ID   DOA10_YEAST             Reviewed;        1319 AA.
AC   P40318; D6VVQ1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=ERAD-associated E3 ubiquitin-protein ligase DOA10;
DE            EC=2.3.2.27 {ECO:0000269|PubMed:31445887};
DE   AltName: Full=RING-type E3 ubiquitin transferase DOA10 {ECO:0000305};
GN   Name=SSM4; Synonyms=DOA10; OrderedLocusNames=YIL030C;
GN   ORFNames=YI3299.01C, YI9905.18C;
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].
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=7816042; DOI=10.1007/bf00290112;
RA   Mandart E., Dufour M.-E., Lacroute F.;
RT   "Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA
RT   instability due to RNA14 mutations.";
RL   Mol. Gen. Genet. 245:323-333(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11641273; DOI=10.1101/gad.933301;
RA   Swanson R., Locher M., Hochstrasser M.;
RT   "A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum
RT   that functions in both ER-associated and Matalpha2 repressor degradation.";
RL   Genes Dev. 15:2660-2674(2001).
RN   [5]
RP   INTERACTION WITH CDC48; UBX2; UBC6 AND UBC7.
RX   PubMed=16179953; DOI=10.1038/ncb1298;
RA   Neuber O., Jarosch E., Volkwein C., Walter J., Sommer T.;
RT   "Ubx2 links the Cdc48 complex to ER-associated protein degradation.";
RL   Nat. Cell Biol. 7:993-998(2005).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH UBX2; CDC48 AND UFD1.
RX   PubMed=16179952; DOI=10.1038/ncb1299;
RA   Schuberth C., Buchberger A.;
RT   "Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their
RT   substrates to ensure efficient ER-associated protein degradation.";
RL   Nat. Cell Biol. 7:999-1006(2005).
RN   [7]
RP   FUNCTION, AND IDENTIFICATION IN THE DOA10 COMPLEX.
RX   PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA   Carvalho P., Goder V., Rapoport T.A.;
RT   "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT   degradation of ER proteins.";
RL   Cell 126:361-373(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=16437165; DOI=10.1038/sj.emboj.7600946;
RA   Ravid T., Kreft S.G., Hochstrasser M.;
RT   "Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded
RT   by distinct pathways.";
RL   EMBO J. 25:533-543(2006).
RN   [9]
RP   TOPOLOGY.
RX   PubMed=16373356; DOI=10.1074/jbc.m512215200;
RA   Kreft S.G., Wang L., Hochstrasser M.;
RT   "Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin
RT   ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI).";
RL   J. Biol. Chem. 281:4646-4653(2006).
RN   [10]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=17051211; DOI=10.1038/nature05170;
RA   Deng M., Hochstrasser M.;
RT   "Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase.";
RL   Nature 443:827-831(2006).
RN   [11]
RP   FUNCTION IN CYTOSOLIC PROTEIN DEGRADATION.
RX   PubMed=18812321; DOI=10.1074/jbc.m806424200;
RA   Metzger M.B., Maurer M.J., Dancy B.M., Michaelis S.;
RT   "Degradation of a cytosolic protein requires endoplasmic reticulum-
RT   associated degradation machinery.";
RL   J. Biol. Chem. 283:32302-32316(2008).
RN   [12]
RP   IDENTIFICATION BY 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).
RN   [13]
RP   INTERACTION WITH PEX29.
RX   PubMed=20159987; DOI=10.1074/jbc.m110.110551;
RA   Liu C., van Dyk D., Xu P., Choe V., Pan H., Peng J., Andrews B., Rao H.;
RT   "Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10
RT   substrates.";
RL   J. Biol. Chem. 285:10265-10272(2010).
RN   [14]
RP   FUNCTION IN N-ACETYLATED PROTEIN DEGRADATION.
RX   PubMed=20110468; DOI=10.1126/science.1183147;
RA   Hwang C.S., Shemorry A., Varshavsky A.;
RT   "N-terminal acetylation of cellular proteins creates specific degradation
RT   signals.";
RL   Science 327:973-977(2010).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=31445887; DOI=10.1016/j.molcel.2019.07.006;
RA   Matsumoto S., Nakatsukasa K., Kakuta C., Tamura Y., Esaki M., Endo T.;
RT   "Msp1 clears mistargeted proteins by facilitating their transfer from
RT   mitochondria to the ER.";
RL   Mol. Cell 76:191-205(2019).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin
CC       specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2
CC       ligases, and transfers it to substrates promoting their degradation
CC       (PubMed:11641273, PubMed:16179952, PubMed:16437165, PubMed:16873066,
CC       PubMed:17051211, PubMed:18812321, PubMed:20110468). Mediates the
CC       degradation of a broad range of substrates, including endoplasmic
CC       reticulum membrane proteins (ERQC), soluble nuclear proteins and
CC       soluble cytoplasmic proteins (CytoQC) (PubMed:11641273,
CC       PubMed:16179952, PubMed:16437165, PubMed:16873066, PubMed:17051211,
CC       PubMed:18812321, PubMed:20110468). Component of the DOA10 ubiquitin
CC       ligase complex, which is part of the ERAD-C pathway responsible for the
CC       rapid degradation of membrane proteins with misfolded cytoplasmic
CC       domains (PubMed:16873066). ERAD-C substrates are ubiquitinated through
CC       DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and
CC       UBC7-CUE1 (PubMed:11641273, PubMed:16179952, PubMed:16437165,
CC       PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468).
