LTE1_YEAST
ID LTE1_YEAST Reviewed; 1435 AA.
AC P07866; D6VPJ4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Guanine nucleotide exchange factor LTE1;
DE AltName: Full=Low temperature essential protein 1;
GN Name=LTE1; Synonyms=EIS4, MSI2; OrderedLocusNames=YAL024C;
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 204511 / S288c / AB972;
RX PubMed=7985422; DOI=10.1002/yea.320100710;
RA Keng T., Clark M.W., Storms R.K., Fortin N., Zhong W., Ouellette B.F.F.,
RA Barton A.B., Kaback D.B., Bussey H.;
RT "LTE1 of Saccharomyces cerevisiae is a 1435 codon open reading frame that
RT has sequence similarities to guanine nucleotide releasing factors.";
RL Yeast 10:953-958(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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], AND FUNCTION.
RX PubMed=7941731; DOI=10.1002/yea.320100404;
RA Shirayama M., Matsui Y., Tanaka K., Toh-e A.;
RT "Isolation of a CDC25 family gene, MSI2/LTE1, as a multicopy suppressor of
RT ira1.";
RL Yeast 10:451-461(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1127-1435, AND FUNCTION.
RX PubMed=3332963; DOI=10.1002/yea.320030108;
RA Wickner R.B., Koh T.J., Crowley J.C., O'Neil J., Kaback D.B.;
RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT isolation of the MAK16 gene and analysis of an adjacent gene essential for
RT growth at low temperatures.";
RL Yeast 3:51-57(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1404-1435.
RX PubMed=3045810; DOI=10.1073/pnas.85.16.6007;
RA Wickner R.B.;
RT "Host function of MAK16: G1 arrest by a mak16 mutant of Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6007-6011(1988).
RN [7]
RP FUNCTION.
RX PubMed=7935462; DOI=10.1128/mcb.14.11.7476-7482.1994;
RA Shirayama M., Matsui Y., Toh-e A.;
RT "The yeast TEM1 gene, which encodes a GTP-binding protein, is involved in
RT termination of M phase.";
RL Mol. Cell. Biol. 14:7476-7482(1994).
RN [8]
RP FUNCTION.
RX PubMed=10219244; DOI=10.1016/s0092-8674(00)80733-3;
RA Shou W., Seol J.H., Shevchenko A., Baskerville C., Moazed D., Chen Z.W.S.,
RA Jang J., Shevchenko A., Charbonneau H., Deshaies R.J.;
RT "Exit from mitosis is triggered by Tem1-dependent release of the protein
RT phosphatase Cdc14 from nucleolar RENT complex.";
RL Cell 97:233-244(1999).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10929710; DOI=10.1016/s0092-8674(00)00007-6;
RA Bardin A.J., Visintin R., Amon A.;
RT "A mechanism for coupling exit from mitosis to partitioning of the
RT nucleus.";
RL Cell 102:21-31(2000).
RN [10]
RP FUNCTION.
RX PubMed=11101520; DOI=10.1093/emboj/19.23.6475;
RA Gruneberg U., Campbell K., Simpson C., Grindlay J., Schiebel E.;
RT "Nud1p links astral microtubule organization and the control of exit from
RT mitosis.";
RL EMBO J. 19:6475-6488(2000).
RN [11]
RP FUNCTION.
RX PubMed=11285282; DOI=10.1083/jcb.153.1.159;
RA Adames N.R., Oberle J.R., Cooper J.A.;
RT "The surveillance mechanism of the spindle position checkpoint in yeast.";
RL J. Cell Biol. 153:159-168(2001).
RN [12]
RP PHOSPHORYLATION.
RX PubMed=11493673; DOI=10.1242/jcs.114.12.2345;
RA Lee S.E., Jensen S., Frenz L.M., Johnson A.L., Fesquet D., Johnston L.H.;
RT "The Bub2-dependent mitotic pathway in yeast acts every cell cycle and
RT regulates cytokinesis.";
RL J. Cell Sci. 114:2345-2354(2001).
RN [13]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH KEL1.
RX PubMed=12498684; DOI=10.1016/s0960-9822(02)01388-x;
RA Seshan A., Bardin A.J., Amon A.;
RT "Control of Lte1 localization by cell polarity determinants and Cdc14.";
RL Curr. Biol. 12:2098-2110(2002).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP CDC24; CDC42; KEL1; KEL2 AND TEM1.
RX PubMed=12234925; DOI=10.1093/emboj/cdf481;
RA Hoefken T., Schiebel E.;
RT "A role for cell polarity proteins in mitotic exit.";
RL EMBO J. 21:4851-4862(2002).
RN [15]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDC28, AND DEPHOSPHORYLATION BY
RP CDC14.
