SZT2_MOUSE
ID SZT2_MOUSE Reviewed; 3431 AA.
AC A2A9C3; Q6PB77; Q7TSS6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=KICSTOR complex protein SZT2 {ECO:0000305};
DE AltName: Full=Seizure threshold 2 protein {ECO:0000303|PubMed:19624305};
DE AltName: Full=Transcript increased in glutamate resistance {ECO:0000303|PubMed:20045724};
DE Short=TIGR {ECO:0000303|PubMed:20045724};
GN Name=Szt2 {ECO:0000303|PubMed:19624305, ECO:0000312|MGI:MGI:3033336};
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), IDENTIFICATION BY MASS
RP SPECTROMETRY, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=19624305; DOI=10.1111/j.1601-183x.2009.00509.x;
RA Frankel W.N., Yang Y., Mahaffey C.L., Beyer B.J., O'Brien T.P.;
RT "Szt2, a novel gene for seizure threshold in mice.";
RL Genes Brain Behav. 8:568-576(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20045724; DOI=10.1016/j.freeradbiomed.2009.12.023;
RA Toutzaris D., Lewerenz J., Albrecht P., Jensen L.T., Letz J., Geerts A.,
RA Golz S., Methner A.;
RT "A novel giant peroxisomal superoxide dismutase motif-containing protein.";
RL Free Radic. Biol. Med. 48:811-820(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2675-3431.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Lung;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Pancreas, and Spleen;
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28199315; DOI=10.1038/nature21378;
RA Peng M., Yin N., Li M.O.;
RT "SZT2 dictates GATOR control of mTORC1 signalling.";
RL Nature 543:433-437(2017).
CC -!- FUNCTION: As part of the KICSTOR complex functions in the amino acid-
CC sensing branch of the TORC1 signaling pathway. Recruits, in an amino
CC acid-independent manner, the GATOR1 complex to the lysosomal membranes
CC and allows its interaction with GATOR2 and the RAG GTPases. Functions
CC upstream of the RAG GTPases and is required to negatively regulate
CC mTORC1 signaling in absence of amino acids (By similarity). In absence
CC of the KICSTOR complex mTORC1 is constitutively localized to the
CC lysosome and activated. The KICSTOR complex is also probably involved
CC in the regulation of mTORC1 by glucose (PubMed:28199306,
CC PubMed:28199315). May play a role in the cellular response to oxidative
CC stress (PubMed:20045724). {ECO:0000250|UniProtKB:Q5T011,
CC ECO:0000269|PubMed:20045724, ECO:0000269|PubMed:28199306,
CC ECO:0000269|PubMed:28199315}.
CC -!- SUBUNIT: Part of the KICSTOR complex composed of KPTN, ITFG2, KICS2 and
CC SZT2. SZT2 probably serves as a link between the other three proteins
CC in the KICSTOR complex and may mediate the direct interaction with the
CC GATOR complex via GATOR1. The KICSTOR complex interacts directly with
CC the GATOR1 complex and most probably indirectly with the GATOR2 complex
CC in an amino acid-independent manner. {ECO:0000250|UniProtKB:Q5T011}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q5T011}.
CC Peroxisome {ECO:0000269|PubMed:20045724}. Note=Localization to
CC lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q5T011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2A9C3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A9C3-2; Sequence=VSP_039917;
CC -!- TISSUE SPECIFICITY: Mostly expressed in brain, spinal cord and lung.
CC {ECO:0000269|PubMed:19624305, ECO:0000269|PubMed:20045724}.
CC -!- INDUCTION: Induced in cells resistant to glutamate toxicity.
CC {ECO:0000269|PubMed:20045724}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice lacking Szt2 are born at an
CC expected Mendelian ratio, but they do not survive weaning or any
CC fasting (PubMed:28199315). They display increased mTORC1 signaling in
CC several tissues (PubMed:28199306, PubMed:28199315). Mutant mice with a
CC gene trap-induced truncating mutation display embryonic lethality and
CC surviving mutants show significantly decreased threshold to minimal
CC forebrain clonic seizures (PubMed:19624305).