CC       Ubiquitinated substrates are then removed to the cytosol via the action
CC       of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the
CC       proteasome (PubMed:11641273, PubMed:16179952, PubMed:16437165,
CC       PubMed:16873066, PubMed:17051211, PubMed:18812321, PubMed:20110468).
CC       Also recognizes the N-terminally acetylated residue of proteins as
CC       degradation signal (degron) (PubMed:20110468). N-terminally acetylated
CC       target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104,
CC       UBP6 and ARO8 (PubMed:20110468). Catalyzes ubiquitination of
CC       mislocalized tail-anchored proteins that are extracted from the
CC       mitochondrion membrane by MSP1: following extraction, mistargeted
CC       proteins are transferred to the endoplasmic reticulum, where they are
CC       ubiquitinated by DOA10 and degraded by the proteasome
CC       (PubMed:31445887). {ECO:0000269|PubMed:11641273,
CC       ECO:0000269|PubMed:16179952, ECO:0000269|PubMed:16437165,
CC       ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:17051211,
CC       ECO:0000269|PubMed:18812321, ECO:0000269|PubMed:20110468,
CC       ECO:0000269|PubMed:31445887}.
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:31445887};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:31445887}.
CC   -!- SUBUNIT: Component of the DOA10 ubiquitin ligase complex which contains
CC       E3 ligase SSM4/DOA10 and CDC48-binding protein UBX2/SEL1. The DOA10
CC       complex interacts with the heterotrimeric CDC48-NPL4-UFD1 ATPase
CC       complex which is recruited by UBX2/SEL1 via its interaction with CDC48.
CC       Interacts with its associated ubiquitin conjugating enzymes UBC6 and
CC       UBC7 with its membrane anchor CUE1. Interacts with PEX29.
CC       {ECO:0000269|PubMed:16179952, ECO:0000269|PubMed:16179953,
CC       ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:20159987}.
CC   -!- INTERACTION:
CC       P40318; P25694: CDC48; NbExp=4; IntAct=EBI-18208, EBI-4308;
CC       P40318; P38428: CUE1; NbExp=2; IntAct=EBI-18208, EBI-27580;
CC       P40318; P12866: STE6; NbExp=3; IntAct=EBI-18208, EBI-18383;
CC       P40318; Q04228: UBX2; NbExp=5; IntAct=EBI-18208, EBI-27730;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:17051211}; Multi-pass
CC       membrane protein {ECO:0000255}. Nucleus inner membrane
CC       {ECO:0000269|PubMed:11641273, ECO:0000269|PubMed:17051211}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC       activity.
CC   -!- SIMILARITY: Belongs to the DOA10/MARCH6 family. {ECO:0000305}.
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DR   EMBL; X76715; CAA54133.1; -; Genomic_DNA.
DR   EMBL; Z46881; CAA86961.1; -; Genomic_DNA.
DR   EMBL; Z46861; CAA86921.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08517.1; -; Genomic_DNA.
DR   PIR; S49951; S49951.
DR   RefSeq; NP_012234.3; NM_001179380.3.
DR   PDB; 2M6M; NMR; -; A=19-101.
DR   PDBsum; 2M6M; -.
DR   AlphaFoldDB; P40318; -.
DR   BMRB; P40318; -.
DR   SMR; P40318; -.
DR   BioGRID; 34959; 268.
DR   ComplexPortal; CPX-3074; Doa10 E3 ubiquitin ligase complex.
DR   DIP; DIP-7286N; -.
DR   IntAct; P40318; 83.
DR   MINT; P40318; -.
DR   STRING; 4932.YIL030C; -.
DR   TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   iPTMnet; P40318; -.
DR   MaxQB; P40318; -.
DR   PaxDb; 4932-YIL030C; -.
DR   PeptideAtlas; P40318; -.
DR   EnsemblFungi; YIL030C_mRNA; YIL030C; YIL030C.
DR   GeneID; 854781; -.
DR   KEGG; sce:YIL030C; -.
DR   AGR; SGD:S000001292; -.
DR   SGD; S000001292; SSM4.
DR   VEuPathDB; FungiDB:YIL030C; -.
DR   eggNOG; KOG1609; Eukaryota.
DR   GeneTree; ENSGT00940000155171; -.
DR   HOGENOM; CLU_006729_0_0_1; -.
DR   InParanoid; P40318; -.
DR   OMA; ALYFQYD; -.
