WDR59_HUMAN
ID WDR59_HUMAN Reviewed; 974 AA.
AC Q6PJI9; B3KRC3; Q71RE7; Q96PW5; Q9BSW6; Q9HA43;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=GATOR complex protein WDR59 {ECO:0000305};
DE AltName: Full=WD repeat-containing protein 59 {ECO:0000312|HGNC:HGNC:25706};
GN Name=WDR59 {ECO:0000312|HGNC:HGNC:25706};
GN Synonyms=KIAA1923 {ECO:0000312|EMBL:BAB67816.1};
GN ORFNames=FP977 {ECO:0000312|EMBL:AAQ15226.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 170-974 (ISOFORM 1).
RC TISSUE=Lung, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-974 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-822, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564; SER-822 AND SER-830, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP INTERACTION WITH SESN1; SESN2 AND SESN3.
RX PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
RA Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
RA Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
RT "The Sestrins interact with GATOR2 to negatively regulate the amino-acid-
RT sensing pathway upstream of mTORC1.";
RL Cell Rep. 9:1-8(2014).
RN [11]
RP FUNCTION, AND INTERACTION WITH SESN2.
RX PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
RA Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K.,
RA Guan K.L., Karin M., Budanov A.V.;
RT "Sestrins inhibit mTORC1 kinase activation through the GATOR complex.";
RL Cell Rep. 9:1281-1291(2014).
RN [12]
RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND SUBUNIT.
RX PubMed=23723238; DOI=10.1126/science.1232044;
RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A.,
RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.;
RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that
RT signal amino acid sufficiency to mTORC1.";
RL Science 340:1100-1106(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP INTERACTION WITH CASTOR2 AND CASTOR1.
RX PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
RA Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K., Wyant G.A.,
RA Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
RT "The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
RL Cell 165:153-164(2016).
RN [15]
RP FUNCTION.
RX PubMed=27487210; DOI=10.1038/nature19079;
RA Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
RA Sabatini D.M.;
RT "Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
RL Nature 536:229-233(2016).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=28199306; DOI=10.1038/nature21423;
RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K.,
RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M.,
RA Frankel W.N., Sabatini D.M.;
RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to
RT regulate mTORC1.";
RL Nature 543:438-442(2017).
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively
CC regulated by the upstream amino acid sensors SESN2 and CASTOR1
CC (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
CC -!- SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes (By
CC similarity). Within the GATOR complex, component of the GATOR2
CC subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR
CC complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC
CC heterodimers. The GATOR2 complex interacts with CASTOR2 and CASTOR1;
CC the interaction is negatively regulated by arginine (PubMed:26972053).
CC The GATOR2 complex interacts with SESN1, SESN2 and SESN3; the
CC interaction is negatively regulated by amino acids (PubMed:25263562,
CC PubMed:25457612). {ECO:0000250, ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:25263562, ECO:0000269|PubMed:25457612,
CC ECO:0000269|PubMed:26972053}.
CC -!- INTERACTION:
CC Q6PJI9; Q96S15: WDR24; NbExp=8; IntAct=EBI-2515073, EBI-746424;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:28199306}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6PJI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PJI9-2; Sequence=VSP_023884;
CC Name=3;
CC IsoId=Q6PJI9-3; Sequence=VSP_023882;
CC Name=4;
CC IsoId=Q6PJI9-4; Sequence=VSP_023881, VSP_023883;
CC -!- SIMILARITY: Belongs to the WD repeat WDR59 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67816.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK022332; BAB14015.1; -; mRNA.
DR EMBL; AK091316; BAG52335.1; -; mRNA.
DR EMBL; AF370390; AAQ15226.1; -; mRNA.
DR EMBL; BC004519; AAH04519.1; -; mRNA.
DR EMBL; BC014887; AAH14887.2; -; mRNA.
DR EMBL; AB067510; BAB67816.1; ALT_FRAME; mRNA.
DR CCDS; CCDS32488.1; -. [Q6PJI9-1]
DR CCDS; CCDS82011.1; -. [Q6PJI9-2]
DR RefSeq; NP_001311100.1; NM_001324171.1. [Q6PJI9-2]
DR RefSeq; NP_085058.3; NM_030581.3. [Q6PJI9-1]
DR AlphaFoldDB; Q6PJI9; -.
DR SMR; Q6PJI9; -.
DR BioGRID; 122841; 117.
DR ComplexPortal; CPX-6227; GATOR2 complex.
DR CORUM; Q6PJI9; -.
DR IntAct; Q6PJI9; 43.
DR MINT; Q6PJI9; -.
DR STRING; 9606.ENSP00000262144; -.
DR iPTMnet; Q6PJI9; -.
DR PhosphoSitePlus; Q6PJI9; -.
DR BioMuta; WDR59; -.
DR DMDM; 134035358; -.
DR EPD; Q6PJI9; -.
DR jPOST; Q6PJI9; -.
DR MassIVE; Q6PJI9; -.
DR MaxQB; Q6PJI9; -.
DR PaxDb; Q6PJI9; -.
DR PeptideAtlas; Q6PJI9; -.
DR PRIDE; Q6PJI9; -.
DR ProteomicsDB; 67210; -. [Q6PJI9-1]
DR ProteomicsDB; 67211; -. [Q6PJI9-2]
DR ProteomicsDB; 67212; -. [Q6PJI9-3]
DR ProteomicsDB; 67213; -. [Q6PJI9-4]
DR Antibodypedia; 48159; 50 antibodies from 16 providers.
DR DNASU; 79726; -.
DR Ensembl; ENST00000262144.11; ENSP00000262144.6; ENSG00000103091.15. [Q6PJI9-1]
DR Ensembl; ENST00000616369.4; ENSP00000482446.1; ENSG00000103091.15. [Q6PJI9-2]
DR GeneID; 79726; -.