CC {ECO:0000269|PubMed:19624305, ECO:0000269|PubMed:28199306,
CC ECO:0000269|PubMed:28199315}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52935.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH52935.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=GU433214; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; FJ998170; ACS91341.1; -; mRNA.
DR EMBL; GU433214; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL627212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059842; AAH59842.2; -; mRNA.
DR EMBL; BC052935; AAH52935.1; ALT_SEQ; mRNA.
DR CCDS; CCDS51283.1; -. [A2A9C3-1]
DR RefSeq; NP_937813.3; NM_198170.4. [A2A9C3-1]
DR BioGRID; 231000; 5.
DR STRING; 10090.ENSMUSP00000074862; -.
DR iPTMnet; A2A9C3; -.
DR PhosphoSitePlus; A2A9C3; -.
DR EPD; A2A9C3; -.
DR jPOST; A2A9C3; -.
DR MaxQB; A2A9C3; -.
DR PaxDb; A2A9C3; -.
DR PeptideAtlas; A2A9C3; -.
DR PRIDE; A2A9C3; -.
DR ProteomicsDB; 263198; -. [A2A9C3-1]
DR ProteomicsDB; 263199; -. [A2A9C3-2]
DR Antibodypedia; 32333; 86 antibodies from 15 providers.
DR DNASU; 230676; -.
DR Ensembl; ENSMUST00000075406; ENSMUSP00000074862; ENSMUSG00000033253. [A2A9C3-1]
DR GeneID; 230676; -.
DR KEGG; mmu:230676; -.
DR UCSC; uc012djw.2; mouse. [A2A9C3-1]
DR UCSC; uc012djx.2; mouse. [A2A9C3-2]
DR CTD; 23334; -.
DR MGI; MGI:3033336; Szt2.
DR VEuPathDB; HostDB:ENSMUSG00000033253; -.
DR eggNOG; ENOG502QPW4; Eukaryota.
DR GeneTree; ENSGT00390000018402; -.
DR HOGENOM; CLU_000250_0_0_1; -.
DR InParanoid; A2A9C3; -.
DR OMA; AHPDLHK; -.
DR OrthoDB; 347778at2759; -.
DR PhylomeDB; A2A9C3; -.
DR TreeFam; TF333377; -.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 230676; 3 hits in 72 CRISPR screens.
DR PRO; PR:A2A9C3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A9C3; protein.
DR Bgee; ENSMUSG00000033253; Expressed in rostral migratory stream and 223 other tissues.
DR ExpressionAtlas; A2A9C3; baseline and differential.
DR Genevisible; A2A9C3; MM.
DR GO; GO:1990130; C:GATOR1 complex; ISO:MGI.
DR GO; GO:0061700; C:GATOR2 complex; ISO:MGI.
DR GO; GO:0140007; C:KICSTOR complex; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0021540; P:corpus callosum morphogenesis; ISO:MGI.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:1901668; P:regulation of superoxide dismutase activity; IMP:UniProtKB.
DR GO; GO:0031667; P:response to nutrient levels; IMP:UniProtKB.
DR InterPro; IPR033228; SZT2.
