SPA2_YEAST
ID SPA2_YEAST Reviewed; 1466 AA.
AC P23201; D6VXY3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein SPA2;
GN Name=SPA2; Synonyms=PEA1; OrderedLocusNames=YLL021W; ORFNames=L1209;
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 204508 / S288c;
RX PubMed=2211820; DOI=10.1083/jcb.111.4.1451;
RA Gehrung S., Snyder M.;
RT "The SPA2 gene of Saccharomyces cerevisiae is important for pheromone-
RT induced morphogenesis and efficient mating.";
RL J. Cell Biol. 111:1451-1464(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046100;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT known genes, a new member of the seripauperins family and a new ABC
RT transporter homologous to the human multidrug resistance protein.";
RL Yeast 13:183-188(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP INTERACTION WITH SHS1.
RX PubMed=9790978; DOI=10.1006/bbrc.1998.9541;
RA Mino A., Tanaka K., Kamei T., Umikawa M., Fujiwara T., Takai Y.;
RT "Shs1p: a novel member of septin that interacts with spa2p, involved in
RT polarized growth in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 251:732-736(1998).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; SER-254;
RP SER-585; SER-599; SER-646; SER-883; SER-937; SER-961; SER-979; THR-1179;
RP SER-1180 AND SER-1263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-820; SER-937;
RP SER-961; SER-1053 AND SER-1056, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-254; SER-274;
RP SER-301; SER-585; SER-599; SER-865; SER-883; SER-910; SER-979; THR-1179 AND
RP SER-1180, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; THR-220;
RP SER-254; SER-274; SER-585; SER-599; SER-817; SER-820; SER-883; SER-961;
RP SER-979; SER-1173; THR-1179; SER-1180; THR-1251 AND SER-1263, AND
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: Involved in pheromone-induced morphogenesis and efficient
CC mating, perhaps as a cytoskeletal protein.
CC -!- SUBUNIT: Interacts with SHS1. {ECO:0000269|PubMed:9790978}.
CC -!- SUBCELLULAR LOCATION: Cell tip. Note=Localizes to a sharp patch at the
CC shmoo tip (mating projection) which corresponds to the site of
CC polarized cell growth.
CC -!- MISCELLANEOUS: Present with 274 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X53731; CAA37763.1; -; Genomic_DNA.
DR EMBL; X97560; CAA66170.1; -; Genomic_DNA.
DR EMBL; Z73126; CAA97469.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09299.1; -; Genomic_DNA.
DR PIR; A36426; A36426.
DR RefSeq; NP_013079.1; NM_001181841.1.
DR AlphaFoldDB; P23201; -.
DR SMR; P23201; -.
DR BioGRID; 31232; 195.
DR ComplexPortal; CPX-3188; Polarisome.
DR DIP; DIP-99N; -.
DR IntAct; P23201; 14.
DR MINT; P23201; -.
DR STRING; 4932.YLL021W; -.
DR iPTMnet; P23201; -.
DR MaxQB; P23201; -.
DR PaxDb; P23201; -.
DR PRIDE; P23201; -.
DR EnsemblFungi; YLL021W_mRNA; YLL021W; YLL021W.
DR GeneID; 850639; -.
DR KEGG; sce:YLL021W; -.
DR SGD; S000003944; SPA2.
DR VEuPathDB; FungiDB:YLL021W; -.
DR eggNOG; ENOG502QS1N; Eukaryota.
DR GeneTree; ENSGT00940000176499; -.
DR HOGENOM; CLU_002012_0_0_1; -.
DR InParanoid; P23201; -.
DR OMA; MKRNQAR; -.
DR BioCyc; YEAST:G3O-32125-MON; -.
DR PRO; PR:P23201; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P23201; protein.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:1902716; C:cell cortex of growing cell tip; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0000133; C:polarisome; IDA:SGD.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:0036267; P:invasive filamentous growth; IGI:SGD.
DR GO; GO:0031382; P:mating projection formation; IGI:SGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0031384; P:regulation of initiation of mating projection growth; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0031385; P:regulation of termination of mating projection growth; IMP:SGD.
DR GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR InterPro; IPR039892; Spa2/Sph1.
DR PANTHER; PTHR21601; PTHR21601; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF08518; GIT_SHD; 2.
DR SMART; SM00555; GIT; 4.
