ID   IML1_YEAST              Reviewed;        1584 AA.
AC   P47170; D6VWV7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Vacuolar membrane-associated protein IML1;
DE   AltName: Full=Increased minichromosome loss protein 1;
DE   AltName: Full=SEH-associated protein 1;
GN   Name=IML1; Synonyms=SEA1; OrderedLocusNames=YJR138W; ORFNames=J2129;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND IDENTIFICATION BY
RP   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680 AND SER-737, AND
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, 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).
RN   [8]
RP   SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX   PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA   Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA   Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA   Rout M.P., Dargemont C.;
RT   "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT   associates with the vacuole in Saccharomyces cerevisiae.";
RL   Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
CC   -!- FUNCTION: Component of the SEA complex which coats the vacuolar
CC       membrane and is involved in intracellular trafficking, autophagy,
CC       response to nitrogen starvation, and amino acid biogenesis.
CC       {ECO:0000269|PubMed:21454883}.
CC   -!- SUBUNIT: Component of the SEA complex composed of at least IML1/SEA1,
CC       RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
CC       {ECO:0000269|PubMed:21454883}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:21454883}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21454883}.
CC   -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the IML1 family. {ECO:0000305}.
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DR   EMBL; Z49638; CAA89670.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08923.1; -; Genomic_DNA.
DR   PIR; S57161; S57161.
DR   RefSeq; NP_012672.1; NM_001181796.2.
DR   PDB; 8ADL; EM; 2.95 A; W/X=1-1584.
DR   PDB; 8AE6; EM; 2.70 A; W=1-1584.
DR   PDBsum; 8ADL; -.
DR   PDBsum; 8AE6; -.
DR   AlphaFoldDB; P47170; -.
DR   SMR; P47170; -.
DR   BioGRID; 33894; 240.
DR   ComplexPortal; CPX-3231; SEA complex.
DR   DIP; DIP-2589N; -.
DR   IntAct; P47170; 29.
DR   MINT; P47170; -.
DR   STRING; 4932.YJR138W; -.
DR   GlyGen; P47170; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P47170; -.
DR   MaxQB; P47170; -.
DR   PaxDb; 4932-YJR138W; -.
DR   PeptideAtlas; P47170; -.
DR   EnsemblFungi; YJR138W_mRNA; YJR138W; YJR138W.
DR   GeneID; 853603; -.
DR   KEGG; sce:YJR138W; -.
DR   AGR; SGD:S000003899; -.
DR   SGD; S000003899; IML1.
DR   VEuPathDB; FungiDB:YJR138W; -.
DR   eggNOG; KOG3572; Eukaryota.
DR   GeneTree; ENSGT00390000016559; -.
DR   HOGENOM; CLU_000935_1_1_1; -.
DR   InParanoid; P47170; -.
DR   OMA; SWMNATP; -.
DR   OrthoDB; 946033at2759; -.
DR   BioCyc; YEAST:G3O-31754-MONOMER; -.
DR   BioGRID-ORCS; 853603; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P47170; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47170; Protein.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:1990130; C:GATOR1 complex; IDA:SGD.
DR   GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; NAS:ComplexPortal.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IGI:SGD.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IMP:SGD.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:SGD.
DR   GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:2000785; P:regulation of autophagosome assembly; IMP:SGD.
DR   GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR   CDD; cd04449; DEP_DEPDC5-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR027244; IML1.
DR   InterPro; IPR048255; IML1_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13179; DEP DOMAIN CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR13179:SF8; GATOR COMPLEX PROTEIN DEPDC5; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF12257; IML1; 1.
DR   SMART; SM00049; DEP; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport; Vacuole.
