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 27-MAR-2024, entry version 203. 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; 119. 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; 4932-YER143W; -. DR PeptideAtlas; P40087; -. DR EnsemblFungi; YER143W_mRNA; YER143W; YER143W. DR GeneID; 856886; -. DR KEGG; sce:YER143W; -. DR AGR; SGD:S000000945; -. 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; LNEERHS; -. DR OrthoDB; 1332686at2759; -. DR BioCyc; YEAST:G3O-30304-MONOMER; -. DR BioGRID-ORCS; 856886; 5 hits in 10 CRISPR screens. 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: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; cd14309; UBA_scDdi1_like; 1. DR CDD; cd01796; Ubl_Ddi1_like; 1. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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 PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1. DR PANTHER; PTHR12917:SF1; AT13091P; 1. DR Pfam; PF09668; Asp_protease; 1. DR Pfam; PF00627; UBA; 1. DR SMART; SM00165; UBA; 1. DR SUPFAM; SSF50630; Acid proteases; 1. DR SUPFAM; SSF46934; UBA-like; 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 //