TOR2_SCHPO
ID TOR2_SCHPO Reviewed; 2337 AA.
AC Q9Y7K2; O94507;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase tor2 {ECO:0000305|PubMed:11096119};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22976295};
DE AltName: Full=Phosphatidylinositol kinase homolog tor2;
DE AltName: Full=Target of rapamycin kinase 2;
GN Name=tor2 {ECO:0000303|PubMed:11096119};
GN ORFNames=SPBC216.07c {ECO:0000312|PomBase:SPBC216.07c}, SPBC646.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION.
RX PubMed=11096119; DOI=10.1074/jbc.m010446200;
RA Weisman R., Choder M.;
RT "The fission yeast TOR homolog, tor1+, is required for the response to
RT starvation and other stresses via a conserved serine.";
RL J. Biol. Chem. 276:7027-7032(2001).
RN [3]
RP FUNCTION, AND INTERACTION WITH RHB1.
RX PubMed=17121544; DOI=10.1111/j.1365-2443.2006.01025.x;
RA Uritani M., Hidaka H., Hotta Y., Ueno M., Ushimaru T., Toda T.;
RT "Fission yeast Tor2 links nitrogen signals to cell proliferation and acts
RT downstream of the Rheb GTPase.";
RL Genes Cells 11:1367-1379(2006).
RN [4]
RP FUNCTION, AND INTERACTION WITH MIP1; POP3; STE11 AND MEI2.
RX PubMed=17046992; DOI=10.1242/jcs.03241;
RA Alvarez B., Moreno S.;
RT "Fission yeast Tor2 promotes cell growth and represses cell
RT differentiation.";
RL J. Cell Sci. 119:4475-4485(2006).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP IDENTIFICATION IN THE TORC1 COMPLEX, PHOSPHORYLATION AT SER-1539,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18076573; DOI=10.1111/j.1365-2443.2007.01141.x;
RA Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,
RA Ebe M., Yanagida M.;
RT "Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and
RT organization of two highly phosphorylated TOR complexes by specific and
RT common subunits.";
RL Genes Cells 12:1357-1370(2007).
RN [7]
RP FUNCTION.
RX PubMed=17179073; DOI=10.1534/genetics.106.064170;
RA Weisman R., Roitburg I., Schonbrun M., Harari R., Kupiec M.;
RT "Opposite effects of tor1 and tor2 on nitrogen starvation responses in
RT fission yeast.";
RL Genetics 175:1153-1162(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH MIP1.
RX PubMed=17261596; DOI=10.1128/mcb.01039-06;
RA Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.;
RT "Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the
RT sexual development pathway in fission yeast.";
RL Mol. Cell. Biol. 27:3154-3164(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2238 AND SER-2240, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [10]
RP FUNCTION.
RX PubMed=20144990; DOI=10.1242/jcs.060319;
RA Nakashima A., Sato T., Tamanoi F.;
RT "Fission yeast TORC1 regulates phosphorylation of ribosomal S6 proteins in
RT response to nutrients and its activity is inhibited by rapamycin.";
RL J. Cell Sci. 123:777-786(2010).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22976295; DOI=10.1242/jcs.111146;
RA Nakashima A., Otsubo Y., Yamashita A., Sato T., Yamamoto M., Tamanoi F.;
RT "Psk1, an AGC kinase family member in fission yeast, is directly
RT phosphorylated and controlled by TORC1 and functions as S6 kinase.";
RL J. Cell Sci. 125:5840-5849(2012).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of TORC1,
CC which regulates multiple cellular processes to control cell growth in
CC response to environmental signals. TORC1 controls the switch between
CC cell proliferation and differentiation by sensing nutrient
CC availability. Nutrient limitation and environmental stress signals
CC cause inactivation of TORC1. Active TORC1 positively controls cell
CC growth and ribosome biogenesis by regulating ribosomal protein gene
CC expression (PubMed:17121544, PubMed:17179073, PubMed:17261596). In
CC nutrient rich conditions, responsible for the phosphorylation of AGC S6
CC kinase (S6K) psk1 at 'Thr-392' and 'Thr-415', activating psk1 kinase
CC activity and promoting phosphorylation of ribosomal protein S6. Also
CC catalyzes the nutrient-dependent phosphorylation of sck1 and sck2
CC (PubMed:20144990, PubMed:22976295). TORC1 negatively controls G1 cell-
CC cycle arrest, sexual development and amino acid uptake. Represses
CC mating, meiosis and sporulation efficiency by interfering with the
CC functions of the transcription factor ste11 and the meiosis-promoting
CC RNA-binding protein mei2 (PubMed:17046992).
