DDI1_YEAST
ID DDI1_YEAST Reviewed; 428 AA.
AC P40087; D3DM50;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=DNA damage-inducible protein 1;
DE EC=3.4.23.- {ECO:0000250|UniProtKB:I7HUG0};
DE AltName: Full=v-SNARE-master 1;
GN Name=DDI1; Synonyms=VSM1; OrderedLocusNames=YER143W;
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], AND INDUCTION.
RC STRAIN=ATCC 64665 / S288c / DC5;
RX PubMed=9157248; DOI=10.1046/j.1365-2958.1997.2701631.x;
RA Liu Y., Xiao W.;
RT "Bidirectional regulation of two DNA-damage-inducible genes, MAG1 and DDI1,
RT from Saccharomyces cerevisiae.";
RL Mol. Microbiol. 23:777-789(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH SNC1 AND
RP SNC2, AND SUBCELLULAR LOCATION.
RX PubMed=10330187; DOI=10.1128/mcb.19.6.4480;
RA Lustgarten V., Gerst J.E.;
RT "Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative
RT regulator of constitutive exocytosis.";
RL Mol. Cell. Biol. 19:4480-4494(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=9826765; DOI=10.1093/nar/26.23.5402;
RA Zhu Y., Xiao W.;
RT "Differential regulation of two closely clustered yeast genes, MAG1 and
RT DDI1, by cell-cycle checkpoints.";
RL Nucleic Acids Res. 26:5402-5408(1998).
RN [7]
RP SUBUNIT, AND INTERACTION WITH RAD23.
RX PubMed=11700052; DOI=10.1006/jmbi.2001.5105;
RA Bertolaet B.L., Clarke D.J., Wolff M., Watson M.H., Henze M., Divita G.,
RA Reed S.I.;
RT "UBA domains mediate protein-protein interactions between two DNA damage-
RT inducible proteins.";
RL J. Mol. Biol. 313:955-963(2001).
RN [8]
RP FUNCTION.
RX PubMed=11238935; DOI=10.1128/mcb.21.6.1997-2007.2001;
RA Clarke D.J., Mondesert G., Segal M., Bertolaet B.L., Jensen S., Wolff M.,
RA Henze M., Reed S.I.;
RT "Dosage suppressors of pds1 implicate ubiquitin-associated domains in
RT checkpoint control.";
RL Mol. Cell. Biol. 21:1997-2007(2001).
RN [9]
RP INDUCTION.
RX PubMed=11713673; DOI=10.1007/s004380100538;
RA Zhu Y., Xiao W.;
RT "Two alternative cell cycle checkpoint pathways differentially control DNA
RT damage-dependent induction of MAG1 and DDI1 expression in yeast.";
RL Mol. Genet. Genomics 266:436-444(2001).
RN [10]
RP FUNCTION.
RX PubMed=12051757; DOI=10.1016/s0006-291x(02)00340-6;
RA Saeki Y., Saitoh A., Toh-e A., Yokosawa H.;
RT "Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-
RT dependent proteolysis.";
RL Biochem. Biophys. Res. Commun. 293:986-992(2002).
RN [11]
RP FUNCTION, AND INTERACTION WITH SNC1; SNC2; SSO; TLG1 AND TLG2.
RX PubMed=12925750; DOI=10.1091/mbc.e02-12-0804;
RA Marash M., Gerst J.E.;
RT "Phosphorylation of the autoinhibitory domain of the Sso t-SNAREs promotes
RT binding of the Vsm1 SNARE regulator in yeast.";
RL Mol. Biol. Cell 14:3114-3125(2003).
RN [12]
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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [15]
RP INDUCTION.
RX PubMed=15452273; DOI=10.1093/nar/gkh838;
RA Zhu Y., Xiao W.;
RT "Pdr3 is required for DNA damage induction of MAG1 and DDI1 via a bi-
RT directional promoter element.";
RL Nucleic Acids Res. 32:5066-5075(2004).
RN [16]
RP FUNCTION, AND INTERACTION WITH THE HO ENDONUCLEASE.
RX PubMed=15964793; DOI=10.1128/mcb.25.13.5355-5362.2005;
RA Kaplun L., Tzirkin R., Bakhrat A., Shabek N., Ivantsiv Y., Raveh D.;
RT "The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-
RT mediated degradation of Ho endonuclease.";
RL Mol. Cell. Biol. 25:5355-5362(2005).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17144915; DOI=10.1186/1747-1028-1-28;
RA Diaz-Martinez L.A., Kang Y., Walters K.J., Clarke D.J.;
RT "Yeast UBL-UBA proteins have partially redundant functions in cell cycle
RT control.";
RL Cell Div. 1:28-28(2006).