PE 1: Evidence at protein level;
KW Cell shape; Coiled coil; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1466
FT /note="Protein SPA2"
FT /id="PRO_0000072090"
FT REPEAT 818..825
FT /note="1"
FT REPEAT 826..834
FT /note="2"
FT REPEAT 835..843
FT /note="3"
FT REPEAT 860..868
FT /note="4"
FT REPEAT 875..883
FT /note="5"
FT REPEAT 884..892
FT /note="6"
FT REPEAT 893..901
FT /note="7"
FT REPEAT 902..910
FT /note="8"
FT REPEAT 911..919
FT /note="9"
FT REPEAT 920..928
FT /note="10"
FT REPEAT 929..937
FT /note="11"
FT REPEAT 938..946
FT /note="12"
FT REPEAT 947..953
FT /note="13"
FT REPEAT 954..961
FT /note="14"
FT REPEAT 962..970
FT /note="15"
FT REPEAT 971..979
FT /note="16"
FT REPEAT 980..988
FT /note="17"
FT REPEAT 989..997
FT /note="18"
FT REPEAT 998..1006
FT /note="19"
FT REPEAT 1007..1015
FT /note="20"
FT REPEAT 1036..1044
FT /note="21"
FT REPEAT 1045..1053
FT /note="22"
FT REPEAT 1054..1062
FT /note="23"
FT REPEAT 1072..1080
FT /note="24"
FT REPEAT 1081..1087
FT /note="25"
FT REGION 123..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..1087
FT /note="25 X 9 AA approximate tandem repeats"
FT REGION 954..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..388
FT /evidence="ECO:0000255"
FT COILED 1169..1189
FT /evidence="ECO:0000255"
FT COILED 1275..1302
FT /evidence="ECO:0000255"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1466 AA; 163143 MW; 2EBB616152382C89 CRC64;
MGTSSEVSLA HHRDIFHYYV SLKTFFEVTG ENRDRSNSTR AQKARAKLLK LSSSQFYELS
TDVSDELQRR IGEDANQPDY LLPKANFHMK RNQARQKLAN LSQTRFNDLL DDILFEIKRR
GFDKDLDAPR PPLPQPMKQE VSKDSDDTAR TSTNSSSVTQ VAPNVSVQPS LVIPKMASID
WSSEEEEEEQ VKEKPNEPEG KQTSMDEKKE AKPALNPIVT DSDLPDSQVL ARDITSMART
PTTTHKNYWD VNDSPIIKVD KDIDNEKGPE QLKSPEVQRA ENNNPNSEME DKVKELTDLN
SDLHLQIEDL NAKLASLTSE KEKEKKEEKE EKEKEKNLKI NYTIDESFQK ELLSLNSQIG
ELSIENENLK QKISEFELHQ KKNDNHNDLK ITDGFISKYS SADGLIPAQY ILNANNLIIQ
FTTRLSAVPI GDSTAISHQI GEELFQILSQ LSNLISQLLL SADLLQYKDQ VILLKASLSH
AITSIRYFSV YGPVLIPKIT VQAAVSEVCF AMCNLIDSAK IKSDSNGEST TSNEGNRQVL
EYSSPTATTP MTPTFPSTSG INMKKGFINP RKPASFLNDV EEEESPVKPL KITQKAINSP
IIRPSSSNGV PTTSRKPSGT GLFSLMIDSS IAKNSSHKED NDKYVSPIKA VTSASNSASS
NISEIPKLTL PPQAKIGTVI PPSENQVPNI KIENTEEDNK RSDITNEISV KPTSSIADKL
KQFEQSSEKK SSPKENPIAK EEMDSKPKLS NKFITSMNDV STDDSSSDGN ENDDADDDDD
FTYMALKQTM KREGSKIEKN NDSKLPANIV ELDLHESPES VKIESPESIK EITSSEMSSE
MPSSSLPKRL VEDVEPSEMP EKGASVESVR KKNFQEPLGN VESPDMTQKV KSLGMTGKAV
GPESDSRVES PGMTGQIKSL NMAGKVVGPE ADSRVESPGM KEQIKSLGMT GKITAQESIK
SPEAARKLAS SGEVDKIESP RMVRESESLE AVGNTIPSNM TVKMESPNLK GNTVSEPQEI
RRDIASSEPI ENVDPPKVLK KIVFPKAVNR TGSPKSVEKT PSSATLKKSG LPEPNSQIVS
PELAKNSPLA PIKKNVELRE TNKPHTETIT SVEPTNKDAN TSWRDADLNR TIKREEEDED
FDRVNHNIQI TGAYTKTGKI DYHKIPVDRK AKSEAEVHTS EEDIDESNNV NGKRADAQIH
ITERKHAFVN PTENSQVKKT SHSPFLNSKP VQYENSESNG GINNHIKIKN TGETTAHDEK
HYSDDDDSSY QFVPMKHEEQ EQEQNRSEEE ESEDDDEEEE DSDFDVDTFD IENPDNTLSE
LLLYLEHQTM DVISTIQSLL TSIKKPQVTK GNLRGESNAI NQVIGQMVDA TSISMEQSRN
ANLKKHGDWV VQSLRDCSRR MTILCQLTGD GILAKEKSDQ DYADKNFKQR LAGIAFDVAK
CTKELVKTVE EASLKDEINY LNSKLK
