SIDT2_MOUSE
ID SIDT2_MOUSE Reviewed; 832 AA.
AC Q8CIF6; Q80XD7; Q922R2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=SID1 transmembrane family member 2;
DE Flags: Precursor;
GN Name=Sidt2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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 [2]
RP PROTEIN SEQUENCE OF 228-235, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-165.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=20965152; DOI=10.1016/j.bbrc.2010.09.133;
RA Jialin G., Xuefan G., Huiwen Z.;
RT "SID1 transmembrane family, member 2 (Sidt2): A novel lysosomal membrane
RT protein.";
RL Biochem. Biophys. Res. Commun. 402:588-594(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-403 AND SER-404, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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 [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23776622; DOI=10.1371/journal.pone.0066139;
RA Gao J., Gu X., Mahuran D.J., Wang Z., Zhang H.;
RT "Impaired glucose tolerance in a mouse model of Sidt2 deficiency.";
RL PLoS ONE 8:E66139-E66139(2013).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF PHE-154 AND SER-564.
RX PubMed=26067272; DOI=10.1074/jbc.m115.658864;
RA Li W., Koutmou K.S., Leahy D.J., Li M.;
RT "Systemic RNA interference deficiency-1 (SID-1) extracellular domain
RT selectively binds long double-stranded RNA and is required for RNA
RT transport by SID-1.";
RL J. Biol. Chem. 290:18904-18913(2015).
RN [8]
RP FUNCTION, INTERACTION WITH LAMP2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP SER-564.
RX PubMed=27046251; DOI=10.1080/15548627.2016.1145325;
RA Aizawa S., Fujiwara Y., Contu V.R., Hase K., Takahashi M., Kikuchi H.,
RA Kabuta C., Wada K., Kabuta T.;
RT "Lysosomal putative RNA transporter SIDT2 mediates direct uptake of RNA by
RT lysosomes.";
RL Autophagy 12:565-578(2016).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=27233614; DOI=10.1016/j.bbrc.2016.05.122;
RA Gao J., Zhang Y., Yu C., Tan F., Wang L.;
RT "Spontaneous nonalcoholic fatty liver disease and ER stress in Sidt2
RT deficiency mice.";
RL Biochem. Biophys. Res. Commun. 476:326-332(2016).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF SER-564.
RX PubMed=27846365; DOI=10.1080/15548627.2016.1248019;
RA Aizawa S., Contu V.R., Fujiwara Y., Hase K., Kikuchi H., Kabuta C.,
RA Wada K., Kabuta T.;
RT "Lysosomal membrane protein SIDT2 mediates the direct uptake of DNA by
RT lysosomes.";
RL Autophagy 13:218-222(2017).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=27987306; DOI=10.1002/1873-3468.12528;
RA Beck A., Fecher-Trost C., Wolske K., Philipp S.E., Flockerzi V.,
RA Wissenbach U.;
RT "Identification of Sidt2 as a lysosomal cation-conducting protein.";
RL FEBS Lett. 591:76-87(2017).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-359; TYR-410; TYR-428
RP AND TYR-830, AND INTERACTION WITH AP-1 AND AP-2 COMPLEXES.
RX PubMed=28724756; DOI=10.1242/jcs.202481;
RA Contu V.R., Hase K., Kozuka-Hata H., Oyama M., Fujiwara Y., Kabuta C.,
RA Takahashi M., Hakuno F., Takahashi S.I., Wada K., Kabuta T.;
RT "Lysosomal targeting of SIDT2 via multiple YXXPhi motifs is required for
RT SIDT2 function in the process of RNautophagy.";
RL J. Cell Sci. 130:2843-2853(2017).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF PHE-154 AND SER-564.
RX PubMed=28277980; DOI=10.1080/15476286.2017.1302641;
RA Takahashi M., Contu V.R., Kabuta C., Hase K., Fujiwara Y., Wada K.,
RA Kabuta T.;
RT "SIDT2 mediates gymnosis, the uptake of naked single-stranded
RT oligonucleotides into living cells.";
RL RNA Biol. 2017:1-10(2017).
CC -!- FUNCTION: Mediates the translocation of RNA and DNA across the
CC lysosomal membrane during RNA and DNA autophagy (RDA), a process in
CC which RNA and DNA is directly imported into lysosomes in an ATP-
CC dependent manner, and degraded (PubMed:27046251, PubMed:27846365,
CC PubMed:28724756). Involved in the uptake of single-stranded
CC oligonucleotides by living cells, a process called gymnosis
CC (PubMed:28277980). In vitro, mediates the uptake of linear DNA more
CC efficiently than that of circular DNA, but exhibits similar uptake
CC efficacy toward RNA and DNA (PubMed:27846365). Binds long double-
CC stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA shorter than
CC 100 bp (PubMed:26067272). {ECO:0000269|PubMed:26067272,
CC ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:27846365,
CC ECO:0000269|PubMed:28277980, ECO:0000269|PubMed:28724756}.
