SPIN_DROME
ID SPIN_DROME Reviewed; 605 AA.
AC Q9GQQ0; A1ZAA4; Q960X6; Q9GQP9; Q9GQQ1; Q9GQQ2; Q9GQQ3; Q9V7J3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein spinster;
DE AltName: Full=Protein benchwarmer;
DE AltName: Full=Protein diphthong;
GN Name=spin; Synonyms=bnch; ORFNames=CG8428;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E), AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11340170; DOI=10.1128/mcb.21.11.3775-3788.2001;
RA Nakano Y., Fujitani K., Kurihara J., Ragan J., Usui-Aoki K., Shimoda L.,
RA Lukacsovich T., Suzuki K., Sezaki M., Sano Y., Ueda R., Awano W.,
RA Kaneda M., Umeda M., Yamamoto D.;
RT "Mutations in the novel membrane protein spinster interfere with programmed
RT cell death and cause neural degeneration in Drosophila melanogaster.";
RL Mol. Cell. Biol. 21:3775-3788(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 74-605 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12408844; DOI=10.1016/s0896-6273(02)01014-0;
RA Sweeney S.T., Davis G.W.;
RT "Unrestricted synaptic growth in spinster-a late endosomal protein
RT implicated in TGF-beta-mediated synaptic growth regulation.";
RL Neuron 36:403-416(2002).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-217.
RX PubMed=15998804; DOI=10.1083/jcb.200412001;
RA Dermaut B., Norga K.K., Kania A., Verstreken P., Pan H., Zhou Y.,
RA Callaerts P., Bellen H.J.;
RT "Aberrant lysosomal carbohydrate storage accompanies endocytic defects and
RT neurodegeneration in Drosophila benchwarmer.";
RL J. Cell Biol. 170:127-139(2005).
CC -!- FUNCTION: Probable sphingolipid transporter that plays a central role
CC in endosomes and/or lysosomes storage. Involved in TGF-beta-mediated
CC synaptic growth regulation both pre- and postsynaptically via its
CC function in endosomal storage regulation. Also required during
CC oogenesis by regulating yolk spheres storage.
CC {ECO:0000269|PubMed:12408844, ECO:0000269|PubMed:15998804}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:12408844}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12408844}. Lysosome membrane
CC {ECO:0000269|PubMed:12408844}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12408844}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A; Synonyms=Type IV;
CC IsoId=Q9GQQ0-1; Sequence=Displayed;
CC Name=B; Synonyms=Type I;
CC IsoId=Q9GQQ0-2; Sequence=VSP_036367, VSP_036368;
CC Name=C; Synonyms=Type III;
CC IsoId=Q9GQQ0-3; Sequence=VSP_036367;
CC Name=D; Synonyms=Type II;
CC IsoId=Q9GQQ0-4; Sequence=VSP_036368;
CC Name=E; Synonyms=Type V;
CC IsoId=Q9GQQ0-5; Sequence=VSP_036366;
CC -!- TISSUE SPECIFICITY: Enriched in brain (at protein level).
CC {ECO:0000269|PubMed:12408844, ECO:0000269|PubMed:15998804}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both motoneurons and muscle
CC throughout the period of synaptic growth and development at the
CC neuromuscular junction. Expressed throughout the CNS, including
CC motoneurons. Weak expression is observed in embryonic muscle as well as
CC other tissues. Expressed throughout the larval CNS with pronounced
CC expression in motoneurons. Also strongly expressed in all body wall
CC muscle as well as other tissues, including a subset of epithelial cells
CC and the salivary glands. {ECO:0000269|PubMed:12408844}.
CC -!- DISRUPTION PHENOTYPE: In most cases, death at the late pupal stage,
CC probably due to lipid accumulation in endosomes/lysosomes. Some flies
CC survive until adulthood and display a strong rejection behavior of
CC female flies in response to male courtship accompanied by decreases in
CC the viability, adult life span, and oviposition rate of the flies. Some
CC oocytes and adult neural cells undergo degeneration, which is preceded
CC by reductions in programmed cell death of nurse cells in ovaries and of
CC neurons in the pupal nervous system, respectively. The central nervous
CC system (CNS) of flies accumulates lipopigments. Flies also display a
CC strong synaptic overgrowth: synapses reveal a strong increase in bouton
CC number and a deficit in presynaptic release caused by
CC enhanced/misregulated TGF-beta signaling. A widespread accumulation of
CC enlarged lysosomal and late endosomal inclusions is also present in
CC yolk spheres during oogenesis. {ECO:0000269|PubMed:11340170,
CC ECO:0000269|PubMed:12408844, ECO:0000269|PubMed:15998804}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC
CC 2.A.1.49) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93216.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF212366; AAG43825.1; -; mRNA.
