ID   LYST_MOUSE              Reviewed;        3788 AA.
AC   P97412; Q62403; Q8VBS6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Lysosomal-trafficking regulator;
DE   AltName: Full=Beige protein;
DE   AltName: Full=CHS1 homolog;
GN   Name=Lyst; Synonyms=Bg, Chs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
RX   PubMed=9215680; DOI=10.1093/hmg/6.7.1091;
RA   Barbosa M.D.F.S., Barrat F.J., Tchernev V.T., Nguyen Q.A., Mishra V.S.,
RA   Colman S.D., Pastural E., Dufourcq-Lagelouse R., Fischer A., Holcombe R.F.,
RA   Wallace M.R., Brandt S.J., De Saint Basile G., Kingsmore S.F.;
RT   "Identification of mutations in two major mRNA isoforms of the Chediak-
RT   Higashi syndrome gene in human and mouse.";
RL   Hum. Mol. Genet. 6:1091-1098(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=8717042; DOI=10.1038/382262a0;
RA   Barbosa M.D.F.S., Nguyen Q.A., Tchernev V.T., Ashley J.A., Detter J.C.,
RA   Blaydes S.M., Brandt S.J., Chotai D., Hodgman C., Solari R.C.E.S.,
RA   Lovett M., Kingsmore S.F.;
RT   "Identification of the homologous beige and Chediak-Higashi syndrome
RT   genes.";
RL   Nature 382:262-265(1996).
RN   [3]
RP   ERRATUM OF PUBMED:8717042.
RA   Barbosa M.D.F.S., Nguyen Q.A., Tchernev V.T., Ashley J.A., Detter J.C.,
RA   Blaydes S.M., Brandt S.J., Chotai D., Hodgman C., Solari R.C.E.S.,
RA   Lovett M., Kingsmore S.F.;
RL   Nature 385:97-97(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1428-3788 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=8673129; DOI=10.1038/ng0796-303;
RA   Perou C.M., Moore K.J., Nagle D.L., Misumi D.J., Woolf E.A., McGrail S.H.,
RA   Holmgren L., Brody T.B., Dussault B.J., Monroe C.A., Duyk G.M., Pryor R.J.,
RA   Li L., Justice M.J., Kaplan J.;
RT   "Identification of the murine beige gene by YAC complementation and
RT   positional cloning.";
RL   Nat. Genet. 13:303-308(1996).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2203, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; THR-165; SER-166;
RP   SER-1503; SER-1504; SER-2099; SER-2118; SER-2203; SER-2207 AND SER-2254,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, AND VARIANT BG 3741-ILE--GLY-3788 DEL.
RX   PubMed=27881733; DOI=10.1084/jem.20141461;
RA   Westphal A., Cheng W., Yu J., Grassl G., Krautkraemer M., Holst O.,
RA   Foeger N., Lee K.H.;
RT   "Lysosomal trafficking regulator Lyst links membrane trafficking to toll-
RT   like receptor-mediated inflammatory responses.";
RL   J. Exp. Med. 214:227-244(2017).
CC   -!- FUNCTION: Adapter protein that regulates and/or fission of
CC       intracellular vesicles such as lysosomes (By similarity). Might
CC       regulate trafficking of effectors involved in exocytosis (By
CC       similarity). In cytotoxic T-cells and natural killer (NK) cells, has
CC       role in the regulation of size, number and exocytosis of lytic granules
CC       (By similarity). In macrophages and dendritic cells, regulates
CC       phagosome maturation by controlling the conversion of early phagosomal
CC       compartments into late phagosomes (PubMed:27881733). In macrophages and
CC       dendritic cells, specifically involved in TLR3- and TLR4-induced
CC       production of pro-inflammatory cytokines by regulating the endosomal
CC       TLR3- TICAM1/TRIF and TLR4- TICAM1/TRIF signaling pathways
CC       (PubMed:27881733). {ECO:0000250|UniProtKB:Q99698,
CC       ECO:0000269|PubMed:27881733}.
CC   -!- SUBUNIT: Interacts with CENPJ, LIP8 and ZNF521.
CC       {ECO:0000250|UniProtKB:Q99698}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=P97412-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97412-2; Sequence=VSP_006783, VSP_006784;
CC   -!- TISSUE SPECIFICITY: Expressed in the heart, lung, liver, spleen, brain
CC       and in different immune cell types (purified B and T lymphocytes, bone
CC       marrow-derived macrophages and dendritic cells).
CC       {ECO:0000269|PubMed:27881733}.
CC   -!- DISEASE: Note=Defects in Lyst are the cause of beige (bg), an autosomal
CC       recessive disorder characterized by hypopigmentation, bleeding, immune
CC       cell dysfunction, abnormal intracellular transport to and from the
CC       lysosome, and giant inclusion bodies in a variety of cell types.