DR PANTHER; PTHR14918; PTHR14918; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lysosome; Membrane; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..3431
FT /note="KICSTOR complex protein SZT2"
FT /id="PRO_0000399821"
FT REGION 699..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1188
FT /note="Mediates interaction with the GATOR1 complex"
FT /evidence="ECO:0000250|UniProtKB:Q5T011"
FT REGION 1162..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2113..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2450..2512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2735..2756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2866..2899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2461..2485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T011"
FT MOD_RES 1415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T011"
FT MOD_RES 1640
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T011"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T011"
FT VAR_SEQ 2131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20045724"
FT /id="VSP_039917"
FT CONFLICT 275
FT /note="C -> S (in Ref. 1; GU433214)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="N -> K (in Ref. 1; GU433214)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="L -> C (in Ref. 1; GU433214)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="L -> H (in Ref. 1; GU433214)"
FT /evidence="ECO:0000305"
FT CONFLICT 1204
FT /note="S -> T (in Ref. 1; GU433214)"
FT /evidence="ECO:0000305"
FT CONFLICT 1308
FT /note="F -> S (in Ref. 1; GU433214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3431 AA; 377627 MW; 2DADDD0F72FC38F7 CRC64;
MASERPEPEV EEAGQVFLLM KKDYRISRNV RLAWFLNHLH QTVQATPQEL LLQSEQELEV
LSVLPPGWQP DEPVVPRPFL LVPSTRVTFL AWQYRFVIEL DLSPSTGIVD DSTGEILFDE
VFHALSRCLG GLLRPFRVPG SCINFQPEIY VTIQAYSSII GLQSHQVLVQ GCLLDPSQRE
AFLQQVYEQL CLFEDKVATM LQQQYEPQGQ AEDQSPESGE SLGRKVGVSM VTADLGLVSM
IRQGILALQL LPSNSSAGII VITDGVTSVP DVAVCETLLN QLRSGTVACS FVQVGGVYSY
DCSFGHVPNV ELMKFIAMAT FGSYLSTCPE TEPGNLGLTV YHRAFLLYSF LRSGEALNPE
YYCGSQHRLF NEHLVSASSN PALALRRKKH TEKEVPADLV STVSVRLREG YSVREVTLAK
GGSQLEVKLV LLWKHNMRIE YVAVAPWPLE PEGPRGTRVE VTMEGGYDIL HDVSCALRQP
IRSLYRTHVI RRFWNTLQSI NQTDQMLAHL QSFSSVPEHF TLPDSTKSGV PLFYIPPGSS
TPVLSLQHSG SDSSHAQFAA YWKPVLSMDA NSWQRWLHMH RLVLILEHDT PLPKHLHTPG
SNGRYSTIQC RISHSSLTSL LRDWSSFVLV EGYSYVKLLS SAPDQPPSSF YMVRIISKTP
CMVLRLGFPI GTPAQARHKI VSGLKEEILR LRFPHRVQSK EPTPKVKRKG LGGVGGSSPS
KSPPTLGPQQ ALSDRPCLVV LHKPLDKLLI RYEKLPLDYR APFLLTLEPP GPLPLVSGRS
ASSSLASLSR YLYHRRWLWS VPSGLAPTLP LSATAQLLSV LTEVRLSEGF HFACSGEGII
NMVLELPVQN EPLGQAAAEE KHTCVVQYIL FPPHSTSTKD SFSTDDDNDV EVEALEGDSE
LNLVTEVWVE PQYGRVGPGP ENWKHLQDLT YSEIPQALHP RDAACIGSLL TFEYLIQLCQ
