CDC13_YEAST
ID CDC13_YEAST Reviewed; 924 AA.
AC P32797; D6VRD4; Q07650;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cell division control protein 13;
GN Name=CDC13; OrderedLocusNames=YDL220C;
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].
RX PubMed=7565765; DOI=10.1128/mcb.15.11.6128;
RA Garvik B., Carson M., Hartwell L.;
RT "Single-stranded DNA arising at telomeres in cdc13 mutants may constitute a
RT specific signal for the RAD9 checkpoint.";
RL Mol. Cell. Biol. 15:6128-6138(1995).
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 INTERACTION WITH TEN1.
RX PubMed=11230140; DOI=10.1093/emboj/20.5.1173;
RA Grandin N., Damon C., Charbonneau M.;
RT "Ten1 functions in telomere end protection and length regulation in
RT association with Stn1 and Cdc13.";
RL EMBO J. 20:1173-1183(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH STN1.
RX PubMed=11230149; DOI=10.1101/gad.861001;
RA Chandra A., Hughes T.R., Nugent C.I., Lundblad V.;
RT "Cdc13 both positively and negatively regulates telomere replication.";
RL Genes Dev. 15:404-414(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH EST1.
RX PubMed=11390652; DOI=10.1128/mcb.21.13.4233-4245.2001;
RA Meier B., Driller L., Jaklin S., Feldmann H.M.;
RT "New function of CDC13 in positive telomere length regulation.";
RL Mol. Cell. Biol. 21:4233-4245(2001).
RN [7]
RP FUNCTION, INTERACTION WITH EST1; FUN12 AND POL1, AND MUTAGENESIS OF LYS-50;
RP ILE-72; CYS-124; LEU-149; SER-228; GLY-243; LEU-392 AND ILE-523.
RX PubMed=10898792;
RA Qi H., Zakian V.A.;
RT "The Saccharomyces telomere-binding protein Cdc13p interacts with both the
RT catalytic subunit of DNA polymerase alpha and the telomerase-associated
RT est1 protein.";
RL Genes Dev. 14:1777-1788(2000).
RN [8]
RP INTERACTION WITH STM1.
RX PubMed=12207228; DOI=10.1007/s00438-002-0712-3;
RA Hayashi N., Murakami S.;
RT "STM1, a gene which encodes a guanine quadruplex binding protein, interacts
RT with CDC13 in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 267:806-813(2002).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND THR-308, 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 [12]
RP STRUCTURE BY NMR OF DNA-BINDING DOMAIN IN COMPLEX WITH DNA.
RX PubMed=11935027; DOI=10.1126/science.1068799;
RA Mitton-Fry R.M., Anderson E.M., Hughes T.R., Lundblad V., Wuttke D.S.;
RT "Conserved structure for single-stranded telomeric DNA recognition.";
RL Science 296:145-147(2002).
RN [13]
RP STRUCTURE BY NMR OF DNA-BINDING DOMAIN IN COMPLEX WITH DNA.
RX PubMed=15066429; DOI=10.1016/j.jmb.2004.01.063;
RA Mitton-Fry R.M., Anderson E.M., Theobald D.L., Glustrom L.W., Wuttke D.S.;
RT "Structural basis for telomeric single-stranded DNA recognition by yeast
RT Cdc13.";
RL J. Mol. Biol. 338:241-255(2004).
CC -!- FUNCTION: Single-stranded telomeric DNA-binding protein that regulates
CC telomere replication. Has a role in both positive and negative
CC regulation. Promotes [TG(1-3)] strand lengthening via interaction with
CC EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha
CC via interaction with POL1. Negatively regulates telomere elongation of
CC the G strand via binding with STN1 thereby inhibiting telomerase
CC activity. {ECO:0000269|PubMed:10898792, ECO:0000269|PubMed:11230149,
CC ECO:0000269|PubMed:11390652}.
CC -!- SUBUNIT: Interacts with POL1, EST1, FUN12, STM1, STN1 and TEN1.
CC {ECO:0000269|PubMed:10898792, ECO:0000269|PubMed:11230140,
CC ECO:0000269|PubMed:11230149, ECO:0000269|PubMed:11390652,
CC ECO:0000269|PubMed:11935027, ECO:0000269|PubMed:12207228,
CC ECO:0000269|PubMed:15066429}.