RX PubMed=12432084; DOI=10.1242/jcs.00189;
RA Jensen S., Geymonat M., Johnson A.L., Segal M., Johnston L.H.;
RT "Spatial regulation of the guanine nucleotide exchange factor Lte1 in
RT Saccharomyces cerevisiae.";
RL J. Cell Sci. 115:4977-4991(2002).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12699621; DOI=10.1016/s0960-9822(03)00247-1;
RA Castillon G.A., Adames N.R., Rosello C.H., Seidel H.S., Longtine M.S.,
RA Cooper J.A., Heil-Chapdelaine R.A.;
RT "Septins have a dual role in controlling mitotic exit in budding yeast.";
RL Curr. Biol. 13:654-658(2003).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAS2.
RX PubMed=12782684; DOI=10.1083/jcb.200301128;
RA Yoshida S., Ichihashi R., Toh-e A.;
RT "Ras recruits mitotic exit regulator Lte1 to the bud cortex in budding
RT yeast.";
RL J. Cell Biol. 161:889-897(2003).
RN [18]
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 [19]
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 [20]
RP FUNCTION.
RX PubMed=15197338;
RA Jensen S., Johnson A.L., Johnston L.H., Segal M.;
RT "Temporal coupling of spindle disassembly and cytokinesis is disrupted by
RT deletion of LTE1 in budding yeast.";
RL Cell Cycle 3:817-822(2004).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14718561; DOI=10.1091/mbc.e03-09-0708;
RA Molk J.N., Schuyler S.C., Liu J.Y., Evans J.G., Salmon E.D., Pellman D.,
RA Bloom K.;
RT "The differential roles of budding yeast Tem1p, Cdc15p, and Bub2p protein
RT dynamics in mitotic exit.";
RL Mol. Biol. Cell 15:1519-1532(2004).
RN [22]
RP FUNCTION.
RX PubMed=17121813; DOI=10.1074/jbc.m610500200;
RA Zhao X., Chang A.Y., Toh-e A., Arvan P.;
RT "A role for Lte1p (a low temperature essential protein involved in mitosis)
RT in proprotein processing in the yeast secretory pathway.";
RL J. Biol. Chem. 282:1670-1678(2007).
RN [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271 AND SER-1028, 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559; SER-689; THR-691;
RP SER-808; SER-810; SER-1028 AND SER-1109, AND IDENTIFICATION BY MASS
RP 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: GDP-GTP exchange factor for TEM1, a Ras-like protein,
CC component of the mitotic exit network (MEN). Activation of TEM1 by LTE1
CC in the bud ultimately leads to activation of CDC15 followed by the
CC release of CDC14 from the nucleolus, which then inactivates cyclin-
CC dependent kinases (CDKs) activity by several mechanism. Required for
CC TEM1 localization to the bud cortex during mitotic exit. Fine-tunes the
CC timing of the mitotic exit and couples this event with cytokinesis.
CC -!- FUNCTION: Involved in proprotein-processing like proalpha factor-
CC processing in the secretory pathway.
CC -!- SUBUNIT: Interacts with CDC24, CDC42, KEL1, KEL2, RAS2 and TEM1.
CC {ECO:0000269|PubMed:12234925, ECO:0000269|PubMed:12498684,
CC ECO:0000269|PubMed:12782684}.
CC -!- INTERACTION:
CC P07866; P38853: KEL1; NbExp=3; IntAct=EBI-10243, EBI-9619;
CC P07866; P01120: RAS2; NbExp=5; IntAct=EBI-10243, EBI-14838;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Bud. Note=The localization to the bud
CC requires interaction with KEL1, as well as the presence of septins,
CC CDC42, CLA4 and RAS2.
CC -!- PTM: Phosphorylated by CDC28 in a cell cycle-dependent manner and in
CC response to nocodazole. Dephosphorylion by CDC14 triggers LTE1 release
CC from bud cortex during the exit of mitosis.
CC {ECO:0000269|PubMed:11493673, ECO:0000269|PubMed:12234925,
CC ECO:0000269|PubMed:12432084, ECO:0000269|PubMed:12498684}.
CC -!- MISCELLANEOUS: Present with 304 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LTE1 family. {ECO:0000305}.
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DR EMBL; L20125; AAA50468.1; -; Genomic_DNA.
DR EMBL; U12980; AAC05008.1; -; Genomic_DNA.
DR EMBL; D21354; BAA04820.1; -; Genomic_DNA.
DR EMBL; M16076; AAA34746.1; -; Genomic_DNA.
DR EMBL; J03852; AAA34751.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06964.1; -; Genomic_DNA.
DR PIR; S51997; BVBYL1.
DR RefSeq; NP_009378.1; NM_001178169.1.
DR AlphaFoldDB; P07866; -.
DR SMR; P07866; -.
DR BioGRID; 31742; 601.
DR DIP; DIP-337N; -.
DR IntAct; P07866; 58.
DR MINT; P07866; -.
DR STRING; 4932.YAL024C; -.
DR CarbonylDB; P07866; -.
DR iPTMnet; P07866; -.
DR MaxQB; P07866; -.
