SIDT2_HUMAN
ID SIDT2_HUMAN Reviewed; 832 AA.
AC Q8NBJ9; Q8NBY7; Q9Y357;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=SID1 transmembrane family member 2;
DE Flags: Precursor;
GN Name=SIDT2; ORFNames=CGI-40, PSEC0072, UNQ685/PRO1325;
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] (ISOFORM 2).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP PROTEIN SEQUENCE OF 19-33.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-832.
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-832.
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-403 AND SER-404, 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 [9]
RP FUNCTION, INTERACTION WITH LAMP2, AND SUBCELLULAR LOCATION.
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 [10]
RP FUNCTION.
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 FUNCTION, AND SUBCELLULAR LOCATION.
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 or DNA is directly imported into lysosomes in an ATP-
CC dependent manner, and degraded (PubMed:27046251, PubMed:27846365).
CC Involved in the uptake of single-stranded oligonucleotides by living
CC cells, a process called gymnosis (PubMed:28277980). In vitro, mediates
CC the uptake of linear DNA more efficiently than that of circular DNA,
CC but exhibits similar uptake efficacy toward RNA and DNA. Binds long
CC double-stranded RNA (dsRNA) (500 - 700 base pairs), but not dsRNA
CC shorter than 100 bp (By similarity). {ECO:0000250|UniProtKB:Q8CIF6,
CC ECO:0000269|PubMed:27046251, ECO:0000269|PubMed:27846365,
CC ECO:0000269|PubMed:28277980}.
CC -!- SUBUNIT: Interacts with adapter protein complex 1 (AP-1) and AP-2, but
CC not AP-3 and AP-4 (By similarity). Interacts with LAMP2
CC (PubMed:27046251). {ECO:0000250|UniProtKB:Q8CIF6,
CC ECO:0000269|PubMed:27046251}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319,
CC ECO:0000269|PubMed:28277980}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17897319}. Cell membrane
CC {ECO:0000269|PubMed:28277980}. Note=Mainly localizes to lysosomes and
CC only partly to the plasma membrane (PubMed:28277980). Lysosomal
CC localization is required for SIDT2-mediated intracellular degradation
CC of endogenous RNA (By similarity). {ECO:0000250|UniProtKB:Q8CIF6,
CC ECO:0000269|PubMed:28277980}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBJ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBJ9-2; Sequence=VSP_013523, VSP_013524;
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SID1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11427.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF151799; AAD34036.1; -; mRNA.
DR EMBL; AY358442; AAQ88807.1; -; mRNA.
DR EMBL; AK075137; BAC11427.1; ALT_INIT; mRNA.
DR EMBL; AK075471; BAC11641.1; ALT_INIT; mRNA.
DR CCDS; CCDS31682.1; -. [Q8NBJ9-1]
DR RefSeq; NP_001035545.1; NM_001040455.1. [Q8NBJ9-1]
DR AlphaFoldDB; Q8NBJ9; -.
DR BioGRID; 119281; 144.
DR IntAct; Q8NBJ9; 18.
DR MINT; Q8NBJ9; -.
DR STRING; 9606.ENSP00000314023; -.
DR TCDB; 1.A.79.1.3; the cholesterol uptake protein (chup) or double stranded rna uptake family.
DR GlyGen; Q8NBJ9; 10 sites.
DR iPTMnet; Q8NBJ9; -.
DR PhosphoSitePlus; Q8NBJ9; -.
DR SwissPalm; Q8NBJ9; -.
DR BioMuta; SIDT2; -.
DR DMDM; 62901098; -.
DR EPD; Q8NBJ9; -.
DR jPOST; Q8NBJ9; -.
DR MassIVE; Q8NBJ9; -.
DR MaxQB; Q8NBJ9; -.
DR PaxDb; Q8NBJ9; -.
DR PeptideAtlas; Q8NBJ9; -.
DR PRIDE; Q8NBJ9; -.
DR ProteomicsDB; 72784; -. [Q8NBJ9-1]
DR ProteomicsDB; 72785; -. [Q8NBJ9-2]
DR Antibodypedia; 32315; 100 antibodies from 20 providers.
DR DNASU; 51092; -.
DR Ensembl; ENST00000324225.9; ENSP00000314023.4; ENSG00000149577.16. [Q8NBJ9-1]
DR Ensembl; ENST00000620360.4; ENSP00000482762.1; ENSG00000149577.16. [Q8NBJ9-1]
DR GeneID; 51092; -.
DR KEGG; hsa:51092; -.
DR MANE-Select; ENST00000324225.9; ENSP00000314023.4; NM_001040455.2; NP_001035545.1.
