BROWN_DROME
ID BROWN_DROME Reviewed; 675 AA.
AC P12428; Q24264; Q7KVI1; Q7KVI2; Q8MRN9; Q9W1N7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein brown;
DE EC=7.6.2.- {ECO:0000305|PubMed:33820991};
DE EC=7.6.2.6 {ECO:0000305|PubMed:117796};
DE AltName: Full=ATP-binding cassette transporter sub-family G member brown {ECO:0000305};
DE AltName: Full=Broad substrate specificity ATP-binding cassette transporter brown {ECO:0000305};
GN Name=bw {ECO:0000312|FlyBase:FBgn0000241};
GN ORFNames=CG17632 {ECO:0000312|FlyBase:FBgn0000241};
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].
RX PubMed=3149712; DOI=10.1128/mcb.8.12.5206-5215.1988;
RA Dreesen T.D., Johnson D.H., Henikoff S.;
RT "The brown protein of Drosophila melanogaster is similar to the white
RT protein and to components of active transport complexes.";
RL Mol. Cell. Biol. 8:5206-5215(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7956072; DOI=10.1101/sqb.1993.058.01.064;
RA Martin-Morris L.E., Loughney K., Kershisnik E.O., Poortinga G.,
RA Henikoff S.;
RT "Characterization of sequences responsible for trans-inactivation of the
RT Drosophila brown gene.";
RL Cold Spring Harb. Symp. Quant. Biol. 58:577-584(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IG281;
RX PubMed=7753025; DOI=10.1007/bf00705646;
RA Nitasaka E., Yamazaki T., Green M.M.;
RT "The molecular analysis of brown eye color mutations isolated from
RT geographically discrete populations of Drosophila melanogaster.";
RL Mol. Gen. Genet. 247:164-168(1995).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316.
RC STRAIN=Berkeley; TISSUE=Head;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=117796; DOI=10.1007/bf00498891;
RA Sullivan D.T., Bell L.A., Paton D.R., Sullivan M.C.;
RT "Purine transport by malpighian tubules of pteridine-deficient eye color
RT mutants of Drosophila melanogaster.";
RL Biochem. Genet. 17:565-573(1979).
RN [8]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-578 AND ASN-638.
RX PubMed=8144619; DOI=10.1016/s0021-9258(17)34070-x;
RA Ewart G.D., Cannell D., Cox G.B., Howells A.J.;
RT "Mutational analysis of the traffic ATPase (ABC) transporters involved in
RT uptake of eye pigment precursors in Drosophila melanogaster. Implications
RT for structure-function relationships.";
RL J. Biol. Chem. 269:10370-10377(1994).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10407069; DOI=10.1016/s0005-2736(99)00064-4;
RA Mackenzie S.M., Brooker M.R., Gill T.R., Cox G.B., Howells A.J.,
RA Ewart G.D.;
RT "Mutations in the white gene of Drosophila melanogaster affecting ABC
RT transporters that determine eye colouration.";
RL Biochim. Biophys. Acta 1419:173-185(1999).
RN [10]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=18931318; DOI=10.1242/jeb.021162;
RA Borycz J., Borycz J.A., Kubow A., Lloyd V., Meinertzhagen I.A.;
RT "Drosophila ABC transporter mutants white, brown and scarlet have altered
RT contents and distribution of biogenic amines in the brain.";
RL J. Exp. Biol. 211:3454-3466(2008).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33820991; DOI=10.1038/s42255-021-00375-x;
RA Sasaki A., Nishimura T., Takano T., Naito S., Yoo S.K.;
RT "white regulates proliferative homeostasis of intestinal stem cells during
RT ageing in Drosophila.";
RL Nat. Metab. 3:546-557(2021).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family which transports various molecules including bioamines,
CC neurotransmitters and metabolic intermediates (PubMed:117796,
CC PubMed:8144619, PubMed:10407069, PubMed:18931318, PubMed:33820991). In
CC the eye and probably in association with w/white, required for the
CC transport of the eye red pigment precursor, guanine, into pigment cell
CC granules (PubMed:8144619, PubMed:117796). In Malpighian tubules,
CC involved in guanine uptake (PubMed:117796). Probably in association
CC with w/white, involved in aging-induced intestinal stem cell
CC proliferation in the midgut by regulating tetrahydrofolate transport
CC (PubMed:33820991). {ECO:0000269|PubMed:10407069,
CC ECO:0000269|PubMed:117796, ECO:0000269|PubMed:18931318,
CC ECO:0000269|PubMed:33820991, ECO:0000269|PubMed:8144619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + guanine(out) + H2O = ADP + guanine(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:20832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16235, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.6;
CC Evidence={ECO:0000305|PubMed:117796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate +
CC riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57986, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:33820991};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate(out) + ATP + H2O = (6S)-5,6,7,8-
CC tetrahydrofolate(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:68592,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:33820991};
CC -!- SUBUNIT: May form a heterodimer with w/white.
CC {ECO:0000305|PubMed:18931318, ECO:0000305|PubMed:8144619}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated during aging in intestinal stem cells.
CC {ECO:0000269|PubMed:33820991}.
CC -!- DISRUPTION PHENOTYPE: Eyes are brown due to a defect in red pigment
CC production (PubMed:10407069). In Malpighian tubules, guanine uptake is
CC impaired (PubMed:117796). Reduces the levels of several metabolites,
CC including kynurenine, kynurenic acid, 3-hydroxykynurenine, guanosine,
CC xanthine, urate, riboflavin, and tetrahydrofolate, and increases the
CC levels of guanine (PubMed:33820991). In the head, levels of
CC neurotransmitters histamine, dopamine and serotonin are reduced;
CC specifically, histamine is reduced in the retina (PubMed:18931318).