CC -!- INTERACTION:
CC P32797; P32797: CDC13; NbExp=4; IntAct=EBI-4187, EBI-4187;
CC P32797; P17214: EST1; NbExp=3; IntAct=EBI-4187, EBI-6684;
CC P32797; P13382: POL1; NbExp=4; IntAct=EBI-4187, EBI-6128;
CC P32797; Q12306: SMT3; NbExp=3; IntAct=EBI-4187, EBI-17490;
CC P32797; P38960: STN1; NbExp=10; IntAct=EBI-4187, EBI-18427;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M76550; AAA99990.1; -; Genomic_DNA.
DR EMBL; Z74269; CAA98800.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11644.1; -; Genomic_DNA.
DR PIR; S67783; S27421.
DR RefSeq; NP_010061.1; NM_001180280.1.
DR PDB; 1KXL; NMR; -; A=497-694.
DR PDB; 1S40; NMR; -; A=497-694.
DR PDB; 3NWS; X-ray; 2.50 A; A/B/C/D=13-227.
DR PDB; 3NWT; X-ray; 2.70 A; A=13-227.
DR PDB; 3OIP; X-ray; 2.50 A; A=12-243.
DR PDB; 3OIQ; X-ray; 2.40 A; A=12-243.
DR PDB; 4HCE; X-ray; 2.30 A; A/B=344-495.
DR PDBsum; 1KXL; -.
DR PDBsum; 1S40; -.
DR PDBsum; 3NWS; -.
DR PDBsum; 3NWT; -.
DR PDBsum; 3OIP; -.
DR PDBsum; 3OIQ; -.
DR PDBsum; 4HCE; -.
DR AlphaFoldDB; P32797; -.
DR BMRB; P32797; -.
DR SMR; P32797; -.
DR BioGRID; 31825; 800.
DR ComplexPortal; CPX-15; CST complex.
DR DIP; DIP-1229N; -.
DR IntAct; P32797; 26.
DR MINT; P32797; -.
DR STRING; 4932.YDL220C; -.
DR iPTMnet; P32797; -.
DR MaxQB; P32797; -.
DR PaxDb; P32797; -.
DR PRIDE; P32797; -.
DR EnsemblFungi; YDL220C_mRNA; YDL220C; YDL220C.
DR GeneID; 851306; -.
DR KEGG; sce:YDL220C; -.
DR SGD; S000002379; CDC13.
DR VEuPathDB; FungiDB:YDL220C; -.
DR eggNOG; ENOG502QU50; Eukaryota.
DR HOGENOM; CLU_011303_0_0_1; -.
DR InParanoid; P32797; -.
DR OMA; KYITMFG; -.
DR BioCyc; YEAST:G3O-29601-MON; -.
DR EvolutionaryTrace; P32797; -.
DR PRO; PR:P32797; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32797; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:1990879; C:CST complex; IPI:SGD.
DR GO; GO:0000783; C:nuclear telomere cap complex; IBA:GO_Central.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0010521; F:telomerase inhibitor activity; IDA:SGD.
DR GO; GO:0061770; F:translation elongation factor binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IDA:SGD.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IDA:SGD.
DR GO; GO:0071166; P:ribonucleoprotein complex localization; IMP:SGD.
DR GO; GO:0016233; P:telomere capping; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR031749; Cdc13_N.
DR InterPro; IPR040650; Cdc13_OB2.
DR InterPro; IPR041028; Cdc13_OB4_dimer.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR028389; POT1.
DR InterPro; IPR011564; Telomer_end-bd_POT1/Cdc13.
DR PANTHER; PTHR14513; PTHR14513; 1.
DR Pfam; PF16853; CDC13_N; 1.
DR Pfam; PF18691; Cdc13_OB2; 1.
DR Pfam; PF18233; Cdc13_OB4_dimer; 1.
DR Pfam; PF02765; POT1; 1.
DR SMART; SM00976; Telo_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; DNA-binding;
KW Phosphoprotein; Reference proteome; Telomere.
FT CHAIN 1..924
FT /note="Cell division control protein 13"
FT /id="PRO_0000089441"
FT DNA_BIND 500..686
FT /note="OB"
FT REGION 265..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MUTAGEN 50
FT /note="K->Q: Increase in length of X' and Y' telomeres.