FT   CHAIN           1..1584
FT                   /note="Vacuolar membrane-associated protein IML1"
FT                   /id="PRO_0000203123"
FT   DOMAIN          1198..1273
FT                   /note="DEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         737
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           161..166
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          173..177
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           178..183
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          205..211
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           218..227
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            228..230
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          231..234
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            242..244
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          260..264
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          269..276
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          278..285
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           287..289
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:8ADL"
FT   HELIX           299..305
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           308..318
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          323..333
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          349..363
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           364..366
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           367..386
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          393..397
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           409..417
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           418..420
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:8ADL"
FT   STRAND          434..442
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           450..460
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          467..473
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          480..486
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          492..504
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           523..526
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            532..534
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           553..562
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          848..852
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           860..865
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            870..873
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           887..890
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          897..899
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           905..908
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          913..919
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            923..925
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          926..929
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           932..946
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          949..951
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           955..960
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          986..989
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          991..998
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1005..1011
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1020..1022
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1028..1030
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            1044..1046
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1054..1062
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1076..1084
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1091..1093
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1105..1121
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            1128..1131
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1152..1158
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1340..1342
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1344..1351
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1357..1359
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1362..1371
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1377..1385
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1388..1404
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1407..1412
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1417..1422
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1430..1432
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            1438..1440
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1447..1452
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1456..1464
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1467..1469
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1475..1477
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1483..1488
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1496..1511
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1513..1515
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   STRAND          1517..1521
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   TURN            1523..1525
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1551..1559
FT                   /evidence="ECO:0007829|PDB:8AE6"
FT   HELIX           1562..1577
FT                   /evidence="ECO:0007829|PDB:8AE6"
SQ   SEQUENCE   1584 AA;  181949 MW;  BB8E73FF5B70CCDF CRC64;
     MFAKLHGKKQ RPISSINSQT PRTSNTTHAN SISLSSGNLI VGSNRNLRQK KEQFGSQQRA
     SGRKLISNKE NDDNVNNGGD NNYDNGERVH RHHIPGLKIK AYQAELGYHE SRFSENLVML
     NLVEFPDIKP GDLVELKTYH KNPSASNGDK KIYFIAKDFD GETKRRAKTS NVSILSGQLQ
     TLLDLPSRSR IWIKLKPNKF DLQADVVEFN IKDCLLNRGD MWVLSSKLVD TCVFMDQRLA
     FLDSIRGTIK GIYRNGKKIV SGYIGEQTRI IFRSESARLI FLIQITDEMW NFEETGEQLF
     QKMVNSFFPK IFKKWKDVDT HHTITIAFAI SMDLSDTSFK DLTPGESLKN SQDYFRIVVD
     QVSIIHWVDI METLREEFME IRKDLLNKQT DKGYSVANGR FSPVIKSNFL ELVNFATTIL
     TDPFKQLDLR HTTTHVMIIS PGSGLFDVDY SLLRLTGKKL LSLEMTMDLI CLSKAPLHIV
     PLFRYRDFEN KLHHCVPLWL SVFFWNDHDK KSNSEWTPRC KIYDLQMMGI TENELIREVD
     VEYLQLNKKV KSLSEFMNDY DKNAFEVKIL CAGSNTKQSK KLNSKFDTVF ENDVVVKARK
     IPATATTTHG NTKFIWRGPK VALPAIKDIQ KPNVIPDLSI KTIEASFYDD CNTTNDKIST
     PTTSNNDNLE MNDSLVSVRS ADNQNTSLAL DSLKGLSKRN SLKDFTQRVI TKFISNIDTS
     KNKKIKSTLL RDDVDNSPLG SNTPLPSSES KISGLKLQQK GLADENVISK RGNLIIKKNL
     SIFGLPSNEI MSGSPSSYLG SSHTRTSSKL SNMSDKAAFI TEGQKSKHDD SNTYSLTQQL
     KHRISETWVD IKSPSIPVSS EFANELLPIR WKDVWPKYVA RKYSKWRSFT TPAELPITIS
     DFPSKDDFDR NFIFRNHSVT LNTDQEQYNQ TYKDLLRDMI YMRLLTGFQI CVGRQVEKIE
     LSRESGESET VVNKYLDFNQ NDAFKLYLMI DSEIHRITCS SSGIIDVERY LRKDEANLFD
     QVPSYIPLVK TRYESSFRDA MIDPLHVKRE SLNWNQIDQV LAGYGDNLID RKWHGFRAKY
     VVLPTDIPPN TYSMVINGKS ETLNPEEIRV EGLRRLIGSI TRSRLRTEKE KKGRKTKREE
     IQPEVMFYTG PLYNFINEQQ TSLESSAINF KDSIFVNDNN LLNRNVELSK LAYQIQRGED
     RITLVNRKWH WKKHEKCFVG SEMVNWLIRN FSDIDTREDA IKYGQKVMKE GLFVHVLNKH
     NFLDGHYFYQ FSPEYVMDTN KLEKTNSHRS TLSDPKQMLR KASTGSSNDP SAMTPFSSVV
     PAISASNASV ADAKEPSRPI LMLSNSLVID VDPAGKSSKQ ESCTVHYDRV HNPDHCFHIR
     LEWLTTTPKL IDDLVGNWSR LCERYGLKMI EIPWEELCTI PSVNPFHSFV EIKLAINPWE
     DPEFKDRELF AKSKFYYHVY LLKASGFLLD NRASKFLQNQ DIEFDIMYSW GKPQFKYVQY
     IHHTGAYVAE LRENGCLFLA PNNIYISRVN PGNIIGKIHS ASSSSLDAQK VILNFKSTCL
     DYQKLRSIFL DAKEMWITGK IVED
//