RN [18]
RP FUNCTION, AND INTERACTION WITH UFO1.
RX PubMed=16478980; DOI=10.1128/mcb.26.5.1579-1588.2006;
RA Ivantsiv Y., Kaplun L., Tzirkin-Goldin R., Shabek N., Raveh D.;
RT "Unique role for the UbL-UbA protein Ddi1 in turnover of SCFUfo1
RT complexes.";
RL Mol. Cell. Biol. 26:1579-1588(2006).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [20]
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 [21]
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 [22]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-220.
RX PubMed=21266539; DOI=10.1096/fj.10-178947;
RA White R.E., Powell D.J., Berry C.;
RT "HIV proteinase inhibitors target the Ddi1-like protein of Leishmania
RT parasites.";
RL FASEB J. 25:1729-1736(2011).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 180-325, AND SUBUNIT.
RX PubMed=17010377; DOI=10.1016/j.jmb.2006.08.086;
RA Sirkis R., Gerst J.E., Fass D.;
RT "Ddi1, a eukaryotic protein with the retroviral protease fold.";
RL J. Mol. Biol. 364:376-387(2006).
CC -!- FUNCTION: Aspartic protease (PubMed:21266539). Appears to act as
CC negative regulator of constitutive exocytosis (PubMed:10330187,
CC PubMed:12051757). May act at the level of secretory vesicle docking and
CC fusion as a competitive inhibitor of SNARE assembly (PubMed:12925750).
CC Acts as a linker between the 19S proteasome and polyubiquitinated
CC proteins like the HO endonuclease and UFO1 via UBA domain interactions
CC with ubiquitin for their subsequent degradation (PubMed:17144915,
CC PubMed:16478980). Required for S-phase checkpoint control
CC (PubMed:11238935, PubMed:17144915). {ECO:0000269|PubMed:10330187,
CC ECO:0000269|PubMed:11238935, ECO:0000269|PubMed:12051757,
CC ECO:0000269|PubMed:12925750, ECO:0000269|PubMed:15964793,
CC ECO:0000269|PubMed:16478980, ECO:0000269|PubMed:17144915,
CC ECO:0000305|PubMed:21266539}.
CC -!- ACTIVITY REGULATION: Inhibited by the proteinase inhibitors indinavir,
CC lopinavir, nelfinavir, isovaleryl pepstatin, ritonavir, saquinavir and
CC tipranavir. {ECO:0000269|PubMed:21266539}.
CC -!- SUBUNIT: Forms homodimers. Interacts with RAD23. These interactions are
CC mediated by the UBA domain. Is also able to bind ubiquitin and
CC polyubiquitinated proteins. Interacts with the SNAREs SNC1, SNC2, SSO1,
CC TLG1 and TLG2. Binding to SSO1 is promoted by the phosphorylation of
CC 'Ser-49' of SSO1 by TKP1. {ECO:0000269|PubMed:10330187,
CC ECO:0000269|PubMed:11700052, ECO:0000269|PubMed:12925750,
CC ECO:0000269|PubMed:15964793, ECO:0000269|PubMed:16478980,
CC ECO:0000269|PubMed:17010377, ECO:0000269|PubMed:17144915}.
CC -!- INTERACTION:
CC P40087; P0CG63: UBI4; NbExp=3; IntAct=EBI-5717, EBI-7000452;
CC P40087; P0CG48: UBC; Xeno; NbExp=2; IntAct=EBI-5717, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10330187}. Cell
CC membrane {ECO:0000269|PubMed:10330187}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10330187}; Cytoplasmic side
CC {ECO:0000269|PubMed:10330187}.
CC -!- INDUCTION: By DNA damage via PDR3. {ECO:0000269|PubMed:11713673,
CC ECO:0000269|PubMed:15452273, ECO:0000269|PubMed:9157248,
CC ECO:0000269|PubMed:9826765}.
CC -!- MISCELLANEOUS: Present with 6510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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; U14002; AAB82066.1; -; Genomic_DNA.
DR EMBL; AF034895; AAC18522.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64670.1; -; Genomic_DNA.
DR EMBL; AY692945; AAT92964.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07804.1; -; Genomic_DNA.
DR PIR; S50646; S50646.
