NUM1_YEAST
ID NUM1_YEAST Reviewed; 2748 AA.
AC Q00402; D6VSD2; Q03767;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Nuclear migration protein NUM1;
GN Name=NUM1; Synonyms=PAC12; OrderedLocusNames=YDR150W; ORFNames=YD8358.06;
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 FUNCTION.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=1745235; DOI=10.1007/bf00290678;
RA Kormanec J., Schaaff-Gerstenschlaeger I., Zimmermann F.K., Perecko D.,
RA Kuentzel H.;
RT "Nuclear migration in Saccharomyces cerevisiae is controlled by the highly
RT repetitive 313 kDa NUM1 protein.";
RL Mol. Gen. Genet. 230:277-287(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7490278; DOI=10.1083/jcb.131.4.1003;
RA Farkasovsky M., Kuentzel H.;
RT "Yeast Num1p associates with the mother cell cortex during S/G2 phase and
RT affects microtubular functions.";
RL J. Cell Biol. 131:1003-1014(1995).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11121446; DOI=10.1083/jcb.151.6.1337;
RA Heil-Chapdelaine R.A., Oberle J.R., Cooper J.A.;
RT "The cortical protein Num1p is essential for dynein-dependent interactions
RT of microtubules with the cortex.";
RL J. Cell Biol. 151:1337-1344(2000).
RN [6]
RP FUNCTION, INTERACTION WITH PAC11 AND TUB3, AND SUBCELLULAR LOCATION.
RX PubMed=11266443; DOI=10.1083/jcb.152.2.251;
RA Farkasovsky M., Kuentzel H.;
RT "Cortical Num1p interacts with the dynein intermediate chain Pac11p and
RT cytoplasmic microtubules in budding yeast.";
RL J. Cell Biol. 152:251-262(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2197, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611; SER-675; SER-746;
RP SER-881; SER-945; SER-1009; SER-1201; SER-1265; SER-1329; SER-2197;
RP SER-2220 AND SER-2221, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746; SER-881; SER-945;
RP SER-1201; SER-1265; SER-2162; SER-2164; SER-2217; SER-2220; SER-2221;
RP SER-2360; SER-2424; SER-2494 AND SER-2545, 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: Controls nuclear migration. NUM1 specifically controls the
CC interaction of the bud neck cytoskeleton with the pre-divisional G2
CC nucleus. Functions in dynein-anchoring. During late anaphase forms
CC dynein-interacting cortical microtubule capture sites at both cellular
CC poles. This leads to dynein-dependent sliding of the microtubules in
CC the bud. {ECO:0000269|PubMed:11121446, ECO:0000269|PubMed:11266443,
CC ECO:0000269|PubMed:1745235, ECO:0000269|PubMed:7490278}.
CC -!- SUBUNIT: Interacts with PAC11 when DYN1 is present, and TUB3.
CC {ECO:0000269|PubMed:11266443}.
CC -!- INTERACTION:
CC Q00402; P40075: SCS2; NbExp=4; IntAct=EBI-12386, EBI-16735;
CC Q00402; P09734: TUB3; NbExp=2; IntAct=EBI-12386, EBI-18981;
CC -!- SUBCELLULAR LOCATION: Bud tip {ECO:0000269|PubMed:11121446,
CC ECO:0000269|PubMed:11266443, ECO:0000269|PubMed:7490278}.
CC -!- MISCELLANEOUS: Additional regions of lower homology to the repeat
CC consensus (always starting with proline) are found in both flanking
CC domains of the tandem repeats.
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DR EMBL; X61236; CAA43554.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90372.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11992.1; -; Genomic_DNA.
DR PIR; S57976; S57976.
DR RefSeq; NP_010434.1; NM_001180457.1.
DR SMR; Q00402; -.
DR BioGRID; 32203; 444.
DR DIP; DIP-3018N; -.
DR IntAct; Q00402; 25.
DR MINT; Q00402; -.
DR STRING; 4932.YDR150W; -.
DR iPTMnet; Q00402; -.
DR MaxQB; Q00402; -.
DR PaxDb; Q00402; -.
DR PRIDE; Q00402; -.
DR EnsemblFungi; YDR150W_mRNA; YDR150W; YDR150W.
DR GeneID; 851727; -.
DR KEGG; sce:YDR150W; -.
DR SGD; S000002557; NUM1.
DR VEuPathDB; FungiDB:YDR150W; -.
DR eggNOG; ENOG502QRR7; Eukaryota.
DR HOGENOM; CLU_000674_0_0_1; -.
