GALT7_DROME
ID GALT7_DROME Reviewed; 591 AA.
AC Q8MV48; A4V4R2; Q5U0W9; Q95RJ3; Q95TN2; Q9VWT6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=N-acetylgalactosaminyltransferase 7;
DE EC=2.4.1.41 {ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:12829714};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7;
DE Short=pp-GaNTase 7;
DE AltName: Full=dGalNAc-T2;
GN Name=Pgant7 {ECO:0000312|FlyBase:FBgn0030930};
GN Synonyms=GalNAc-T2 {ECO:0000312|FlyBase:FBgn0030930}; ORFNames=CG6394;
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], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11925450; DOI=10.1074/jbc.m202684200;
RA Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A.,
RA Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R.,
RA Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A.,
RA Clausen H.;
RT "Functional conservation of subfamilies of putative UDP-N-
RT acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in
RT Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of
RT l(2)35Aa is essential in Drosophila.";
RL J. Biol. Chem. 277:22623-22638(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=12829714; DOI=10.1074/jbc.m303836200;
RA Ten Hagen K.G., Tran D.T., Gerken T.A., Stein D.S., Zhang Z.;
RT "Functional characterization and expression analysis of members of the UDP-
RT GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila
RT melanogaster.";
RL J. Biol. Chem. 278:35039-35048(2003).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-591.
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 [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16251381; DOI=10.1093/glycob/cwj051;
RA Tian E., Ten Hagen K.G.;
RT "Expression of the UDP-GalNAc: polypeptide N-
RT acetylgalactosaminyltransferase family is spatially and temporally
RT regulated during Drosophila development.";
RL Glycobiology 16:83-95(2006).
RN [8]
RP FUNCTION.
RX PubMed=20807760; DOI=10.1074/jbc.m110.133561;
RA Zhang L., Ten Hagen K.G.;
RT "Dissecting the biological role of mucin-type O-glycosylation using RNA
RT interference in Drosophila cell culture.";
RL J. Biol. Chem. 285:34477-34484(2010).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=22157008; DOI=10.1074/jbc.m111.306159;
RA Tran D.T., Zhang L., Zhang Y., Tian E., Earl L.A., Ten Hagen K.G.;
RT "Multiple members of the UDP-GalNAc: polypeptide N-
RT acetylgalactosaminyltransferase family are essential for viability in
RT Drosophila.";
RL J. Biol. Chem. 287:5243-5252(2012).
CC -!- FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide
CC biosynthesis, which catalyzes the transfer of an N-acetyl-D-
CC galactosamine residue to an already glycosylated peptide
CC (PubMed:11925450, PubMed:12829714). In contrast to other proteins of
CC the family, it does not act as a peptide transferase that transfers
CC GalNAc onto serine or threonine residue on the protein receptor, but
CC instead requires the prior addition of a GalNAc on a peptide before
CC adding additional GalNAc moieties (PubMed:11925450). Some peptide
CC transferase activity is however not excluded, considering that its
CC appropriate peptide substrate may remain unidentified. Prefers the
CC monoglycosylated Muc5AC-3 as substrate (PubMed:11925450). Might have a
CC role in protein O-glycosylation in the Golgi and thereby in
CC establishing and/or maintaining a proper secretory apparatus structure
CC (PubMed:20807760). {ECO:0000269|PubMed:11925450,
CC ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:20807760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:12829714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:12829714};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:11925450, ECO:0000305|PubMed:12829714}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in developing oocytes and egg chambers.
CC During embryonic stages 9-11, expressed in the primordium of the
CC foregut, midgut and hindgut. Expressed in the salivary glands from
CC embryonic stage 12 onwards. During embryonic stages 12-13, expressed in
CC the posterior midgut and hindgut. During embryonic stages 14-15,
CC expression continues in the hindgut. During embryonic stages 16-17,
CC expressed in the antennomaxillary complex. In third instar larvae,
CC ubiquitously expressed in wing, with increased expression in the notum
CC and ventral wing pouch, eye-antennal, leg and haltere imaginal disks.
CC {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:16251381}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout embryonic, larval, pupal and adult stages, with
CC increasing levels during larval development.
CC {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:16251381}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the whole body or
CC respiratory system during development is lethal (PubMed:22157008).