DR UCSC; uc001pqh.2; human. [Q8NBJ9-1]
DR CTD; 51092; -.
DR DisGeNET; 51092; -.
DR GeneCards; SIDT2; -.
DR HGNC; HGNC:24272; SIDT2.
DR HPA; ENSG00000149577; Low tissue specificity.
DR MIM; 617551; gene.
DR neXtProt; NX_Q8NBJ9; -.
DR OpenTargets; ENSG00000149577; -.
DR PharmGKB; PA134910333; -.
DR VEuPathDB; HostDB:ENSG00000149577; -.
DR eggNOG; ENOG502QUXZ; Eukaryota.
DR GeneTree; ENSGT00390000010091; -.
DR InParanoid; Q8NBJ9; -.
DR OrthoDB; 139174at2759; -.
DR PhylomeDB; Q8NBJ9; -.
DR TreeFam; TF313076; -.
DR PathwayCommons; Q8NBJ9; -.
DR SignaLink; Q8NBJ9; -.
DR BioGRID-ORCS; 51092; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; SIDT2; human.
DR GenomeRNAi; 51092; -.
DR Pharos; Q8NBJ9; Tbio.
DR PRO; PR:Q8NBJ9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NBJ9; protein.
DR Bgee; ENSG00000149577; Expressed in endothelial cell and 196 other tissues.
DR ExpressionAtlas; Q8NBJ9; baseline and differential.
DR Genevisible; Q8NBJ9; HS.
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; ISS:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0051032; F:nucleic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0051033; F:RNA transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
DR GO; GO:0050658; P:RNA transport; IDA:UniProtKB.
DR GO; GO:0003323; P:type B pancreatic cell development; IEA:Ensembl.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
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:0000269|PubMed:15340161"
FT CHAIN 19..832
FT /note="SID1 transmembrane family member 2"
FT /id="PRO_0000032578"
FT TOPO_DOM 19..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..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:18669648"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
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:0000255"
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 387
FT /note="G -> GHDQFKRRLPSGQMRQLCIAMG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_013523"
FT VAR_SEQ 814..832
FT /note="LLTLDDDLDTVQRDKIYVF -> SGPPGAALRIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_013524"
FT VARIANT 631
FT /note="T -> M (in dbSNP:rs12285035)"
FT /id="VAR_034493"
FT VARIANT 636
FT /note="V -> I (in dbSNP:rs17120425)"
FT /id="VAR_034494"
FT CONFLICT 450
FT /note="F -> L (in Ref. 4; BAC11427)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="Q -> R (in Ref. 5; BAC11641)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="D -> N (in Ref. 5; BAC11641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 94454 MW; 5DDA17E7DC5A33FD CRC64;
MFALGLPFLV LLVASVESHL GVLGPKNVSQ KDAEFERTYV DEVNSELVNI YTFNHTVTRN
RTEGVRVSVN VLNKQKGAPL LFVVRQKEAV VSFQVPLILR GMFQRKYLYQ KVERTLCQPP
TKNESEIQFF YVDVSTLSPV NTTYQLRVSR MDDFVLRTGE QFSFNTTAAQ PQYFKYEFPE
GVDSVIVKVT SNKAFPCSVI SIQDVLCPVY DLDNNVAFIG MYQTMTKKAA ITVQRKDFPS
NSFYVVVVVK TEDQACGGSL PFYPFAEDEP VDQGHRQKTL SVLVSQAVTS EAYVSGMLFC
LGIFLSFYLL TVLLACWENW RQKKKTLLVA IDRACPESGH PRVLADSFPG SSPYEGYNYG
SFENVSGSTD GLVDSAGTGD LSYGYQGRSF EPVGTRPRVD SMSSVEEDDY DTLTDIDSDK
NVIRTKQYLY VADLARKDKR VLRKKYQIYF WNIATIAVFY ALPVVQLVIT YQTVVNVTGN
QDICYYNFLC AHPLGNLSAF NNILSNLGYI LLGLLFLLII LQREINHNRA LLRNDLCALE
CGIPKHFGLF YAMGTALMME GLLSACYHVC PNYTNFQFDT SFMYMIAGLC MLKLYQKRHP
DINASAYSAY ACLAIVIFFS VLGVVFGKGN TAFWIVFSII HIIATLLLST QLYYMGRWKL
DSGIFRRILH VLYTDCIRQC SGPLYVDRMV LLVMGNVINW SLAAYGLIMR PNDFASYLLA
IGICNLLLYF AFYIIMKLRS GERIKLIPLL CIVCTSVVWG FALFFFFQGL STWQKTPAES
REHNRDCILL DFFDDHDIWH FLSSIAMFGS FLVLLTLDDD LDTVQRDKIY VF