FT Disrupts interaction with POL1 but not FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 72
FT /note="I->T: Disrupts interaction with POL1 and FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 124
FT /note="C->R: Disrupts interaction with POL1 but not FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 149
FT /note="L->S: Disrupts interaction with POL1 but not FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 228
FT /note="S->P: Disrupts interaction with POL1 but not FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 243
FT /note="G->R: Disrupts interaction with POL1 and FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 392
FT /note="L->P: Disrupts interaction with POL1 but not FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT MUTAGEN 523
FT /note="I->V: Increase in length of X' and Y' telomeres.
FT Disrupts interaction with POL1 but not FUN12."
FT /evidence="ECO:0000269|PubMed:10898792"
FT CONFLICT 40
FT /note="L -> A (in Ref. 1; AAA99990)"
FT /evidence="ECO:0000305"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 32..46
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3NWT"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 138..148
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:3OIQ"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:3OIQ"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 359..372
FT /evidence="ECO:0007829|PDB:4HCE"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4HCE"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:4HCE"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:4HCE"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:4HCE"
FT HELIX 429..436
FT /evidence="ECO:0007829|PDB:4HCE"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 444..453
FT /evidence="ECO:0007829|PDB:4HCE"
FT STRAND 463..472
FT /evidence="ECO:0007829|PDB:4HCE"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:1KXL"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 575..580
FT /evidence="ECO:0007829|PDB:1KXL"
FT HELIX 581..592
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1KXL"
FT HELIX 599..602
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 617..624
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:1KXL"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:1KXL"
FT HELIX 645..648
FT /evidence="ECO:0007829|PDB:1KXL"
FT HELIX 653..668
FT /evidence="ECO:0007829|PDB:1KXL"
FT HELIX 670..675
FT /evidence="ECO:0007829|PDB:1KXL"
FT HELIX 677..680
FT /evidence="ECO:0007829|PDB:1KXL"
SQ SEQUENCE 924 AA; 104904 MW; 9FE0AD08520A6F8A CRC64;
MDTLEEPECP PHKNRIFVSS SKDFEGYPSK AIVPVQFVAL LTSIHLTETK CLLGFSNFER
RGDQSQEDQY LIKLKFKDRG SERLARITIS LLCQYFDIEL PDLDSDSGAS PTVILRDIHL
ERLCFSSCKA LYVSKHGNYT LFLEDIKPLD LVSVISTIST KSTNSSKHSS SELISECDLN
NSLVDIFNNL IEMNRDEKNR FKFVKLIHYD IELKKFVQDQ QKVLSQKSKA AAINPFFVPN
RLGIPYIESQ NEFNSQLMTL NVDEPTTDIS NMGEEMHDSA DPIEDSDSST TSSTGKYFSS
KSYIQSQTPE RKTSVPNNWH DDDSGSKRKR KLSFHSPNAS SIRKAISYEQ LSLASVGSVE
RLEGKIVGMN PPQFASINEF KYCTLKLYFT QLLPNVPDKV LVPGVNCIEI VIPTRERICE
LFGVLNCQSD KISDILLLEK PDRISVEVER ILWDNDKTAS PGMAVWSLKN ISTDTQAQAQ
VQVPAQSSAS IDPSRTRMSK MARKDPTIEF CQLGLDTFET KYITMFGMLV SCSFDKPAFI
SFVFSDFTKN DIVQNYLYDR YLIDYENKLE LNEGFKAIMY KNQFETFDSK LRKIFNNGLR
DLQNGRDENL SQYGIVCKMN IKVKMYNGKL NAIVRECEPV PHSQISSIAS PSQCEHLRLF
YQRAFKRIGE SAISRYFEEY RRFFPIHRNG SHLAKLRFDE VKHEPKKSPT TPALAEHIPD
LNADVSSFDV KFTDISSLLD SSARLPRPQQ THKSNTLYSC EGRIIAIEYH ASDLCFHITN
ELPLLQTRGL APERVLQLHI ITSKNFAYFF NRSSAYLQRQ PLEEKYTQLA QFLGHSFKFN
ITSSLTLFPD TTVALQIWCP IECTFRELQQ QLAHPKVAAA PDSGSLDCAI NATVNPLRLL
AAQNGVTVKK EEDNDDDAGA VPTS