CC {ECO:0000269|PubMed:17046992, ECO:0000269|PubMed:17121544,
CC ECO:0000269|PubMed:17179073, ECO:0000269|PubMed:17261596,
CC ECO:0000269|PubMed:20144990, ECO:0000269|PubMed:22976295}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:22976295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22976295};
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least mip1, pop3/wat1, tco89, toc1 and tor2 (PubMed:17046992,
CC PubMed:18076573, PubMed:17261596). Tor2 interacts with the small GTPase
CC rhb1 (PubMed:17121544). Tor2 interacts with ste11 and mei2
CC (PubMed:17046992). {ECO:0000269|PubMed:17046992,
CC ECO:0000269|PubMed:17121544, ECO:0000269|PubMed:17261596,
CC ECO:0000269|PubMed:18076573}.
CC -!- INTERACTION:
CC Q9Y7K2; Q9P3W5: tel2; NbExp=3; IntAct=EBI-2014299, EBI-2014377;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:18076573}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; CU329671; CAB40167.1; -; Genomic_DNA.
DR PIR; T39913; T40577.
DR RefSeq; NP_595359.2; NM_001021266.3.
DR AlphaFoldDB; Q9Y7K2; -.
DR SMR; Q9Y7K2; -.
DR BioGRID; 277243; 56.
DR IntAct; Q9Y7K2; 7.
DR STRING; 4896.SPBC216.07c.1; -.
DR iPTMnet; Q9Y7K2; -.
DR MaxQB; Q9Y7K2; -.
DR PaxDb; Q9Y7K2; -.
DR PRIDE; Q9Y7K2; -.
DR EnsemblFungi; SPBC216.07c.1; SPBC216.07c.1:pep; SPBC216.07c.
DR GeneID; 2540720; -.
DR KEGG; spo:SPBC216.07c; -.
DR PomBase; SPBC216.07c; tor2.
DR VEuPathDB; FungiDB:SPBC216.07c; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; Q9Y7K2; -.
DR OMA; DPYKHQQ; -.
DR PhylomeDB; Q9Y7K2; -.
DR BRENDA; 2.7.1.137; 5613.
DR Reactome; R-SPO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR Reactome; R-SPO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q9Y7K2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:PomBase.
DR GO; GO:0034064; C:Tor2-Mei2-Ste11 complex; IDA:PomBase.
DR GO; GO:0031931; C:TORC1 complex; IDA:PomBase.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0051728; P:cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0110045; P:negative regulation of cell cycle switching, mitotic to meiotic cell cycle; IMP:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:PomBase.
DR GO; GO:0030307; P:positive regulation of cell growth; EXP:PomBase.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:PomBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0120272; P:positive regulation of nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; IDA:PomBase.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.20.120.150; -; 1.
DR Gene3D; 1.25.10.10; -; 4.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024585; DUF3385_TOR.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF47212; SSF47212; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cytoplasm; Kinase; Meiosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Sporulation; Transferase.
FT CHAIN 1..2337
FT /note="Serine/threonine-protein kinase tor2"
FT /id="PRO_0000088814"
FT REPEAT 163..200
FT /note="HEAT 1"
FT REPEAT 249..286
FT /note="HEAT 2"
FT REPEAT 290..326
FT /note="HEAT 3"
FT REPEAT 409..446
FT /note="HEAT 4"
FT REPEAT 474..512
FT /note="HEAT 5"
FT REPEAT 559..596
FT /note="HEAT 6"
FT REPEAT 642..679
FT /note="HEAT 7"
FT REPEAT 683..721
FT /note="HEAT 8"
FT REPEAT 727..765
FT /note="HEAT 9"
FT REPEAT 802..840
FT /note="HEAT 10"
FT REPEAT 844..880
FT /note="HEAT 11"