DR EMBL; AF212367; AAG43826.1; -; mRNA.
DR EMBL; AF212368; AAG43827.1; -; mRNA.
DR EMBL; AF212369; AAG43828.1; -; mRNA.
DR EMBL; AF212370; AAG43829.1; -; mRNA.
DR EMBL; AE013599; AAF58060.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM70950.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70951.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70952.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70953.1; -; Genomic_DNA.
DR EMBL; BT032842; ACD81856.1; -; mRNA.
DR EMBL; AY051792; AAK93216.1; ALT_INIT; mRNA.
DR RefSeq; NP_524823.1; NM_080084.3. [Q9GQQ0-4]
DR RefSeq; NP_725530.1; NM_166144.2. [Q9GQQ0-3]
DR RefSeq; NP_725531.1; NM_166145.2. [Q9GQQ0-1]
DR RefSeq; NP_725532.1; NM_166146.2. [Q9GQQ0-2]
DR RefSeq; NP_725533.1; NM_166147.2. [Q9GQQ0-5]
DR AlphaFoldDB; Q9GQQ0; -.
DR SMR; Q9GQQ0; -.
DR BioGRID; 69637; 12.
DR IntAct; Q9GQQ0; 12.
DR STRING; 7227.FBpp0088549; -.
DR TCDB; 2.A.1.49.1; the major facilitator superfamily (mfs).
DR GlyGen; Q9GQQ0; 4 sites.
DR PaxDb; Q9GQQ0; -.
DR PRIDE; Q9GQQ0; -.
DR DNASU; 45380; -.
DR EnsemblMetazoa; FBtr0089589; FBpp0088548; FBgn0086676. [Q9GQQ0-5]
DR EnsemblMetazoa; FBtr0089590; FBpp0088549; FBgn0086676. [Q9GQQ0-4]
DR EnsemblMetazoa; FBtr0089591; FBpp0088550; FBgn0086676. [Q9GQQ0-3]
DR EnsemblMetazoa; FBtr0089592; FBpp0088551; FBgn0086676. [Q9GQQ0-2]
DR EnsemblMetazoa; FBtr0089593; FBpp0088552; FBgn0086676. [Q9GQQ0-1]
DR GeneID; 45380; -.
DR KEGG; dme:Dmel_CG8428; -.
DR UCSC; CG8428-RA; d. melanogaster. [Q9GQQ0-1]
DR UCSC; CG8428-RB; d. melanogaster.
DR UCSC; CG8428-RC; d. melanogaster.
DR UCSC; CG8428-RD; d. melanogaster.
DR UCSC; CG8428-RE; d. melanogaster.
DR CTD; 45380; -.
DR FlyBase; FBgn0086676; spin.
DR VEuPathDB; VectorBase:FBgn0086676; -.
DR eggNOG; KOG1330; Eukaryota.
DR GeneTree; ENSGT00390000005976; -.
DR HOGENOM; CLU_001265_5_12_1; -.
DR InParanoid; Q9GQQ0; -.
DR OMA; DQMVMSP; -.
DR PhylomeDB; Q9GQQ0; -.
DR Reactome; R-DME-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 45380; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45380; -.
DR PRO; PR:Q9GQQ0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0086676; Expressed in embryonic/larval hemocyte (Drosophila) and 21 other tissues.
DR ExpressionAtlas; Q9GQQ0; baseline and differential.
DR Genevisible; Q9GQQ0; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IDA:FlyBase.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; NAS:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:FlyBase.
DR GO; GO:0010001; P:glial cell differentiation; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0035193; P:larval central nervous system remodeling; IMP:FlyBase.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0040011; P:locomotion; IMP:FlyBase.
DR GO; GO:0007040; P:lysosome organization; IMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:FlyBase.