DR   OrthoDB; 1342875at2759; -.
DR   BioCyc; MetaCyc:G3O-31303-MONOMER; -.
DR   BioCyc; YEAST:G3O-31303-MONOMER; -.
DR   BRENDA; 2.3.2.27; 984.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 854781; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P40318; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40318; Protein.
DR   GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; NAS:ComplexPortal.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IDA:SGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR   CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR   PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Endoplasmic reticulum; Membrane; Metal-binding;
KW   Nucleus; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..1319
FT                   /note="ERAD-associated E3 ubiquitin-protein ligase DOA10"
FT                   /id="PRO_0000072214"
FT   TOPO_DOM        1..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..203
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        490..491
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        492..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        513..626
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        627..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        648..660
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        682..739
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        740..760
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        761..777
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        778..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        798..965
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        966..986
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        987..1019
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1020..1040
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1041..1113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1114..1134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1135..1168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1169..1189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1190..1213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1214..1234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1235..1270
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1271..1291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1292..1319
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         31..100
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   REGION          291..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CONFLICT        241
FT                   /note="L -> F (in Ref. 1; CAA54133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        743
FT                   /note="A -> T (in Ref. 1; CAA54133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1085
FT                   /note="N -> D (in Ref. 1; CAA54133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1186
FT                   /note="Y -> F (in Ref. 1; CAA54133)"
FT                   /evidence="ECO:0000305"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:2M6M"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:2M6M"
FT   HELIX           67..76
FT                   /evidence="ECO:0007829|PDB:2M6M"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:2M6M"
SQ   SEQUENCE   1319 AA;  151455 MW;  3EDFF7F9D90A0C8C CRC64;
     MDVDSDVNVS RLRDELHKVA NEETDTATFN DDAPSGATCR ICRGEATEDN PLFHPCKCRG
     SIKYMHESCL LEWVASKNID ISKPGADVKC DICHYPIQFK TIYAENMPEK IPFSLLLSKS
     ILTFFEKARL ALTIGLAAVL YIIGVPLVWN MFGKLYTMML DGSSPYPGDF LKSLIYGYDQ
     SATPELTTRA IFYQLLQNHS FTSLQFIMIV ILHIALYFQY DMIVREDVFS KMVFHKIGPR
     LSPKDLKSRL KERFPMMDDR MVEYLAREMR AHDENRQEQG HDRLNMPAAA ADNNNNVINP
     RNDNVPPQDP NDHRNFENLR HVDELDHDEA TEEHENNDSD NSLPSGDDSS RILPGSSSDN
     EEDEEAEGQQ QQQQPEEEAD YRDHIEPNPI DMWANRRAQN EFDDLIAAQQ NAINRPNAPV
     FIPPPAQNRA GNVDQDEQDF GAAVGVPPAQ ANPDDQGQGP LVINLKLKLL NVIAYFIIAV
     VFTAIYLAIS YLFPTFIGFG LLKIYFGIFK VILRGLCHLY YLSGAHIAYN GLTKLVPKVD
     VAMSWISDHL IHDIIYLYNG YTENTMKHSI FIRALPALTT YLTSVSIVCA SSNLVSRGYG
     RENGMSNPTR RLIFQILFAL KCTFKVFTLF FIELAGFPIL AGVMLDFSLF CPILASNSRM
     LWVPSICAIW PPFSLFVYWT IGTLYMYWFA KYIGMIRKNI IRPGVLFFIR SPEDPNIKIL
     HDSLIHPMSI QLSRLCLSMF IYAIFIVLGF GFHTRIFFPF MLKSNLLSVP EAYKPTSIIS
     WKFNTILLTL YFTKRILESS SYVKPLLERY WKTIFKLCSR KLRLSSFILG KDTPTERGHI
     VYRNLFYKYI AAKNAEWSNQ ELFTKPKTLE QAEELFGQVR DVHAYFVPDG VLMRVPSSDI
     VSRNYVQTMF VPVTKDDKLL KPLDLERIKE RNKRAAGEFG YLDEQNTEYD QYYIVYVPPD
     FRLRYMTLLG LVWLFASILM LGVTFISQAL INFVCSFGFL PVVKLLLGER NKVYVAWKEL
     SDISYSYLNI YYVCVGSVCL SKIAKDILHF TEGQNTLDEH AVDENEVEEV EHDIPERDIN
     NAPVNNINNV EEGQGIFMAI FNSIFDSMLV KYNLMVFIAI MIAVIRTMVS WVVLTDGILA
     CYNYLTIRVF GNSSYTIGNS KWFKYDESLL FVVWIISSMV NFGTGYKSLK LFFRNRNTSK
     LNFLKTMALE LFKQGFLHMV IYVLPIIILS LVFLRDVSTK QIIDISHGSR SFTLSLNESF
     PTWTRMQDIY FGLLIALESF TFFFQATVLF IQWFKSTVQN VKDEVYTKGR ALENLPDES
//