FT REPEAT 881..921
FT /note="HEAT 12"
FT REPEAT 965..1004
FT /note="HEAT 13"
FT REPEAT 1006..1043
FT /note="HEAT 14"
FT DOMAIN 1228..1784
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 1958..2285
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2305..2337
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1964..1970
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2137..2145
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2157..2182
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 1539
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18076573"
FT MOD_RES 2238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 2240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 2337 AA; 266379 MW; 190F448DA04FD2D9 CRC64;
MKEFPGLKSR NEEIRNKAAN DLYEYVIAYS RELSGEALVQ FNNDVNKYVY TLIHSTDPLD
RLAGVTAINR LIDYEGEDTT RITRFANYLR IILPGTDQKA TVLAAKALGR LAVPGGALTS
EFVNFEVKRA LEWLQGERNE NRRYAAVLIL KELAKNTSTL IYAHIDSIFE LLWHGLRDPK
VTIRIASADA LSEFLKIVRQ RDSSIRLQWY TSILNEAQRG VAQGSSDYIH GSLLVYRQLF
LKAGMFMHER YREVSDIILQ FRDHKDLLIR KTVTELIATL AAYNPDEFVS NYLHVCMLHL
LNLLKKENVK MLAFATIGKV AVAITNSIIP YLDPICDSIK ESLKIHIRNK SASDAAIFQC
ISLLSIALGQ AFSNYAYDLF DLIFASGLSE ASYRALSDLA HNIPPLLPVI QERLLDMLSK
ILSGRPFIPP GCPPQYVARS LKSSKSASLK TGFFPNDVYI LALKVLGNFD FSGYILNEFV
KDCVVVYLEN NDPEVRKTAS ITCSQLFARD PILSQTSDHA IQVVAEVLEK LLTVGICDTV
PDIRLTVLNS LDSRFNKHLA QADKIRLLFI AINDENFAVR ESALRIIGRL NVYNPAYVMP
YLRKIMLKTL TILDYSTIIR TKEENAKLLC LLIAAAPRLI ESHVEPILQI LLPKAKDSSS
IVAASIVNSL GEICQISGEV IVPFIKDLMP LIIEALQDQS SPIRRAAALK ALGNLSSSTG
YVIDPYIEFP SLLDILIGIT KTEQDITIRR ETIKLIGTLG ALDPNRHRVL EKGTEKVVPE
QKNIPPDISL LMSGIGPSSD EYYPTVVITA LMSILKDPSL TIHHTAVIQA VMYIFKTMGL
RCAPFLSQII PEFIAVMRTC PTNILEFYFQ QLSILVLIVR QHIRSFLPDL FKLIKDFWNP
HSNLQFTILS LIESLARAMQ GEFKPYLPSL LVMMLQIFDS DVSVDSVSTK KVLHAFIVFG
DTLADYFHML LDPILRLYER NDVSIGIKES IMITIGRLSM VINLSEYASR IIHPVMRMLS
CNNASLIRVS MDTVCALIYQ LNVDFAIFIP MIDKCLKMNG VTHETYSILV EQFLQEQPLP
IKLNPYEKYD KPKLDVVASA ADITSKKLPV NQEILRNAWE ASQRSTKDDW QEWIRRLGVA
LLRESPSHAL RACAALAAAY QPLARDLFNA SFVSCWSELY DHFQEELVKS IEIALTSPHI
SPEIIQILLN LAEFMEHDDK PLPIDIRTLG AYAAKCHAFA KALHYKELEF IEEELVTKPS
VDTIEALISI NNQLQQPDAA IGILKHAQQH DKMNLKETWY EKLQRWEDAL SAYEKREAAG
AGNFEITMGK LRCLHALGEW DRLSQLAQEN WIHAGHDARR YIAPLSVAAA WGLGQWEQMD
EYISVMKSES PDKAFFNAIV ALHRSQFEEA ASYITRARDL LDTELTALVG ESYNRAYSVA
VRVQMLSELE EIITYKKAED KPEVREMIKK TWVRRLKGCQ RNVDVWQRML RIRSLVISPR
DNMEMWIKFA NLCRKSGRIS LAKKSLNLLL EDDENLDNSL VLKKTHPSIV YANLKFLWAV
DDKRKALNSM QEFTSQLISD INVDPALFVQ STSVNTQKSQ EEIQYYFHLL ARCYHKQGQW
QQEIENNWSE GSFDGVLQSY MYATQFDSKW YKAWHSWALA NFEAVKFLEQ SEEQIPSAAY
EQYIIPAVKG FFKSIALSKG NLQDTLRLLN LWFKFGNNSN VINTLNVGIS TVNIDIWLDV
IPQLIARIHA SSLSVRKSVH QLLSDVGRAH PQALVYPLTV AAKSQSSARQ NAALAIMDSL
KTHSPRLVEQ ARLVSHELIR AAILWHEQWH EGLEEASRLY FGDHNIEGMF AVLRPLHEML
ERGPETLREI SFQQAFGRDL VEARDCCIRF EQTGDISDLN QAWDLYYQVF KKIRKQLPQL
TTLDLQYVSP KLLHVHDLEL AVPGTYVSGK PVIRIVKFYP TFNVITSKQR PRRLSIKGSD
GKDYQYVLKG HEDIRQDERV MQLFGLCNNL LLADPETFKR LLSIQRYPVI PLSPDSGLLG
WVLDSDTLHV LIRDYRESRK ILLNIEHRLI IQMAPDYDRL TLLQKVEVFE YALLSTTGQD
LYRVLWLKSR SSEAWLNRRT NYSRTLAVMS MVGYILGLGD RHPSNLMLDR YTGNIIHIDF
GDCFEVAMHR EKFPEKIPFR LTRMLVNAME VSGIEGTFRI TCEHVMRVLR TNKESVMAVL
EAFVYDPLIN WRLAPAYSPS IDEKQSNEPN TLLGETIDGL HRKRLNEEGI TLEERQKPEI
LNQRAITVLN RVSNKLTGRD FKPQQQLDVP SQVEKLILQA TSIENLCLCY IGWCSFW
