USO1_YEAST
ID USO1_YEAST Reviewed; 1790 AA.
AC P25386; D6VRT8; E9PAG8; P89892; Q07380;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Intracellular protein transport protein USO1;
DE Short=Int-1;
GN Name=USO1; Synonyms=INT1; OrderedLocusNames=YDL058W;
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 26786 / X2180-1A;
RX PubMed=2010462; DOI=10.1083/jcb.113.2.245;
RA Nakajima H., Hirata A., Ogawa Y., Yonehara T., Yoda K., Yamasaki M.;
RT "A cytoskeleton-related gene, uso1, is required for intracellular protein
RT transport in Saccharomyces cerevisiae.";
RL J. Cell Biol. 113:245-260(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RA Bai Y., Symington L.S.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 782-1790.
RX PubMed=7582869; DOI=10.1006/bmme.1995.1042;
RA Hostetter M.K., Tao N.J., Gale C., Herman D.J., McClellan M., Sharp R.L.,
RA Kendrick K.E.;
RT "Antigenic and functional conservation of an integrin I-domain in
RT Saccharomyces cerevisiae.";
RL Biochem. Mol. Med. 55:122-130(1995).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, AND DOMAIN.
RX PubMed=8812994; DOI=10.1006/jsbi.1996.0053;
RA Yamakawa H., Seog D.H., Yoda K., Yamasaki M., Wakabayashi T.;
RT "Uso1 protein is a dimer with two globular heads and a long coiled-coil
RT tail.";
RL J. Struct. Biol. 116:356-365(1996).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1770, 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: Required for protein transport from the ER to the Golgi
CC complex.
CC -!- SUBUNIT: Homodimer. Dimerizes by parallel association of the tails,
CC resulting in an elongated structure with two globular head domains side
CC by side, and a long rod-like tail structure.
CC {ECO:0000269|PubMed:8812994}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasmic vesicle
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Note=Probably present on
CC vesicles operational between the ER and the Golgi complex.
CC -!- DOMAIN: Composed of a globular head region and a rod-like C-terminal
CC coiled coil domain. The rodlike tail sequence is highly repetitive,
CC composed of a heptapeptide repeat pattern characteristic of alpha-
CC helical coiled coils. May form filamentous structures in the cell.
CC {ECO:0000269|PubMed:8812994}.
CC -!- MISCELLANEOUS: Present with 2330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}.
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DR EMBL; X54378; CAA38253.1; -; Genomic_DNA.
DR EMBL; Z74105; CAA98620.1; -; Genomic_DNA.
DR EMBL; Z74106; CAA98621.1; -; Genomic_DNA.
DR EMBL; U53668; AAB66659.1; -; Genomic_DNA.
DR EMBL; L03188; AAB00143.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11798.1; -; Genomic_DNA.
DR PIR; S67593; S67593.
DR RefSeq; NP_010225.1; NM_001180117.1.
DR PDB; 6LST; X-ray; 2.94 A; A=1-726.
DR PDB; 6LSU; X-ray; 2.70 A; A=1-726.
DR PDBsum; 6LST; -.
DR PDBsum; 6LSU; -.
DR AlphaFoldDB; P25386; -.
DR SMR; P25386; -.
DR BioGRID; 32000; 310.
DR DIP; DIP-6815N; -.
DR IntAct; P25386; 6.
DR MINT; P25386; -.
DR STRING; 4932.YDL058W; -.
DR CarbonylDB; P25386; -.
DR iPTMnet; P25386; -.
DR MaxQB; P25386; -.
DR PaxDb; P25386; -.
DR PRIDE; P25386; -.
DR EnsemblFungi; YDL058W_mRNA; YDL058W; YDL058W.
DR GeneID; 851501; -.
DR KEGG; sce:YDL058W; -.
DR SGD; S000002216; USO1.
DR VEuPathDB; FungiDB:YDL058W; -.
DR eggNOG; KOG0946; Eukaryota.
DR GeneTree; ENSGT00390000017018; -.
DR HOGENOM; CLU_001063_0_0_1; -.
DR InParanoid; P25386; -.
DR OMA; RGWISQQ; -.
DR BioCyc; YEAST:G3O-29474-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR PRO; PR:P25386; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P25386; protein.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0048211; P:Golgi vesicle docking; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0035493; P:SNARE complex assembly; IMP:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006955; Uso1_p115_C.
DR InterPro; IPR006953; Vesicle_Uso1_P115_head.
DR Pfam; PF04871; Uso1_p115_C; 1.