DR KEGG; hsa:79726; -.
DR MANE-Select; ENST00000262144.11; ENSP00000262144.6; NM_030581.4; NP_085058.3.
DR UCSC; uc002fdh.2; human. [Q6PJI9-1]
DR CTD; 79726; -.
DR DisGeNET; 79726; -.
DR GeneCards; WDR59; -.
DR HGNC; HGNC:25706; WDR59.
DR HPA; ENSG00000103091; Low tissue specificity.
DR MIM; 617418; gene.
DR neXtProt; NX_Q6PJI9; -.
DR OpenTargets; ENSG00000103091; -.
DR PharmGKB; PA142670593; -.
DR VEuPathDB; HostDB:ENSG00000103091; -.
DR eggNOG; KOG0264; Eukaryota.
DR eggNOG; KOG0309; Eukaryota.
DR GeneTree; ENSGT00940000157600; -.
DR HOGENOM; CLU_009370_0_0_1; -.
DR InParanoid; Q6PJI9; -.
DR OMA; HDACIPF; -.
DR OrthoDB; 590848at2759; -.
DR PhylomeDB; Q6PJI9; -.
DR TreeFam; TF314695; -.
DR PathwayCommons; Q6PJI9; -.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SignaLink; Q6PJI9; -.
DR SIGNOR; Q6PJI9; -.
DR BioGRID-ORCS; 79726; 125 hits in 1083 CRISPR screens.
DR ChiTaRS; WDR59; human.
DR GenomeRNAi; 79726; -.
DR Pharos; Q6PJI9; Tdark.
DR PRO; PR:Q6PJI9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6PJI9; protein.
DR Bgee; ENSG00000103091; Expressed in right lobe of thyroid gland and 194 other tissues.
DR ExpressionAtlas; Q6PJI9; baseline and differential.
DR Genevisible; Q6PJI9; HS.
DR GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0035859; C:Seh1-associated complex; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IC:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR CDD; cd16692; mRING-H2-C3H3C2_WDR59; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR039456; WDR59_mRING-H2-C3H3C2.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..974
FT /note="GATOR complex protein WDR59"
FT /id="PRO_0000280721"
FT REPEAT 57..98
FT /note="WD 1"
FT REPEAT 103..143
FT /note="WD 2"
FT REPEAT 146..185
FT /note="WD 3"
FT REPEAT 189..229
FT /note="WD 4"
FT REPEAT 232..276
FT /note="WD 5"
FT REPEAT 278..318
FT /note="WD 6"
FT REPEAT 319..362
FT /note="WD 7"
FT DOMAIN 393..494
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REPEAT 668..706
FT /note="WD 8"
FT REGION 350..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..556
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023881"
FT VAR_SEQ 1..408
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_023882"
FT VAR_SEQ 557..571
FT /note="MTMHRAVSPTEPTPR -> MTGLQPVWIIIIFNYR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023883"
FT VAR_SEQ 572..974
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023884"
FT VARIANT 201
FT /note="P -> T (in dbSNP:rs11557260)"
FT /id="VAR_053436"
FT CONFLICT 441
FT /note="A -> S (in Ref. 4; BAB67816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 974 AA; 109793 MW; 72F651A38EA51CBA CRC64;
MAARWSSENV VVEFRDSQAT AMSVDCLGQH AVLSGRRFLY IVNLDAPFEG HRKISRQSKW
DIGAVQWNPH DSFAHYFAAS SNQRVDLYKW KDGSGEVGTT LQGHTRVISD LDWAVFEPDL
LVTSSVDTYI YIWDIKDTRK PTVALSAVAG ASQVKWNKKN ANCLATSHDG DVRIWDKRKP
STAVEYLAAH LSKIHGLDWH PDSEHILATS SQDNSVKFWD YRQPRKYLNI LPCQVPVWKA
RYTPFSNGLV TVMVPQLRRE NSLLLWNVFD LNTPVHTFVG HDDVVLEFQW RKQKEGSKDY
QLVTWSRDQT LRMWRVDSQM QRLCANDILD GVDEFIESIS LLPEPEKTLH TEDTDHQHTA
SHGEEEALKE DPPRNLLEER KSDQLGLPQT LQQEFSLINV QIRNVNVEMD AADRSCTVSV
HCSNHRVKML VKFPAQYPNN AAPSFQFINP TTITSTMKAK LLKILKDTAL QKVKRGQSCL
EPCLRQLVSC LESFVNQEDS ASSNPFALPN SVTPPLPTFA RVTTAYGSYQ DANIPFPRTS
GARFCGAGYL VYFTRPMTMH RAVSPTEPTP RSLSALSAYH TGLIAPMKIR TEAPGNLRLY
SGSPTRSEKE QVSISSFYYK ERKSRRWKSK REGSDSGNRQ IKAAGKVIIQ DIACLLPVHK
SLGELYILNV NDIQETCQKN AASALLVGRK DLVQVWSLAT VATDLCLGPK SDPDLETPWA
RHPFGRQLLE SLLAHYCRLR DVQTLAMLCS VFEAQSRPQG LPNPFGPFPN RSSNLVVSHS
RYPSFTSSGS CSSMSDPGLN TGGWNIAGRE AEHLSSPWGE SSPEELRFGS LTYSDPRERE
RDQHDKNKRL LDPANTQQFD DFKKCYGEIL YRWGLREKRA EVLKFVSCPP DPHKGIEFGV
YCSHCRSEVR GTQCAICKGF TFQCAICHVA VRGSSNFCLT CGHGGHTSHM MEWFRTQEVC
PTGCGCHCLL ESTF
