1243..1254
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1255..1257
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1261..1267
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1271..1276
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1284..1296
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1305..1308
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1309..1311
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1323..1325
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1326..1342
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1350..1362
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1364..1367
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1374..1397
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1398..1400
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1404..1414
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1419..1422
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1476..1504
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1507..1509
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1511..1513
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1518..1527
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1539..1542
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1545..1547
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1548..1551
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1553..1561
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1570..1573
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1578..1580
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1584..1587
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1589..1592
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1596..1598
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1601..1604
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1607..1609
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1612..1615
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1618..1620
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1622..1625
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1630..1634
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            1641..1643
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          1644..1647
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1654..1669
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1682..1689
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1694..1703
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1713..1723
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           1731..1743
FT                   /evidence="ECO:0007829|PDB:8A3T"
SQ   SEQUENCE   1748 AA;  196162 MW;  33D32EC47CA40E61 CRC64;
     MTSKPSTRND YLPRETHNGE YTGDSPEWQL QINITNKIGG INGDIWLSRD GRSVKWCIED
     QCLRQFTYNQ KIIKAGYIDF EKTPDCFVVV LSDIAHVYML KNGGSTTVCF PFQIGNAFWY
     ANGVILERET SASFMDGGYD LKPIEFDLKH KYITLTDPMA PFGLISITNT FKGGINSASG
     NKTDILQDFQ LVLFPSDKDK CIAVFLDRNS KVLRFYYSRI LSSDQSRKGE LTISSTKKTG
     LDAAGNSQKS GGISKDLRKF SHLTRRSTSI NSNSHDFNAA ERVLSGNVGN ASGRTDIFAL
     PSSCSRRSLS ATLDRMGNNI APTNRAAPSG FFDSSSANTA THSNITPVSQ PMQQQQQEYL
     NQTATSSKDI VLTEISSLKL PDDIIFTSRR LSSILSKLKF LSLRFERREG LLIFHEPTHF
     CKIWLIDLLP DVLDSIPFKI YGNSPQNMIR LENLKLKEPS RIQAMYIHEL LESCLILVSE
     GQNKEEYKAC LYDPFVKITS PSKNISEELT KQNSLPSLQK LFPYPETSFT KLCFEAVKYI
     TSPAFNISFI FLWQSAYSIL LSRANDDVVG GLKMEHDAFS LVLSLLILPI PSSSAQEYQE
     YKEIYERDLF QHLKQDSEIT SSVLPRIVIG LHLIREEYSL NVLCRNEHAL LGQFLRFATA
     AMGWPDLWQS YYVPKMDSES KTFLHPREQN STFFHPLDEP PSITKSLYSI TENSSIPLCP
     FISFSRLVAT DTQVELRITP RSFKILGLYE LVHSPNFLPD YVLGILSSFK VDKDELQTYP
     LGILVPLQNI LKILEDKLSE VRDNLELLDR ADLQRCSAII NSIRSDSKEV LKRGQRDSYM
     LCKVPLAKNR SSLSKKPSDI YSILSEIVKS ASQVPLDGSA MRMSNIQDDE DIDEGRSLKL
     NAGLIFSEDK RFTHVVSLLA YYRPTKTQFF TTKTEYAQIL AQKKYFAKIM ALRTCTNGVG
     WGAVAYATEK PISTQKWVIQ PLNLISVFPD DTKITVKAPE DIAHDIVEWG QFHAGVSSGL
     RISKKATGIT GSWIAFNKPK ELDAYHGGFL LGLGLNGHLK NLEEWHIYNY LSPRNTHISI
     GLLLGMSSSM KGSMDSKLIK VISVHLVAFL PSGSSDLNID LKLQTAGIIG MGMLYLNSRH
     KRMSDSIFAQ LVSLLNVNDE MVADEEYRLA AGISLGLINL GAGQTKLRKW DSSLLGLGDD
     LPEDVYDSSD VEQNVMYEDL TTKLLEIVTS TYDVENDWIP ENSQIGAVIA IMFLFLKSNN
     FGISNMLKVD LKEILKANIN TRPELLMYRE WASNMILWEF IGDDLSFIMK DVDIGVKFSE
     LNTDLLPIYY TMAGRILAMG IRFASTGNLK IRNILLSLVD KFLPLYQYPG KQNLDFRLTI
     SVINVLTNVI VVSLSMVMCA SGDLEVLRRV KYLHEVASGP YSDLFQEIPS SKSDVSGVTQ
     VTSNTNTPGN SDRERVDETA ASLDDERSSN GSDISDPTAY LEDKKDIDDH YGKFISTNLA
     LGFLFLGSGQ YALNTSTLES IAFLSMSVLP TYTTPHPLQE LKHFWSMAVE PRCLVIKDIS
     TGDAVNNVPI ELVVEEDVEK EEVIREISTP CLLPDFSKIK SIRVKMHGYF PLEVNFTKDY
     SASDFFSGGT IIYIQRKSES VFENKASFRN VEDIHVALKR KAAESKNYSR LNLKNEQGNT
     TSSQLVESLG IQDLTMVELD TLLSAGNNTA LTDSESYNLG LLCSDKNSGD ILDCQLELWY
     KSFGPHDE
//