CC Severe loss of white protein in the retina lamina and photoreceptors
CC (PubMed:18931318). In addition, in lamina photoreceptor terminals R1-
CC R6, number of synaptic vesicles is reduced (PubMed:18931318). Inhibits
CC aging-induced intestinal stem cell proliferation (PubMed:33820991).
CC {ECO:0000269|PubMed:10407069, ECO:0000269|PubMed:117796,
CC ECO:0000269|PubMed:18931318, ECO:0000269|PubMed:33820991}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50157.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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; M20630; AAA28397.1; -; mRNA.
DR EMBL; L23543; AAC37214.1; -; Genomic_DNA.
DR EMBL; L05635; AAA28398.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47020.3; -; Genomic_DNA.
DR EMBL; AY119503; AAM50157.1; ALT_SEQ; mRNA.
DR PIR; A31399; FYFFB.
DR RefSeq; NP_001286769.1; NM_001299840.1.
DR RefSeq; NP_523824.1; NM_079100.3.
DR AlphaFoldDB; P12428; -.
DR SMR; P12428; -.
DR BioGRID; 63324; 38.
DR DIP; DIP-387N; -.
DR IntAct; P12428; 1.
DR STRING; 7227.FBpp0072026; -.
DR TCDB; 3.A.1.204.18; the atp-binding cassette (abc) superfamily.
DR PaxDb; P12428; -.
DR PRIDE; P12428; -.
DR DNASU; 37724; -.
DR EnsemblMetazoa; FBtr0072117; FBpp0072026; FBgn0000241.
DR EnsemblMetazoa; FBtr0346612; FBpp0312192; FBgn0000241.
DR GeneID; 37724; -.
DR KEGG; dme:Dmel_CG17632; -.
DR CTD; 37724; -.
DR FlyBase; FBgn0000241; bw.
DR VEuPathDB; VectorBase:FBgn0000241; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_406887_0_0_1; -.
DR InParanoid; P12428; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; P12428; -.
DR BioGRID-ORCS; 37724; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37724; -.
DR PRO; PR:P12428; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000241; Expressed in seminal fluid secreting gland and 18 other tissues.
DR ExpressionAtlas; P12428; baseline and differential.
DR Genevisible; P12428; DM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IMP:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:FlyBase.
DR GO; GO:0015208; F:guanine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IMP:FlyBase.
DR GO; GO:0006856; P:eye pigment precursor transport; TAS:FlyBase.
DR GO; GO:0015854; P:guanine transport; IMP:UniProtKB.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005284; Pigment_permease/Abcg.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00955; 3a01204; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Pigment; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..675
FT /note="Protein brown"
FT /id="PRO_0000093375"
FT TOPO_DOM 1..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..460
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..531
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..644
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 34..261
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 229..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 578
FT /note="G->D: In T50; normal eye color. Eyes are brown due
FT to a reduction in red pigment production in a w/white co2
FT mutant background."
FT /evidence="ECO:0000269|PubMed:8144619"
FT MUTAGEN 638
FT /note="N->T: In 6; normal eye color. Eyes are brown due to
FT a reduction in red pigment production in a w/white co2
FT mutant background."
FT /evidence="ECO:0000269|PubMed:8144619"
FT CONFLICT 28
FT /note="D -> A (in Ref. 2; AAC37214, 3; AAA28398 and 6;
FT AAM50157)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="R -> P (in Ref. 3; AAA28398)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="L -> I (in Ref. 2; AAC37214 and 3; AAA28398)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="E -> Q (in Ref. 2; AAC37214)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="R -> P (in Ref. 2; AAC37214)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="N -> T (in Ref. 2; AAC37214 and 3; AAA28398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 75943 MW; 81DEBDF856F4F174 CRC64;
MQESGGSSGQ GGPSLCLEWK QLNYYVPDQE QSNYSFWNEC RKKRELRILQ DASGHMKTGD
LIAILGGSGA GKTTLLAAIS QRLRGNLTGD VVLNGMAMER HQMTRISSFL PQFEINVKTF
TAYEHLYFMS HFKMHRRTTK AEKRQRVADL LLAVGLRDAA HTRIQQLSGG ERKRLSLAEE
LITDPIFLFC DEPTTGLDSF SAYSVIKTLR HLCTRRRIAK HSLNQVYGED SFETPSGESS
ASGSGSKSIE MEVVAESHES LLQTMRELPA LGVLSNSPNG THKKAAICSI HQPTSDIFEL
FTHIILMDGG RIVYQGRTEQ AAKFFTDLGY ELPLNCNPAD FYLKTLADKE GKENAGAVLR
AKYEHETDGL YSGSWLLARS YSGDYLKHVQ NFKKIRWIYQ VYLLMVRFMT EDLRNIRSGL
IAFGFFMITA VTLSLMYSGI GGLTQRTVQD VGGSIFMLSN EMIFTFSYGV TYIFPAALPI
IRREVGEGTY SLSAYYVALV LSFVPVAFFK GYVFLSVIYA SIYYTRGFLL YLSMGFLMSL
SAVAAVGYGV FLSSLFESDK MASECAAPFD LIFLIFGGTY MNVDTVPGLK YLSLFFYSNE
ALMYKFWIDI DNIDCPVNED HPCIKTGVEV LQQGSYRNAD YTYWLDCFSL VVVAVIFHIV
SFGLVRRYIH RSGYY