CC       {ECO:0000269|PubMed:27881733, ECO:0000269|PubMed:9215680}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U70015; AAC53011.1; -; mRNA.
DR   EMBL; L77884; AAL40134.1; -; mRNA.
DR   EMBL; U52461; AAB60778.1; -; mRNA.
DR   PIR; T30851; T30851.
DR   RefSeq; NP_034878.2; NM_010748.2.
DR   SMR; P97412; -.
DR   BioGRID; 201257; 2.
DR   STRING; 10090.ENSMUSP00000106188; -.
DR   iPTMnet; P97412; -.
DR   PhosphoSitePlus; P97412; -.
DR   SwissPalm; P97412; -.
DR   EPD; P97412; -.
DR   jPOST; P97412; -.
DR   MaxQB; P97412; -.
DR   PaxDb; 10090-ENSMUSP00000106188; -.
DR   PeptideAtlas; P97412; -.
DR   ProteomicsDB; 290203; -. [P97412-1]
DR   ProteomicsDB; 290204; -. [P97412-2]
DR   Pumba; P97412; -.
DR   DNASU; 17101; -.
DR   GeneID; 17101; -.
DR   KEGG; mmu:17101; -.
DR   AGR; MGI:107448; -.
DR   CTD; 1130; -.
DR   MGI; MGI:107448; Lyst.
DR   eggNOG; KOG1786; Eukaryota.
DR   InParanoid; P97412; -.
DR   OrthoDB; 47483at2759; -.
DR   PhylomeDB; P97412; -.
DR   BioGRID-ORCS; 17101; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Lyst; mouse.
DR   PRO; PR:P97412; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P97412; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR   GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR   GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR   GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISO:MGI.
DR   GO; GO:0071621; P:granulocyte chemotaxis; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0033364; P:mast cell secretory granule organization; IMP:MGI.
DR   GO; GO:0032438; P:melanosome organization; IMP:MGI.
DR   GO; GO:0007017; P:microtubule-based process; IMP:MGI.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:MGI.
DR   GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0055091; P:phospholipid homeostasis; IMP:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR   GO; GO:0048753; P:pigment granule organization; IMP:MGI.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR   GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI.
DR   GO; GO:0002456; P:T cell mediated immunity; IMP:MGI.
DR   CDD; cd06071; Beach; 1.
DR   CDD; cd01201; PH_BEACH; 1.
DR   Gene3D; 1.10.1540.10; BEACH domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000409; BEACH_dom.
DR   InterPro; IPR036372; BEACH_dom_sf.
DR   InterPro; IPR023362; PH-BEACH_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR13743; BEIGE/BEACH-RELATED; 1.
DR   PANTHER; PTHR13743:SF163; LYSOSOMAL-TRAFFICKING REGULATOR; 1.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF14844; PH_BEACH; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM01026; Beach; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF81837; BEACH domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS51783; PH_BEACH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Disease variant; Phagocytosis;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport;
KW   WD repeat.
FT   CHAIN           1..3788
FT                   /note="Lysosomal-trafficking regulator"
FT                   /id="PRO_0000051072"
FT   REPEAT          662..700
FT                   /note="WD 1"
FT   REPEAT          1576..1620
FT                   /note="WD 2"
FT   DOMAIN          2996..3102