SKEWGPLPPE PRLSDGLDQR GDTCVHEIPF HFDLLGLLPQ CQQLQMFFLL LSREPEGVPL
AEGPCPTNDM VLCLLHSCLG QELSDREIPL TPADQAAFLN EVLRRSLRDP GPEGPPVGGH
AVAKDRAGNS TQASGDSTLP SQSVVIPGVL RSSISAQPPQ WHCYARLLGP QHVFLTFLPA
TFSDVQHLTA YGLESSFQEE TKPKLGDWSG APSLKDPGAT GTKATESQVP TLSVTLASDS
AQDSGEPSTP SCQDLAANSG RQAPQTEGAD GPRTRCPVYI YSCSLEALRE QMVGLQPPQA
PRDLIFRAQD LDHPSSSSAW MEPRCKEAAT HCALLQEHAQ RCFVRGLFRS LQQAQSVTCQ
DLLTAVDACE ELLQEIDITS FLLALCGHTW GLPHAPPSPG PLSPGPFSSS IEEGPEPRER
AILVSESSIE TEDLSEPEFQ SSRVSGNLDP GPEISLTDVC QLRGEAHDAL HSLIQEKFLE
ISRLHFRTVP SNPHYFFYCP PSSRREDEGP RDTVDRKISD LEFSEAELVG EEGDTSACCV
VTESDPELEV EYRESREPDL GPAGLDSASL SDADTVNPDE DSFSILGGDS PTGPDSLMHD
LPPLFLHLTC SVRLRGQHSS VPVCSLPTCL GQVLSSLEGP PIGGRVPLRD LSITLDVFVL
TLPLEVELPP ASDPQHHRST SESSASFPRS PGQPSSLRSD DGLGPPLPPP EEERHPGLSS
LAMPHRLAIE STMNEIRWLL EDEMVGALRR GGIPQSPALH RAAAHIHSSS GRPTCLRQAP
PLSFVFGPER SLTQFKEEFR RLHLPGHVLL EDPDSGFFFV AAGQQPGVLH GEPPSAAWAW
HNHEDRAEDA EGEVLTASPQ VPGSLEDSEG TPLISLPSLS QGGSQPGPSR GLSLMSSQGS
VDSDHLGYDG GSSGSDSEGP GETLGEKALF TLRTPPGPAP PQPSLPVLPG PSLPDFWLIV
RILQDRVEVY AHARSLSRED GGPGAECRHL QQFLVRRVGE ICREVNQRLL LQDLHDSHVC
NSLLVAESEE DLWRSETPFH SRQRAVLPSD DFAADESCAP RGYLAATMQF VPGHFSCDVV
WGTVIRVHSR LKMGPSMGVS RAIQALRSVL NAFSVVNRKN MFVYQERATK AVYYLRLLET
SCSDRPWEGD TLPPSLALSR SQEPISSEDS VAPRSPLDMA SSRSSDAVRP VGQVDRHIQL
LVHGVGQAGP EITDELVRVL RRRLDEATLD IITVMLVRNC KLTPADVEFI QPPGSLPSEV
LHLVLPPSCR PCLPALAWYL RQNLLTFLHS PKYTDSNSRN HFQHPLPAQG GLPDLDIYLY
NKPGGQGTGG KGVACITLAF VEEGGTPISL ASWPPSSPGP PDPLREEEFE QLTQVIRCPN
TLDSCSAQDG SPRLRLDVWE KGNISIVQLE EKLRAAARQA LADAIMELRL LPASLCTEDI
PPGSLKSGPL DTKSPACRAN TFPCTPVSGE PVTPPSKAGR RSFWDMLSKT EAGDLGSPKT
TDDIVLDRPE DTRGRRRHKT ENVRTPGGSE RAPGPDSGAQ RQRRRTTQLE EGEVGTLHPV
FARVIQRWMG FMVQIGCASV SRSSTHMVSR FLLPSILSEF TTLVISMAGD TSVRVFEQHL
GSEPDVFSPC SPGQLGPAPR PAAQRHLLLL GRNFAQWRRP TQQAAKAVQR FESGGDGSPG
RSAPRQRLLL LEVTDKKLQL LTYNWAPDLG AALGRALIRL VQWQNARAHL ISCLLSQKLG
LFHHCGQLDF PMRDGKEPNP FLLPTMEVET LIRNASPPLS REQGRLSGSS RGGGPLSLDT
FPFDEALRDI TAARPSSTGG PAPRPPDPVT YHGQQFLEIK MTERKELERQ MKMENLFVTW
QQRSAPASMP ISAGELETLK QSSRLVHYCA TALLFDPAAW LHGPPETCAP SEGQRRPCPE
SGSGSREVPT SCESLDVPPP GAREEPWLKE LSLAFLQQYV QYLQSIGFVL VPLRPPSPAR
STSRLRAMAI LGTEGRGSFS CPKAKAEGSP KSTSTPVTTY HLQRALPGGI ILMELTFQGC
YFCVKQFALE CSRIPMGQAV NSQLSLLFTE ECDKVRDLMH VHSFSYDFHL RLVHQHVLGA
HLALRHGYHL TTFLQHFLAH HPDGPHFGRN HIYQGTLELP TPLIAAHQLY NYVADHASSY
HMKPLRMARP GGPEHNEYAL VSAWHSSGSY LDSEGLRHQD DFDVSLLVCH SAAPFEEQGE
AERHVLRLQF FVVLTSQREL FPRLTADMRR FRKPSRLPLE PETPGSLVGS PREASGMMLA
PGPAPLFPPL AAEVGMARAR LAQLVRLAGG HCRRDTLWKR LFLLEPPGPD RLRLGGRLAL
AELEELLEAV HAKSIADIDP QLDCFLSMTV SWYQSLIKVL LSRFPQSCRH FQSPDLGTQY
LVVLNQKFTD CFVLVFLDSH LGKTSLTVVF REPFPVQPQD SESPPAQLVS TYHHLESVIN
TACFTLWTRL L