DR RefSeq; NP_011070.3; NM_001179033.3.
DR PDB; 2I1A; X-ray; 2.30 A; A/B/C/D=180-325.
DR PDB; 2MR9; NMR; -; A=389-428.
DR PDB; 2MRO; NMR; -; B=389-428.
DR PDB; 2MRP; NMR; -; A=2-80.
DR PDB; 2MWS; NMR; -; B=2-80.
DR PDB; 2N7E; NMR; -; A=1-80.
DR PDB; 4Z2Z; X-ray; 1.80 A; A/B=185-325.
DR PDB; 5KES; NMR; -; A=86-196.
DR PDBsum; 2I1A; -.
DR PDBsum; 2MR9; -.
DR PDBsum; 2MRO; -.
DR PDBsum; 2MRP; -.
DR PDBsum; 2MWS; -.
DR PDBsum; 2N7E; -.
DR PDBsum; 4Z2Z; -.
DR PDBsum; 5KES; -.
DR AlphaFoldDB; P40087; -.
DR BMRB; P40087; -.
DR SMR; P40087; -.
DR BioGRID; 36892; 116.
DR DIP; DIP-1216N; -.
DR IntAct; P40087; 5.
DR MINT; P40087; -.
DR STRING; 4932.YER143W; -.
DR MEROPS; A28.001; -.
DR iPTMnet; P40087; -.
DR MaxQB; P40087; -.
DR PaxDb; P40087; -.
DR PRIDE; P40087; -.
DR EnsemblFungi; YER143W_mRNA; YER143W; YER143W.
DR GeneID; 856886; -.
DR KEGG; sce:YER143W; -.
DR SGD; S000000945; DDI1.
DR VEuPathDB; FungiDB:YER143W; -.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00950000182999; -.
DR HOGENOM; CLU_020435_2_0_1; -.
DR InParanoid; P40087; -.
DR OMA; PCRFTVI; -.
DR BioCyc; YEAST:G3O-30304-MON; -.
DR EvolutionaryTrace; P40087; -.
DR PRO; PR:P40087; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40087; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:SGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:SGD.
DR GO; GO:1904855; F:proteasome regulatory particle binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:SGD.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR CDD; cd05479; RP_DDI; 1.
DR CDD; cd01796; Ubl_Ddi1_like; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR033882; DDI1_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cell membrane; Cytoplasm; Hydrolase;
KW Isopeptide bond; Membrane; Protease; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..428
FT /note="DNA damage-inducible protein 1"
FT /id="PRO_0000210997"
FT DOMAIN 1..80
FT /note="Ubiquitin-like"
FT DOMAIN 389..428
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 328..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /evidence="ECO:0000305"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:14557538"
FT MUTAGEN 220
FT /note="D->A: Increased protein secretion most likely due to
FT reduced catalytic activity. Cells are larger and clump
FT together."
FT /evidence="ECO:0000269|PubMed:21266539"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2MRP"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2MRP"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2MRP"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:2MRP"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2MRP"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2MRP"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2N7E"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2MRP"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2MRP"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2MRP"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:5KES"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:5KES"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:5KES"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:5KES"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:5KES"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:5KES"
FT HELIX 168..189
FT /evidence="ECO:0007829|PDB:5KES"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4Z2Z"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:2MR9"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:2MR9"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:2MR9"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:2MR9"
SQ SEQUENCE 428 AA; 47354 MW; B43425B029B7658B CRC64;
MDLTISNELT GEIYGPIEVS EDMALTDLIA LLQADCGFDK TKHDLYYNMD ILDSNRTQSL
KELGLKTDDL LLIRGKISNS IQTDAATLSD EAFIEQFRQE LLNNQMLRSQ LILQIPGLND
LVNDPLLFRE RLGPLILQRR YGGYNTAMNP FGIPQDEYTR LMANPDDPDN KKRIAELLDQ
QAIDEQLRNA IEYTPEMFTQ VPMLYINIEI NNYPVKAFVD TGAQTTIMST RLAKKTGLSR
MIDKRFIGEA RGVGTGKIIG RIHQAQVKIE TQYIPCSFTV LDTDIDVLIG LDMLKRHLAC
VDLKENVLRI AEVETSFLSE AEIPKSFQEG LPAPTSVTTS SDKPLTPTKT SSTLPPQPGA
VPALAPRTGM GPTPTGRSTA GATTATGRTF PEQTIKQLMD LGFPRDAVVK ALKQTNGNAE
FAASLLFQ
