SIZ1_YEAST
ID SIZ1_YEAST Reviewed; 904 AA.
AC Q04195; D6VT41; Q06762; Q7LIJ4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=E3 SUMO-protein ligase SIZ1;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase SIZ2 {ECO:0000305};
DE AltName: Full=SAP and Miz-finger domain-containing protein 1;
DE AltName: Full=Ubiquitin-like protein ligase 1;
GN Name=SIZ1; Synonyms=ULL1; OrderedLocusNames=YDR409W;
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 709-904.
RC STRAIN=JRY3205;
RX PubMed=8212897; DOI=10.1002/yea.320090810;
RA Ashby M.N., Errada P.R., Boyartchuk V.L., Rine J.;
RT "Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine:
RT carboxyl methyltransferase.";
RL Yeast 9:907-913(1993).
RN [4]
RP FUNCTION, INTERACTION WITH UBC9, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=11572779; DOI=10.1016/s0092-8674(01)00491-3;
RA Johnson E.S., Gupta A.A.;
RT "An E3-like factor that promotes SUMO conjugation to the yeast septins.";
RL Cell 106:735-744(2001).
RN [5]
RP FUNCTION, INTERACTION WITH UBC9 AND CDC3, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF CYS-377, AND PHOSPHORYLATION.
RX PubMed=11587849; DOI=10.1016/s0378-1119(01)00662-x;
RA Takahashi Y., Toh-e A., Kikuchi Y.;
RT "A novel factor required for the SUMO1/Smt3 conjugation of yeast septins.";
RL Gene 275:223-231(2001).
RN [6]
RP FUNCTION.
RX PubMed=11333221; DOI=10.1093/genetics/158.1.95;
RA Strunnikov A.V., Aravind L., Koonin E.V.;
RT "Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease
RT with a role in chromosome condensation regulation.";
RL Genetics 158:95-107(2001).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF CYS-361; CYS-377; CYS-400 AND SER-460.
RX PubMed=11577116; DOI=10.1074/jbc.m109295200;
RA Takahashi Y., Kahyo T., Toh-e A., Yasuda H., Kikuchi Y.;
RT "Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and
RT functions as an adaptor between conjugating enzyme and substrates.";
RL J. Biol. Chem. 276:48973-48977(2001).
RN [8]
RP FUNCTION.
RX PubMed=12226657; DOI=10.1038/nature00991;
RA Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
RT "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin
RT and SUMO.";
RL Nature 419:135-141(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-377.
RX PubMed=12761287; DOI=10.1093/jb/mvg054;
RA Takahashi Y., Toh-e A., Kikuchi Y.;
RT "Comparative analysis of yeast PIAS-type SUMO ligases in vivo and in
RT vitro.";
RL J. Biochem. 133:415-422(2003).
RN [10]
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 [11]
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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16109721; DOI=10.1074/jbc.m506794200;
RA Takahashi Y., Kikuchi Y.;
RT "Yeast PIAS-type Ull1/Siz1 is composed of SUMO ligase and regulatory
RT domains.";
RL J. Biol. Chem. 280:35822-35828(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-794, 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 [15]
RP IDENTIFICATION BY 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: Acts as an E3 ligase mediating SUMO/Smt3 attachment to
CC septins and PCNA. May be involved in chromosome maintenance.
CC {ECO:0000269|PubMed:11333221, ECO:0000269|PubMed:11572779,
CC ECO:0000269|PubMed:11577116, ECO:0000269|PubMed:11587849,
CC ECO:0000269|PubMed:12226657}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with UBC9 and CDC3. {ECO:0000269|PubMed:11572779,
CC ECO:0000269|PubMed:11587849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16109721}. Nucleus
CC {ECO:0000269|PubMed:11572779, ECO:0000269|PubMed:16109721}. Bud neck
CC {ECO:0000269|PubMed:11572779, ECO:0000269|PubMed:11587849,
CC ECO:0000269|PubMed:12761287, ECO:0000269|PubMed:16109721}. Note=Present
CC at the bud neck in early M-phase. {ECO:0000269|PubMed:11587849}.
CC -!- DOMAIN: The SAP domain is required for nuclear targeting.
CC -!- DOMAIN: The SP-RING-type zinc finger mediates interaction with UBC9 and
CC CDC3 and is required for E3 activity.
CC -!- PTM: Phosphorylated in early M-phase. {ECO:0000269|PubMed:11572779,
CC ECO:0000269|PubMed:11587849}.
CC -!- PTM: Autosumoylated upon ethanol stress. {ECO:0000269|PubMed:15166219}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; U32274; AAB64849.1; -; Genomic_DNA.
DR EMBL; L07952; AAA16519.1; -; Unassigned_DNA.
DR EMBL; BK006938; DAA12251.1; -; Genomic_DNA.
DR PIR; S69691; S69691.
DR RefSeq; NP_010697.3; NM_001180717.3.
DR PDB; 2RNN; NMR; -; A=1-111.