DR Pfam; PF04869; Uso1_p115_head; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..1790
FT /note="Intracellular protein transport protein USO1"
FT /id="PRO_0000065730"
FT REPEAT 45..89
FT /note="ARM 1"
FT REPEAT 127..170
FT /note="ARM 2"
FT REPEAT 173..213
FT /note="ARM 3"
FT REPEAT 215..260
FT /note="ARM 4"
FT REPEAT 261..312
FT /note="ARM 5"
FT REPEAT 314..362
FT /note="ARM 6"
FT REPEAT 363..429
FT /note="ARM 7"
FT REPEAT 431..512
FT /note="ARM 8"
FT REPEAT 543..584
FT /note="ARM 9"
FT REPEAT 586..630
FT /note="ARM 10"
FT REGION 1..724
FT /note="Globular head"
FT REGION 452..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..487
FT /note="Charged (hyper-hydrophilic)"
FT REGION 991..1790
FT /note="Dispensable for the protein function"
FT REGION 1185..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 725..1790
FT /evidence="ECO:0000255"
FT COMPBIAS 463..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1790
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 390..391
FT /note="NG -> TA (in Ref. 1; CAA38253)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="N -> S (in Ref. 1; CAA38253)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="G -> E (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="E -> K (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1253
FT /note="V -> I (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="I -> V (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1461
FT /note="N -> S (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1581
FT /note="G -> S (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1600
FT /note="I -> V (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1661
FT /note="R -> S (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT CONFLICT 1772
FT /note="D -> DEEDDEE (in Ref. 5; AAB00143)"
FT /evidence="ECO:0000305"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6LST"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6LST"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:6LST"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 332..341
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 365..371
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 399..409
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 416..430
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 434..452
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 509..523
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:6LST"
FT HELIX 530..538
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:6LSU"
FT TURN 564..567
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 572..585
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 589..596
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 599..609
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 617..632
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 642..653
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 655..668
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:6LST"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:6LST"
FT HELIX 698..706
FT /evidence="ECO:0007829|PDB:6LSU"
FT HELIX 708..712
FT /evidence="ECO:0007829|PDB:6LSU"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:6LSU"
SQ SEQUENCE 1790 AA; 206452 MW; 90062544F55A52EE CRC64;
MDIIQGLIQQ PKIQSVDETI PTLCDRVENS TLISDRRSAV LGLKAFSRQY RESVIASGLK
PLLNTLKRDY MDEDSVKAIL ETILILFIRG DGHDDLTRGW ISQQSRLQNG KYPSPLVMKQ
EKEQVDQFSL WIADALTQSE DLIHLLVEFW EIDNFHIRLY TIQLLEAVMA TRPLKARSAL
ISLPTSISTM VSLLDDMHEP IRDEAILLLM AVVNDSPHVQ KLVAFENIFE RLFSIIEEEG
GLRGSLVVND CLSLINNILK YNTSNQTLFL ETGNLPKLAH LLSEPISQDE VFFWNDQRIV
NINTALDIVS LTVEPGNTVT TKHQNALLDS SVLMVVLRLA FFHNIPKKVR PVALLTAANM
VRSNEHAQLE FSKIDVPYFD PSLPVNSTAN GGPIKLIPVV SILINWMLYA NSVHTFDTRV
ACSRLLKAYF MDNFDLQRDF LLKQVQLCNN STNNVGDNAK ENGGSNKSDK ESDSDKDTDG
KDGTEYEGSF KANLFEVLLN YDAELNLNPF KLFFTTDIFM FFFQQDHKYS EELREITRNV
TTGNDLEDEE PLKAIQTISE LLTTSLTAAD IRIPISYLTF LIYWLFGDFK ATNDFLSDKS
VIKSLLSFSY QIQDEDVTIK CLVTMLLGVA YEFSSKESPF PRKEYFEFIT KTLGKDNYAS
RIKQFKKDSY FSKVDMNEDS ILTPELDETG LPKVYFSTYF IQLFNENIYR IRTALSHDPD
EEPINKISFE EVEKLQRQCT KLKGEITSLQ TETESTHENL TEKLIALTNE HKELDEKYQI
LNSSHSSLKE NFSILETELK NVRDSLDEMT QLRDVLETKD KENQTALLEY KSTIHKQEDS
IKTLEKGLET ILSQKKKAED GINKMGKDLF ALSREMQAVE ENCKNLQKEK DKSNVNHQKE
TKSLKEDIAA KITEIKAINE NLEEMKIQCN NLSKEKEHIS KELVEYKSRF QSHDNLVAKL
TEKLKSLANN YKDMQAENES LIKAVEESKN ESSIQLSNLQ NKIDSMSQEK ENFQIERGSI
EKNIEQLKKT ISDLEQTKEE IISKSDSSKD EYESQISLLK EKLETATTAN DENVNKISEL
TKTREELEAE LAAYKNLKNE LETKLETSEK ALKEVKENEE HLKEEKIQLE KEATETKQQL
NSLRANLESL EKEHEDLAAQ LKKYEEQIAN KERQYNEEIS QLNDEITSTQ QENESIKKKN
DELEGEVKAM KSTSEEQSNL KKSEIDALNL QIKELKKKNE TNEASLLESI KSVESETVKI
KELQDECNFK EKEVSELEDK LKASEDKNSK YLELQKESEK IKEELDAKTT ELKIQLEKIT
NLSKAKEKSE SELSRLKKTS SEERKNAEEQ LEKLKNEIQI KNQAFEKERK LLNEGSSTIT
QEYSEKINTL EDELIRLQNE NELKAKEIDN TRSELEKVSL SNDELLEEKQ NTIKSLQDEI
LSYKDKITRN DEKLLSIERD NKRDLESLKE QLRAAQESKA KVEEGLKKLE EESSKEKAEL
EKSKEMMKKL ESTIESNETE LKSSMETIRK SDEKLEQSKK SAEEDIKNLQ HEKSDLISRI
NESEKDIEEL KSKLRIEAKS GSELETVKQE LNNAQEKIRI NAEENTVLKS KLEDIERELK
DKQAEIKSNQ EEKELLTSRL KELEQELDST QQKAQKSEEE RRAEVRKFQV EKSQLDEKAM
LLETKYNDLV NKEQAWKRDE DTVKKTTDSQ RQEIEKLAKE LDNLKAENSK LKEANEDRSE
IDDLMLLVTD LDEKNAKYRS KLKDLGVEIS SDEEDDEEDD EEDEEEGQVA