FT                   /note="BEACH-type PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01119"
FT   DOMAIN          3126..3409
FT                   /note="BEACH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00026"
FT   REPEAT          3550..3589
FT                   /note="WD 3"
FT   REPEAT          3601..3640
FT                   /note="WD 4"
FT   REPEAT          3643..3686
FT                   /note="WD 5"
FT   REPEAT          3687..3731
FT                   /note="WD 6"
FT   REPEAT          3736..3775
FT                   /note="WD 7"
FT   REGION          148..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1169..1196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1482..1519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2177..2221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2556..2581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2659..2681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2187..2217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2099
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         2207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1509..1545
FT                   /note="EGDRPEVTESINPGDRLIEDGCIHLISLGSKALMIQV -> GMMAGSDLYTK
FT                   ILQIAACLSFKHIWQYFNVFFKCYSP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8717042"
FT                   /id="VSP_006783"
FT   VAR_SEQ         1546..3788
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8717042"
FT                   /id="VSP_006784"
FT   VARIANT         3741..3788
FT                   /note="Missing (in bg; macrophages and dendritic cells show
FT                   impaired pro-inflammatory cytokine production in response
FT                   to stimulation of TLR3 and TLR4 receptors; shows impaired
FT                   inflammatory responses to lipopolysaccharides; following
FT                   bacteria infections, shows defective phagosomal
FT                   maturation)"
FT                   /evidence="ECO:0000269|PubMed:27881733"
SQ   SEQUENCE   3788 AA;  425287 MW;  F01BE837C676A750 CRC64;
     MSTDSNSLAR EFLIDVNQLC NAVVQRAEAR EEEEEETHMA TLGQYLVHGR GFLLLTKLNS
     IIDQALTCRE ELLTLLLSLL PLVWKIPVQE QQATDFNLPL SSDIILTKEK NSSLQKSTQG
     KLYLEGSAPS GQVSAKVNLF RKIRRQRKST HRYSVRDARK TQLSTSDSEG NSDEKSTVVS
     KHRRLHALPR FLTQSPKEGH LVAKPDPSAT KEQVLSDTMS VENSREVILR QDSNGDILSE
     PAALSILSNM NNSPFDLCHV LLSLLEKVCK FDIALNHNSS LALSVVPTLT EFLAGFGDCC
     NQSDTLEGQL VSAGWTEEPV ALVQRMLFRT VLHLMSVDVS TAEAMPESLR KNLTELLRAA
     LKIRACLEKQ PEPFSPRQKK TLQEVQEGFV FSKYRHRALL LPELLEGVLQ LLISCLQSAA
     SNPFYFSQAM DLVQEFIQHQ GFNLFGTAVL QMEWLLTRDG VPSEAAEHLK ALINSVIKIM
     STVKKVKSEQ LHHSMCTRKR HRRCEYSHFM QHHRDLSGLL VSAFKNQLSK SPFEETAEGD
     VQYPERCCCI AVCAHQCLRL LQQVSLSTTC VQILSGVHSV GICCCMDPKS VIAPLLHAFK
     LPALKAFQQH ILNVLSKLLV DQLGGAELSP RIKKAACNIC TVDSDQLAKL GETLQGTLCG
     AGPTSGLPSP SYRFQGILPS SGSEDLLWKW DALEAYQSFV FQEDRLHNIQ IANHICNLLQ
     KGNVVVQWKL YNYIFNPVLQ RGVELVHHCQ QLSIPSAQTH MCSQLKQYLP QEVLQIYLKT
     LPVLLKSRVI RDLFLSCNGV NHIIELNYLD GIRSHSLKAF ETLIVSLGEQ QKDAAVLDVD
     GLDIQQELPS LSVGPSLHKQ QASSDSPCSL RKFYASLREP DPKKRKTIHQ DVHINTINLF
     LCVAFLCVSK EADSDRESAN ESEDTSGYDS PPSEPLSHML PCLSLEDVVL PSPECLHHAA
     DIWSMCRWIY MLNSVFQKQF HRLGGFQVCH ELIFMIIQKL FRSHTEDQGR RQGEMSRNEN