DR PDB; 3I2D; X-ray; 2.60 A; A=112-465.
DR PDB; 5JNE; X-ray; 2.85 A; A/E=167-449.
DR PDBsum; 2RNN; -.
DR PDBsum; 3I2D; -.
DR PDBsum; 5JNE; -.
DR AlphaFoldDB; Q04195; -.
DR BMRB; Q04195; -.
DR SMR; Q04195; -.
DR BioGRID; 32469; 227.
DR DIP; DIP-1011N; -.
DR IntAct; Q04195; 2.
DR MINT; Q04195; -.
DR STRING; 4932.YDR409W; -.
DR iPTMnet; Q04195; -.
DR MaxQB; Q04195; -.
DR PaxDb; Q04195; -.
DR PRIDE; Q04195; -.
DR EnsemblFungi; YDR409W_mRNA; YDR409W; YDR409W.
DR GeneID; 852018; -.
DR KEGG; sce:YDR409W; -.
DR SGD; S000002817; SIZ1.
DR VEuPathDB; FungiDB:YDR409W; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_014307_0_0_1; -.
DR InParanoid; Q04195; -.
DR OMA; YIVEMIT; -.
DR BioCyc; YEAST:G3O-29952-MON; -.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR UniPathway; UPA00886; -.
DR EvolutionaryTrace; Q04195; -.
DR PRO; PR:Q04195; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04195; protein.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005940; C:septin ring; IDA:SGD.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IGI:SGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:SGD.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..904
FT /note="E3 SUMO-protein ligase SIZ1"
FT /id="PRO_0000245783"
FT DOMAIN 34..68
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 162..314
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 344..431
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..904
FT /note="Required for localization at the bud neck"
FT REGION 877..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 361
FT /note="C->S: Reduces E3 activity."
FT /evidence="ECO:0000269|PubMed:11577116"
FT MUTAGEN 377
FT /note="C->S: Strongly reduces E3 activity, but no effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:11577116,
FT ECO:0000269|PubMed:11587849, ECO:0000269|PubMed:12761287"
FT MUTAGEN 400
FT /note="C->S: Reduces E3 activity."
FT /evidence="ECO:0000269|PubMed:11577116"
FT MUTAGEN 460
FT /note="S->C: No effect on E3 activity."
FT /evidence="ECO:0000269|PubMed:11577116"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2RNN"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2RNN"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:2RNN"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2RNN"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:2RNN"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:2RNN"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2RNN"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 183..196
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 226..236
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5JNE"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 291..302
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 331..343
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:3I2D"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:3I2D"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:3I2D"
FT HELIX 416..422
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:3I2D"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3I2D"
SQ SEQUENCE 904 AA; 100796 MW; CBD581DFF23F7802 CRC64;
MINLEDYWED ETPGPDREPT NELRNEVEET ITLMELLKVS ELKDICRSVS FPVSGRKAVL
QDLIRNFLQN ALVVGKSDPY RVQAVKFLIE RIRKNEPLPV YKDLWNALRK GTPLSAITVR
SMEGPPTVQQ QSPSVIRQSP TQRRKTSTTS STSRAPPPTN PDASSSSSSF AVPTIHFKES
PFYKIQRLIP ELVMNVEVTG GRGMCSAKFK LSKADYNLLS NPNSKHRLYL FSGMINPLGS
RGNEPIQFPF PNELRCNNVQ IKDNIRGFKS KPGTAKPADL TPHLKPYTQQ NNVELIYAFT
TKEYKLFGYI VEMITPEQLL EKVLQHPKII KQATLLYLKK TLREDEEMGL TTTSTIMSLQ
CPISYTRMKY PSKSINCKHL QCFDALWFLH SQLQIPTWQC PVCQIDIALE NLAISEFVDD
ILQNCQKNVE QVELTSDGKW TAILEDDDDS DSDSNDGSRS PEKGTSVSDH HCSSSHPSEP
IIINLDSDDD EPNGNNPHVT NNHDDSNRHS NDNNNNSIKN NDSHNKNNNN NNNNNNNNND
NNNSIENNDS NSNNKHDHGS RSNTPSHNHT KNLMNDNDDD DDDRLMAEIT SNHLKSTNTD
ILTEKGSSAP SRTLDPKSYN IVASETTTPV TNRVIPEYLG NSSSYIGKQL PNILGKTPLN
VTAVDNSSHL ISPDVSVSSP TPRNTASNAS SSALSTPPLI RMSSLDPRGS TVPDKTIRPP
INSNSYTASI SDSFVQPQES SVFPPREQNM DMSFPSTVNS RFNDPRLNTT RFPDSTLRGA
TILSNNGLDQ RNNSLPTTEA ITRNDVGRQN STPVLPTLPQ NVPIRTNSNK SGLPLINNEN
SVPNPPNTAT IPLQKSRLIV NPFIPRRPYS NVLPQKRQLS NTSSTSPIMG TWKTQDYGKK
YNSG