DR InParanoid; Q00402; -.
DR OMA; EQPNEQH; -.
DR BioCyc; YEAST:G3O-29744-MON; -.
DR PRO; PR:Q00402; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q00402; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IDA:SGD.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IBA:GO_Central.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IBA:GO_Central.
DR GO; GO:0032065; P:maintenance of protein location in cell cortex; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:SGD.
DR GO; GO:0000266; P:mitochondrial fission; IMP:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR InterPro; IPR024774; PH_dom-Mcp5-type.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF12814; Mcp5_PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2748
FT /note="Nuclear migration protein NUM1"
FT /id="PRO_0000057997"
FT REPEAT 593..656
FT /note="1"
FT REPEAT 657..727
FT /note="2"
FT REPEAT 728..798
FT /note="3"
FT REPEAT 799..862
FT /note="4"
FT REPEAT 863..926
FT /note="5"
FT REPEAT 927..990
FT /note="6"
FT REPEAT 991..1054
FT /note="7"
FT REPEAT 1055..1118
FT /note="8"
FT REPEAT 1119..1182
FT /note="9"
FT REPEAT 1183..1246
FT /note="10"
FT REPEAT 1247..1310
FT /note="11"
FT REPEAT 1311..1374
FT /note="12"
FT REPEAT 1375..1384
FT /note="13; truncated"
FT DOMAIN 2573..2683
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..1384
FT /note="13 X tandem repeats"
FT REGION 2111..2133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2444..2536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2707..2748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2119..2133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2444..2462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2516..2536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2711..2748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 2162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 2217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 2221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 2360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 1570
FT /note="A -> V (in Ref. 1; CAA43554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1822
FT /note="E -> K (in Ref. 1; CAA43554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1960..1962
FT /note="KAS -> RHL (in Ref. 1; CAA43554)"
FT /evidence="ECO:0000305"
FT CONFLICT 1971..1972
FT /note="KD -> RN (in Ref. 1; CAA43554)"
FT /evidence="ECO:0000305"
FT CONFLICT 2049
FT /note="S -> N (in Ref. 1; CAA43554)"
FT /evidence="ECO:0000305"
FT CONFLICT 2637
FT /note="V -> A (in Ref. 1; CAA43554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2748 AA; 313033 MW; EB4E48F950621142 CRC64;
MSHNNRHKKN NDKDSSAGQY ANSIDNSLSQ ESVSTNGVTR MANLKADECG SGDEGDKTKR
FSISSILSKR ETKDVLPEFA GSSSHNGVLT ANSSKDMNFT LELSENLLVE CRKLQSSNEA
KNEQIKSLKQ IKESLSDKIE ELTNQKKSFM KELDSTKDLN WDLESKLTNL SMECRQLKEL