DR GO; GO:0045476; P:nurse cell apoptotic process; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0012501; P:programmed cell death; NAS:FlyBase.
DR GO; GO:0045924; P:regulation of female receptivity; IMP:FlyBase.
DR GO; GO:0045477; P:regulation of nurse cell apoptotic process; IMP:FlyBase.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:FlyBase.
DR CDD; cd17328; MFS_spinster_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044770; MFS_spinster-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23505; PTHR23505; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; Endosome;
KW Glycoprotein; Lipid transport; Lysosome; Membrane; Oogenesis;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..605
FT /note="Protein spinster"
FT /id="PRO_0000363955"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 365..605
FT /note="VAFNFGVITMLAGLLGVPLGSFLSQYLVKRYPTADPVICAFGLLVSAPLLTG
FT ACLLVNSNSVGTYALIFFGQLALNLNWAIVADILLYVVVPTRRSTAEAFQILISHALGD
FT AGSPYLVGAISEAIMKHLHKNPSDSGLTTELRSMSQVAGSAISNATQVIAEATTSLMET
FT ARSSASQEYSDVEQFEGLQYALFSTSFVEVLGGIFFIFTACFIIKDKYNATRGLQDATA
FT QQQQRDERGQIA -> MWWFPRDVQQPRPSKSSSHTHSVMPAVRIWLEQSPRPS (in
FT isoform E)"
FT /evidence="ECO:0000303|PubMed:11340170"
FT /id="VSP_036366"
FT VAR_SEQ 365..444
FT /note="VAFNFGVITMLAGLLGVPLGSFLSQYLVKRYPTADPVICAFGLLVSAPLLTG
FT ACLLVNSNSVGTYALIFFGQLALNLNWA -> ISYKFGLVAMLAGLIGVPLGSFLAQRL
FT RGRYENCDPYICAVGLFISAPMVFAALVVPQTSESLCFFFVFVAQVALNLCWS (in
FT isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:11340170, ECO:0000303|Ref.4"
FT /id="VSP_036367"
FT VAR_SEQ 590..605
FT /note="DATAQQQQRDERGQIA -> GDQGAQAVRSSVALASGQKDVESFNSDCLVLC
FT TDIALRERT (in isoform B and isoform D)"
FT /evidence="ECO:0000303|PubMed:11340170"
FT /id="VSP_036368"
FT MUTAGEN 217
FT /note="E->K: In bnch(N); leads to storage in yolk spheres
FT during oogenesis and results in widespread accumulation of
FT enlarged lysosomal and late endosomal inclusions."
FT /evidence="ECO:0000269|PubMed:15998804"
FT CONFLICT Q9GQQ0-5:389
FT /note="P -> Q (in Ref. 1; AAG43829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 65820 MW; D79951AEDE20F5C8 CRC64;
MSLKHQKQSY QPLPTAAAMD NPAMIQSSGS SGSSSSEEGG SREDVANLSP LGLPTTYSSQ
QLMPSDTDSM EEERHRLRPH HHHHHPLGEH HHIPGIPPSA VVPSRLSSVG RSQWFTVTVL
CFVNLINYMD RFTIAGVLTD VRNDFDIGND SAGLLQTVFV ISYMVCAPIF GYLGDRYSRP
WIMAVGVGLW STTTLLGSFM KQFGWFIAFR ALVGIGEASY STIAPTIISD LFVHDMRSKM
LALFYFAIPV GSGLGYIVGS KTAHLANDWR WALRVTPILG IVAVFLILLI KDPVRGHSEG
SHNLEATTYK QDIKALVRNR SFMLSTAGFT CVAFVAGALA WWGPSFIYLG MKMQPGNENI
VQDDVAFNFG VITMLAGLLG VPLGSFLSQY LVKRYPTADP VICAFGLLVS APLLTGACLL
VNSNSVGTYA LIFFGQLALN LNWAIVADIL LYVVVPTRRS TAEAFQILIS HALGDAGSPY
LVGAISEAIM KHLHKNPSDS GLTTELRSMS QVAGSAISNA TQVIAEATTS LMETARSSAS
QEYSDVEQFE GLQYALFSTS FVEVLGGIFF IFTACFIIKD KYNATRGLQD ATAQQQQRDE
RGQIA