CC RNAi-mediated knockdown in hemocytes, amnioserosa, mesoderm or
CC digestive system and reproductive tract causes no defect
CC (PubMed:22157008). {ECO:0000269|PubMed:22157008}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13889.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL28887.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF493067; AAM62412.1; -; mRNA.
DR EMBL; AY268068; AAQ56704.1; -; mRNA.
DR EMBL; AE014298; AAF48851.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09470.1; -; Genomic_DNA.
DR EMBL; BT016123; AAV37008.1; -; mRNA.
DR EMBL; AY058660; AAL13889.1; ALT_INIT; mRNA.
DR EMBL; AY061339; AAL28887.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285406.1; NM_001298477.1.
DR RefSeq; NP_573301.2; NM_133073.3.
DR RefSeq; NP_728178.1; NM_167623.2.
DR AlphaFoldDB; Q8MV48; -.
DR SMR; Q8MV48; -.
DR BioGRID; 59149; 4.
DR IntAct; Q8MV48; 4.
DR STRING; 7227.FBpp0074396; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8MV48; 2 sites.
DR SwissPalm; Q8MV48; -.
DR PaxDb; Q8MV48; -.
DR PRIDE; Q8MV48; -.
DR DNASU; 32836; -.
DR EnsemblMetazoa; FBtr0074624; FBpp0074395; FBgn0030930.
DR EnsemblMetazoa; FBtr0074625; FBpp0074396; FBgn0030930.
DR EnsemblMetazoa; FBtr0346082; FBpp0311917; FBgn0030930.
DR GeneID; 32836; -.
DR KEGG; dme:Dmel_CG6394; -.
DR UCSC; CG6394-RB; d. melanogaster.
DR CTD; 32836; -.
DR FlyBase; FBgn0030930; Pgant7.
DR VEuPathDB; VectorBase:FBgn0030930; -.
DR eggNOG; KOG3737; Eukaryota.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8MV48; -.
DR OMA; FDDTHKE; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8MV48; -.
DR BRENDA; 2.4.1.41; 1994.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 32836; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32836; -.
DR PRO; PR:Q8MV48; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030930; Expressed in hindgut proper primordium (Drosophila) and 45 other tissues.
DR ExpressionAtlas; Q8MV48; baseline and differential.
DR Genevisible; Q8MV48; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; NAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..591
FT /note="N-acetylgalactosaminyltransferase 7"
FT /id="PRO_0000059161"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..591
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 466..585
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 68..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..251
FT /note="Catalytic subdomain A"
FT REGION 313..375
FT /note="Catalytic subdomain B"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 358..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 479..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 519..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 558..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 84
FT /note="P -> S (in Ref. 1; AAM62412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 68333 MW; 6CC2F7DC38E4CF17 CRC64;
MRVSTIRSGR ICRLALCLLV LLPLLYLLAN WSDHHKRVQE AYHTRFGGPK FAHQRLEGRP
REVPKLVDGL GNFEPKDVKP RSGPGENGEA HSLSPDKKHM SDASEMEYGM NIACSDEISM
HRSVRDTRLE ECRHWDYPFD LPRTSVIIVF HNEGFSVLMR TVHSVIDRSP THMLHEIILV
DDFSDKENLR SQLDEYVLQF KGLVKVIRNK EREGLIRTRS RGAMEATGEV IVFLDAHCEV
NTNWLPPLLA PIYRDRTVMT VPIIDGIDHK NFEYRPVYGT DNHFRGIFEW GMLYKENEVP
RREQRRRAHN SEPYRSPTHA GGLFAINREY FLELGAYDPG LLVWGGENFE LSFKIWQCGG
SIEWVPCSRV GHVYRGFMPY NFGKLASKKK GPLITINYKR VIETWFDDTH KEYFYTREPL
ARYLDMGDIS EQLALKKRLN CKSFQWFMDH IAYDVYDKFP GLPANLHWGE LRSVASDGCL
DSMGHQPPAI MGLTYCHGGG NNQLVRLNAA GQLGVGERCV EADRQGIKLA VCRLGTVDGP
WQYNEHTKHL MHRVHKKCMA LHPATQQLSL GHCDVNDSYQ QWWFKEIRPR W