KKKTEKSWND EKESLKLLKT DLEILTLTKN GMENDLSSQK LHYDKEISEL KERILDLNNE
NDRLLISVSD LTSEINSLQS NRTERIKIQK QLDDAKASIS SLKRKVQKKY YQKQHTSDTT
VTSDPDSEGT TSEEDIFDIV IEIDHMIETG PSVEDISEDL VKKYSEKNNM ILLSNDSYKN
LLQKSESASK PKDDELMTKE VAENLNMIAL PNDDNYSKKE FSLESHIKYL EASGYKVLPL
EEFENLNESL SNPSYNYLKE KLQALKKIPI DQSTFNLLKE PTIDFLLPLT SKIDCLIIPT
KDYNDLFESV KNPSIEQMKK CLEAKNDLQS NICKWLEERN GCKWLSNDLY FSMVNKIETP
SKQYLSDKAK EYDQVLIDTK ALEGLKNPTI DFLREKASAS DYLLLKKEDY VSPSLEYLVE
HAKATNHHLL SDSAYEDLVK CKENPDMEFL KEKSAKLGHT VVSNEAYSEL EKKLEQPSLE
YLVEHAKATN HHLLSDSAYE DLVKCKENPD MEFLKEKSAK LGHTVVSNEA YSELQRKYSE
LEKEVEQPSL AYLVEHAKAT DHHLLSDSAY EDLVKCKENP DVEFLKEKSA KLGHTVVSSE
EYSELQRKYS ELEKEVEQPS LAYLVEHAKA TDHHLLSDSA YEELVKCKEN PDMEFLKEKS
AKLGHTVVSN EAYSELEKKL EQPSLAYLVE HAKATDHHLL SDSAYEDLVK CKENSDVEFL
KEKSAKLGHT VVSNEAYSEL EKKLEQPSLA YLVEHAKATD HHLLSDSAYE DLVKCKENPD
MEFLKEKSAK LGHTVVSNEA YSELEKKLEQ PSLEYLVEHA KATNHHLLSD SAYEDLVKCK
ENPDMEFLKE KSAKLGHTVV SNEAYSELEK KLEQPSLEYL VEHAKATNHH LLSDSAYEEL
VKCKENPDVE FLKEKSAKLG HTVVSNEAYS ELEKKLEQPS LEYLVEHAKA TNHHLLSDSA
YEELVKCKEN PDVEFLKEKS AKLGHTVVSN EAYSELEKKL EQPSLAYLVE HAKATDHHLL
SDSAYEDLVK CKENPDVEFL KEKSAKLGHT VVSNEAYSEL EKKLEQPSLA YLVEHAKATD
HHLLSDSAYE DLVKCKENPD MEFLKEKSAK LGHTVVSNEA YSELEKKLEQ PSLEYLVEHA
KATNHHLLSD SAYEDLVKCK ENPDMEFLKE KSAKLGHTVV SNKEYSELEK KLEQPSLEYL
VKHAEQIQSK IISISDFNTL ANPSMEDMAS KLQKLEYQIV SNDEYIALKN TMEKPDVELL
RSKLKGYHII DTTTYNELVS NFNSPTLKFI EEKAKSKGYR LIEPNEYLDL NRIATTPSKE
EIDNFCKQIG CYALDSKEYE RLKNSLENPS KKFIEENAAL LDLVLVDKTE YQAMKDNASN
KKSLIPSTKA LDFVTMPAPQ LASAEKSSLQ KRTLSDIENE LKALGYVAIR KENLPNLEKP
IVDNASKNDV LNLCSKFSLV PLSTEEYDNM RKEHTKILNI LGDPSIDFLK EKCEKYQMLI
ISKHDYEEKQ EAIENPGYEF ILEKASALGY ELVSEVELDR MKQMIDSPDI DYMQEKAARN
EMVLLRNEEK EALQKKIEYP SLTFLIEKAA GMNKILVDQI EYDETIRKCN HPTRMELEES
CHHLNLVLLD QNEYSTLREP LENRNVEDLI NTLSKLNYIA IPNTIYQDLI GKYENPNFDY
LKDSLNKMDY VAISRQDYEL MVAKYEKPQL DYLKISSEKI DHIVVPLSEY NLMVTNYRNP
SLSYLKEKAV LNNHILIKED DYKNILAVSE HPTVIHLSEK ASLLNKVLVD KDDFATMSRS
IEKPTIDFLS TKALSMGKIL VNESTHKRNE KLLSEPDSEF LTMKAKEQGL IIISEKEYSE
LRDQIDRPSL DVLKEKAAIF DSIIVENIEY QQLVNTTSPC PPITYEDLKV YAHQFGMELC
LQKPNKLSGA ERAERIDEQS INTTSSNSTT TSSMFTDALD DNIEELNRVE LQNNEDYTDI
ISKSSTVKDA TIFIPAYENI KNSAEKLGYK LVPFEKSNIN LKNIEAPLFS KDNDDTSVAS
SIDLDHLSRK AEKYGMTLIS DQEFEEYHIL KDNAVNLNGG MEEMNNPLSE NQNLAAKTTN
TAQEGAFQNT VPHNDMDNEE VEYGPDDPTF TVRQLKKPAG DRNLILTSRE KTLLSRDDNI
MSQNEAVYGD DISDSFVDES QEIKNDVDII KTQAMKYGML CIPESNFVGA SYASAQDMSD
IVVLSASYYH NLMSPEDMKW NCVSNEELQA EVKKRGLQIA LTTKEDKKGQ ATASKHEYVS
HKLNNKTSTV STKSGAKKGL AEAAATTAYE DSESHPQIEE QSHRTNHHKH HKRQQSLNSN
STSKTTHSSR NTPASRRDIV ASFMSRAGSA SRTASLQTLA SLNEPSIIPA LTQTVIGEYL
FKYYPRLGPF GFESRHERFF WVHPYTLTLY WSASNPILEN PANTKTKGVA ILGVESVTDP
NPYPTGLYHK SIVVTTETRT IKFTCPTRQR HNIWYNSLRY LLQRNMQGIS LEDIADDPTD
NMYSGKIFPL PGENTKSSSK RLSASRRSVS TRSLRHRVPQ SRSFGNLR