     QELIRISYPE LTLKGDVSSA TAPDLGFLRK SADSVRGFQS QPVLPTSAEQ IVATESVPGE
     RKAFMSQQSE TSLQSIRLLE SLLDICLHSA RACQQKMELE LPSQGLSVEN ILCELREHLS
     QSKVAETELA KPLFDALLRV ALGNHSADLG PGDAVTEKSH PSEEELLSQP GDFSEEAEDS
     QCCSLKLLGE EEGYEADSES NPEDVDTQDD GVELNPEAEG FSGSIVSNNL LENLTHGEII
     YPEICMLGLN LLSASKAKLD VLAHVFESFL KIVRQKEKNI SLLIQQGTVK ILLGGFLNIL
     TQTNSDFQAC QRVLVDLLVS LMSSRTCSED LTLLWRIFLE KSPCTEILLL GIHKIVESDF
     TMSPSQCLTF PFLHTPSLSN GVLSQKPPGI LNSKALGLLR RARISRGKKE ADRESFPYRL
     LSSWHIAPIH LPLLGQNCWP HLSEGFSVSL VGLMWNTSNE SESAAERGKR VKKRNKPSVL
     EDSSFEGAEG DRPEVTESIN PGDRLIEDGC IHLISLGSKA LMIQVWADPH SGTFIFRVCM
     DSNDDTKAVS LAQVESQENI FFPSKWQHLV LTYIQHPQGK KNVHGEISIW VSGQRKTDVI
     LDFVLPRKTS LSSDSNKTFC MIGHCLTSQE ESLQLAGKWD LGNLLLFNGA KIGSQEAFFL
     YACGPNYTSI MPCKYGQPVI DYSKYINKDI LRCDEIRDLF MTKKEVDVGL LIESLSVVYT
     TCCPAQYTIY EPVIRLKGQV KTQPSQRPFS SKEAQSILLE PSQLKGLQPT ECKAIQGILH
     EIGGAGTFVF LFARVVELSS CEETQALALR VILSLIKYSQ QRTQELENCN GLSMIHQVLV
     KQKCIVGFHI LKTLLEGCCG EEVIHVSEHG EFKLDVESHA IIQDVKLLQE LLLDWKIWNK
     AEQGVWETLL AALEVLIRVE HHQQQFNIKQ LLNAHVVHHF LLTCQVLQEH REGQLTSMPR
     EVCRSFVKII AEVLGSPPDL ELLTVIFNFL LAVHPPTNTY VCHNPTNFYF SLHIDGKIFQ
     EKVQSLAYLR HSSSGGQAFP SPGFLVISPS AFTAAPPEGT SSSNIVPQRM AAQMVRSRSL
     PAFPTYLPLI RAQKLAASLG FSVDKLQNIA DANPEKQNLL GRPYALKTSK EEAFISSCES
     AKTVCEMEAL LGAHASANGV SRGSPRFPRA RVDHKDVGTE PRSDDDSPGD ESYPRRPDNL
     KGLASFQRSQ STVASLGLAF PSQNGSAVAS RWPSLVDRNA DDWENFTFSP AYEASYNRAT
     STHSVIEDCL IPICCGLYEL LSGVLLVLPD AMLEDVMDRI IQADILLVLV NHPSPAIQQG
     VIKLLHAYIN RASKEQKDKF LKNRGFSLLA NQLYLHRGTQ ELLECFVEMF FGRPIGLDEE
     FDLEEVKHME LFQKWSVIPV LGLIETSLYD NVLLHNALLL LLQVLNSCSK VADMLLDNGL
     LYVLCNTVAA LNGLEKNIPV NEYKLLACDI QQLFIAVTIH ACSSSGTQYF RVIEDLIVLL
     GYLHNSKNKR TQNMALALQL RVLQAALEFI RSTANHDSES PVHSPSAHRH SVPPKRRSIA
     GSRKFPLAQT ESLLMKMRSV ASDELHSMMQ RRMSQEHPSQ ASEAELAQRL QRLTILAVNR
     IIYQELNSDI IDILRTPENT SQSKTSVSQT EISEEDMHHE QPSVYNPFQK EMLTYLLDGF
     KVCIGSSKTS VSKQQWTKIL GSCKETLRDQ LGRLLAHILS PTHTVQERKQ ILEIVHEPAH
     QDILRDCLSP SPQHGAKLVL YLSELIHNHQ DELSEEEMDT AELLMNALKL CGHKCIPPSA
     PSKPELIKII REEQKKYESE ESVSKGSWQK TVNNNQQSLF QRLDFKSKDI SKIAADITQA
     VSLSQGIERK KVIQHIRGMY KVDLSASRHW QECIQQLTHD RAVWYDPIYY PTSWQLDPTE
     GPNRERRRLQ RCYLTIPNKY LLRDRQKSEG VLRPPLSYLF EDKTHSSFSS TVKDKAASES
     IRVNRRCISV APSRETAGEL LLGKCGMYFV EDNASDAVES SSLQGELEPA SFSWTYEEIK
     EVHRRWWQLR DNAVEIFLTN GRTLLLAFDN NKVRDDVYQS ILTNNLPNLL EYGNITALTN
     LWYSGQITNF EYLTHLNKHA GRSFNDLMQY PVFPFILSDY VSETLDLNDP SIYRNLSKPI
     AVQYKEKEDR YVDTYKYLEE EYRKGAREDD PMPPVQPYHY GSHYSNSGTV LHFLVRMPPF
     TKMFLAYQDQ SFDIPDRTFH STNTTWRLSS FESMTDVKEL IPEFFYLPEF LVNREGFDFG
     VRQNGERVNH VNLPPWARND PRLFILIHRQ ALESDHVSQN ICHWIDLVFG YKQKGKASVQ
     AINVFHPATY FGMDVSAVED PVQRRALETM IKTYGQTPRQ LFHTAHASRP GAKLNIEGEL
     PAAVGLLVQF AFRETREPVK EVTHPSPLSW IKGLKWGEYV GSPSAPVPVV CFSQPHGERF
     GSLQALPTRA ICGLSRNFCL LMTYNKEQGV RSMNNTNIQW SAILSWGYAD NILRLKSKQS
     EPPINFIQSS QQHQVTSCAW VPDSCQLFTG SKCGVITAYT NRLTSSTPSE IEMESQMHLY
     GHTEEITGLC VCKPYSVMIS VSRDGTCIVW DLNRLCYVQS LAGHKSPVTA VSASETSGDI
     ATVCDSAGGG SDLRLWTVNG DLVGHVHCRE IICSVAFSNQ PEGVSINVIA GGLENGIVRL
     WSTWDLKPVR EITFPKSNKP IISLTFSCDG HHLYTANSEG TVIAWCRKDQ QRVKLPMFYS
     FLSSYAAG
//