CC -!- SUBUNIT: Interacts with adapter protein complex 1 (AP-1) and AP-2, but
CC not AP-3 and AP-4 (PubMed:28724756). Interacts with LAMP2
CC (PubMed:27046251). {ECO:0000269|PubMed:27046251,
CC ECO:0000269|PubMed:28724756}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:20965152,
CC ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:28724756}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:20965152}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8NBJ9}. Note=Mainly localizes to lysosomes and
CC only partly to the plasma membrane (By similarity). Lysosomal
CC localization is required for SIDT2-mediated intracellular degradation
CC of endogenous RNA (PubMed:28724756). {ECO:0000250|UniProtKB:Q8NBJ9,
CC ECO:0000269|PubMed:28724756}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CIF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CIF6-2; Sequence=VSP_013525;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in the liver, brain and
CC kidney (at protein level). {ECO:0000269|PubMed:20965152,
CC ECO:0000269|PubMed:23776622, ECO:0000269|PubMed:27987306}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19349973,
CC ECO:0000269|PubMed:20965152}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice demonstrate a statistically
CC significant departure from Mendel's law, but there is no significant
CC differences in their weights or appearance as compared to wild-type
CC controls as newborns. At 5 weeks of age, male mice show reduced weight
CC and size as compared to control animals. This phenotype is not observed
CC in females. Mutant animals exhibit increased fasting glucose levels and
CC impaired glucose tolerance, probably due to impaired insulin granule
CC exocytosis by pancreatic islet cells (PubMed:23776622). At 3 months of
CC age, serum triglyceride and free fatty acid levels increase in knockout
CC mice fed on normal chow. Mice gradually develop hepatic steatosis, with
CC varying degrees of inflammatory changes (PubMed:27233614).
CC {ECO:0000269|PubMed:23776622, ECO:0000269|PubMed:27233614}.
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
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DR EMBL; BC006873; AAH06873.1; -; mRNA.
DR EMBL; BC023957; AAH23957.1; -; mRNA.
DR EMBL; BC051101; AAH51101.1; -; mRNA.
DR CCDS; CCDS23138.1; -. [Q8CIF6-1]
DR CCDS; CCDS72225.1; -. [Q8CIF6-2]
DR RefSeq; NP_001276597.1; NM_001289668.1. [Q8CIF6-2]
DR RefSeq; NP_758461.1; NM_172257.4. [Q8CIF6-1]
DR AlphaFoldDB; Q8CIF6; -.
DR BioGRID; 229546; 34.
DR IntAct; Q8CIF6; 34.
DR STRING; 10090.ENSMUSP00000044290; -.
DR GlyGen; Q8CIF6; 10 sites.
DR iPTMnet; Q8CIF6; -.
DR PhosphoSitePlus; Q8CIF6; -.
DR SwissPalm; Q8CIF6; -.
DR EPD; Q8CIF6; -.
DR jPOST; Q8CIF6; -.
DR MaxQB; Q8CIF6; -.
DR PaxDb; Q8CIF6; -.
DR PRIDE; Q8CIF6; -.
DR ProteomicsDB; 261402; -. [Q8CIF6-1]
DR ProteomicsDB; 261403; -. [Q8CIF6-2]
DR Antibodypedia; 32315; 100 antibodies from 20 providers.
DR DNASU; 214597; -.
DR Ensembl; ENSMUST00000038488; ENSMUSP00000044290; ENSMUSG00000034908. [Q8CIF6-1]
DR Ensembl; ENSMUST00000114573; ENSMUSP00000110220; ENSMUSG00000034908. [Q8CIF6-2]
DR GeneID; 214597; -.
DR KEGG; mmu:214597; -.
DR UCSC; uc009pgt.2; mouse. [Q8CIF6-1]
DR UCSC; uc009pgu.2; mouse. [Q8CIF6-2]
DR CTD; 51092; -.
DR MGI; MGI:2446134; Sidt2.
DR VEuPathDB; HostDB:ENSMUSG00000034908; -.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR GeneTree; ENSGT00390000010091; -.
DR HOGENOM; CLU_357018_0_0_1; -.
DR InParanoid; Q8CIF6; -.
DR OMA; GLHQTMT; -.
DR OrthoDB; 139174at2759; -.
DR PhylomeDB; Q8CIF6; -.
DR TreeFam; TF313076; -.
DR BioGRID-ORCS; 214597; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Sidt2; mouse.
DR PRO; PR:Q8CIF6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CIF6; protein.
DR Bgee; ENSMUSG00000034908; Expressed in granulocyte and 64 other tissues.
DR ExpressionAtlas; Q8CIF6; baseline and differential.
DR Genevisible; Q8CIF6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035650; F:AP-1 adaptor complex binding; IDA:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:WormBase.
DR GO; GO:0051032; F:nucleic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0009749; P:response to glucose; IMP:MGI.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR GO; GO:0050658; P:RNA transport; IDA:UniProtKB.
DR GO; GO:0003323; P:type B pancreatic cell development; IMP:MGI.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:MGI.
DR InterPro; IPR025958; SID1_TM_fam.
DR PANTHER; PTHR12185; PTHR12185; 1.