DR PaxDb; P07866; -.
DR PRIDE; P07866; -.
DR EnsemblFungi; YAL024C_mRNA; YAL024C; YAL024C.
DR GeneID; 851209; -.
DR KEGG; sce:YAL024C; -.
DR SGD; S000000022; LTE1.
DR VEuPathDB; FungiDB:YAL024C; -.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_004883_0_0_1; -.
DR InParanoid; P07866; -.
DR OMA; PFILMYD; -.
DR BioCyc; YEAST:G3O-28835-MON; -.
DR Reactome; R-SCE-354192; Integrin signaling.
DR Reactome; R-SCE-392517; Rap1 signalling.
DR Reactome; R-SCE-416482; G alpha (12/13) signalling events.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR PRO; PR:P07866; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P07866; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:SGD.
DR GO; GO:0061510; P:asymmetric protein localization to new mitotic spindle pole body; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IGI:SGD.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Guanine-nucleotide releasing factor;
KW Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..1435
FT /note="Guanine nucleotide exchange factor LTE1"
FT /id="PRO_0000068884"
FT DOMAIN 25..157
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 1194..1434
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 235..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 998..1009
FT /note="TNSNISGSVLTM -> LIVHIRKCIDN (in Ref. 4; BAA04820)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161..1163
FT /note="AAQ -> GE (in Ref. 5; AAA34746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1435 AA; 163150 MW; EED7E5150BECA3DE CRC64;
MEIFSQKDYY PTPSSNVISY ESDCVSKPVN SADLPALIVH LSSPLEGVDY NASADFFLIY
RNFITPQDLH DLLIYRFRWC IREITTNAAK AKRRRIGEVA LVRTFVLLRH SILNYFVQDF
LPNITLRLRL IEFLNDKHIE QYPKIISSCI INLKKNWVHC SKLVWENIEL NEPDKLDFDA
WLHYSLKDFT QLESLHKRGS RLSIYARQSF ASPDFRNQSV LSLYKTSDVF RLPEKLQSSN
SSKNQRSPSM LLFPDNTSNV YSKHRIAKEP SVDNESEDMS DSKQKISHLS KVTLVSTLMK
GVDYPSSYAV DKIMPPTPAK KVEFILNSLY IPEDLNEQSG TLQGTSTTSS LDNNSNSNSR
SNTSSMSVLH RSAIGLLAKW MKNHNRHDSS NDKKFMSAIK PANQKPEMDA FVKYVVSISS
LNRKSSKEEE EEFLNSDSSK FDILSARTID EVESLLHLQN QLIEKVQTHS NNNRGPTVNV
DCERREHIHD IKILQQNSFK PSNDNFSAMD NLDLYQTVSS IAQSVISLTN TLNKQLQNNE
SNMQPSPSYD ALQRRKVKSL TTAYYNKMHG SYSAESMRLF DKDNSSSRTD ENGPQRLLFH
ETDKTNSEAI TNMTPRRKNH SQSQKSMTSS PLKNVLPDLK ESSPLNDSRE DTESITYSYD
SELSSSSPPR DTVTKKSRKV RNIVNNTDSP TLKTKTGFLN LREFTFEDTK SLDEKKSTID
GLEKNYDNKE NQESEYESTK KLDNSLDASS EANNYDITTR KKHSSCNHKI KQAVVRPASG
RISISRVQSI AITPTKELSI VDPEQNKSNS VIEEISEIEP LNLEYNKKSA LYSDTSSTVI
SISTSKLFES AQNSPLKQTQ NPQREFPNGT SVSETNRIRL SIAPTIESVV SDLNSITTGS
TVETFETSRD LPVPHQRIIN LREEYQRGNQ DIISNTSSLH ELKTIDLSDS NNDLESPSTH
AKNNKYFFSP DDGSIDVASP MKNVEELKSK FLKNESETNS NISGSVLTMD DIDINDTSSA
RNTRRANSES AFTGSLNKKN LNEIANMLDD SINDDPITVA LMKLEGTYEK IPEKPENTKS
SDAIGIKTSK LADEVEMLNL NNLPSFQNSP AEKRKSLLIE RRRQTIMNIP FTPDQSEKEG
FTSSSPEKID VSANVDVAVQ AAQIQELIGQ YRIHDSRLMI SNNESHVPFI LMYDSLSVAQ
QMTLIEKEIL GEIDWKDLLD LKMKHEGPQV ISWLQLLVRN ETLSGIDLAI SRFNLTVDWI
ISEILLTKSS KMKRNVIQRF IHVADHCRTF QNFNTLMEII LALSSSVVQK FTDAWRLIEP
GDLLTWEELK KIPSLDRNYS TIRNLLNSVN PLVGCVPFIV VYLSDLSANA EKKDWILEDK
VVNYNKFDTN VQIVKNFIQR VQWSKFYTFK VNHELLSKCV YISTLTQEEI NELST