DR Pfam; PF13965; SID-1_RNA_chan; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW DNA-binding; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; RNA-binding; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..832
FT /note="SID1 transmembrane family member 2"
FT /id="PRO_0000032579"
FT TOPO_DOM 19..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..746
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 797..817
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 818..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 386
FT /note="Q -> QGHDQFKRRLPSGQMRQLCIAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013525"
FT MUTAGEN 154
FT /note="F->T: Decreased gymnosis and decreased affinity for
FT 700-bp RNA. No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:26067272,
FT ECO:0000269|PubMed:28277980"
FT MUTAGEN 359
FT /note="Y->S: Decreased lysosomal localization. Decreased
FT interaction with AP-1 and AP-2 complexes; when associated
FT with S-410. Almost complete loss of lysosomal localization
FT and decreased interaction with AP-1 and AP-2 complexes;
FT when associated with S-428. Decreased interaction with AP-1
FT and AP-2 complexes, almost complete loss of lysosomal
FT localization, mislocalization to the Golgi apparatus and
FT almost complete loss of RNA degradation by lysosomes; when
FT associated with S-410 and S-428."
FT /evidence="ECO:0000269|PubMed:28724756"
FT MUTAGEN 410
FT /note="Y->S: Drastically decreased lysosomal localization.
FT Decreased interaction with AP-1 and AP-2 complexes; when
FT associated with S-359. Decreased interaction with AP-1 and
FT AP-2 complexes, almost complete loss of lysosomal
FT localization, mislocalization to the Golgi apparatus and
FT almost complete loss of RNA degradation by lysosomes; when
FT associated with S-359 and S-428. No effect on interaction
FT with AP-1 and AP-2 complexes, nor on RNA uptake by
FT lysosomes; when associated with S-428."
FT /evidence="ECO:0000269|PubMed:28724756"
FT MUTAGEN 428
FT /note="Y->S: Drastically decreased lysosomal localization.
FT Almost complete loss of lysosomal localization and
FT decreased interaction with AP-1 and AP-2 complexes; when
FT associated with S-359. No effect on interaction with AP-1
FT and AP-2 complexes, nor on RNA uptake by lysosomes; when
FT associated with S-410. Decreased interaction with AP-1 and
FT AP-2 complexes, almost complete loss of lysosomal
FT localization, mislocalization to the Golgi apparatus and
FT almost complete loss of RNA degradation by lysosomes; when
FT associated with S-359 and S-410."
FT /evidence="ECO:0000269|PubMed:28724756"
FT MUTAGEN 564
FT /note="S->A: Decreased gymnosis and RNA and DNA uptake by
FT lysosomes and degradation. Decreased affinity for 700-bp
FT RNA. No effect on lysosomal subcellular location, nor on
FT LAMP2-binding."
FT /evidence="ECO:0000269|PubMed:26067272,
FT ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:28277980"
FT MUTAGEN 830
FT /note="Y->S: No effect on lysosomal localization, nor on
FT RNA uptake by lysosomes."
FT /evidence="ECO:0000269|PubMed:28724756"
SQ SEQUENCE 832 AA; 94501 MW; 99C5C8C25E4464A5 CRC64;
MIAWRLPLCV LLVASVESHL GALGPKNVSQ KDAEFERTYA DDVNSELVNI YTFNHTVTRN
RTEGVRVSVN VLNKQKGAPL LFVVRQKEAV VSFQVPLILR GLYQRKYLYQ KVERTLCQPP
TKNESEIQFF YVDVSTLSPV NTTYQLRVNR VDNFVLRTGE LFTFNTTAAQ PQYFKYEFPD
GVDSVIVKVT SKKAFPCSVI SIQDVLCPVY DLDNNVAFIG MYQTMTKKAA ITVQRKDFPS
NSFYVVVVVK TEDQACGGSL PFYPFVEDEP VDQGHRQKTL SVLVSQAVTS EAYVGGMLFC
LGIFLSFYLL TVLLACWENW RQRKKTLLLA IDRACPESGH ARVLADSFPG SAPYEGYNYG
SFENGSGSTD GLVESAGSGD LSYSYQDRSF DAVGPRPRLD SMSSVEEDDY DTLTDIDSDK
NVIRTKQYLC VADLARKDKR VLRKKYQIYF WNIATIAVFY ALPVVQLVIT YQTVVNVTGN
QDICYYNFLC AHPLGNLSAF NNILSNLGYI LLGLLFLLII LQREINHNRA LLRNDLYALE
CGIPKHFGLF YAMGTALMME GLLSACYHVC PNYTNFQFDT SFMYMIAGLC MLKLYQKRHP
DINASAYSAY ACLAIVIFFS VLGVVFGKGN TAFWIVFSVI HIISTLLLST QLYYMGRWKL
DSGIFRRILH VLYTDCIRQC SGPLYTDRMV LLVMGNIINW SLAAYGLIMR PNDFASYLLA
IGICNLLLYF AFYIIMKLRS GERIKLIPLL CIVCTSVVWG FALFFFFQGL STWQKTPAES
REHNRDCILL DFFDDHDIWH FLSSIAMFGS FLVLLTLDDD LDTVQRDKIY VF
