ID GALT3_DROME Reviewed; 667 AA. AC Q9Y117; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3; DE Short=pp-GaNTase 3; DE EC=2.4.1.41 {ECO:0000269|PubMed:12829714}; DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 3; DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3; GN Name=Pgant3 {ECO:0000312|FlyBase:FBgn0027558}; GN ORFNames=CG4445 {ECO:0000312|FlyBase:FBgn0027558}; 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 [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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. 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 [5] 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 [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=18835818; DOI=10.1074/jbc.m804267200; RA Zhang L., Zhang Y., Hagen K.G.; RT "A mucin-type O-glycosyltransferase modulates cell adhesion during RT Drosophila development."; RL J. Biol. Chem. 283:34076-34086(2008). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP ARG-130. RX PubMed=20371600; DOI=10.1074/jbc.m109.098145; RA Zhang L., Tran D.T., Ten Hagen K.G.; RT "An O-glycosyltransferase promotes cell adhesion during development by RT influencing secretion of an extracellular matrix integrin ligand."; RL J. Biol. Chem. 285:19491-19501(2010). 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 FUNCTION, AND 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). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=25253852; DOI=10.1523/jneurosci.1484-14.2014; RA Dani N., Zhu H., Broadie K.; RT "Two protein N-acetylgalactosaminyl transferases regulate synaptic RT plasticity by activity-dependent regulation of integrin signaling."; RL J. Neurosci. 34:13047-13065(2014). CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a CC serine or threonine residue on the protein receptor (PubMed:12829714). CC It can both act as a peptide transferase that transfers GalNAc onto CC unmodified peptide substrates, and as a glycopeptide transferase that CC requires the prior addition of a GalNAc on a peptide before adding CC additional GalNAc moieties. Prefers EA2 as substrate. Has weak activity CC toward Muc5AC-3, -13 and -3/13 substrates (PubMed:12829714). Plays a CC critical role in the regulation of integrin-mediated cell adhesion CC during wing development by influencing, via glycosylation, the CC secretion and localization of the integrin ligand Tig to the basal cell CC layer interface (PubMed:18835818, PubMed:20371600, PubMed:20807760, CC PubMed:22157008). Might have a role in protein O-glycosylation in the CC Golgi and thereby in establishing and/or maintaining a proper secretory CC apparatus structure (PubMed:20807760). Together with Pgant35A, CC regulates integrin levels and activity-dependent integrin signaling at CC the synapse in neurons and muscles (PubMed:25253852). CC {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:18835818, CC ECO:0000269|PubMed:20371600, ECO:0000269|PubMed:20807760, CC ECO:0000269|PubMed:22157008, ECO:0000269|PubMed:25253852}. 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: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:12829714}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000305|PubMed:12829714}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:20371600}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:20371600}. CC -!- TISSUE SPECIFICITY: Expressed in developing oocytes and egg chambers. CC During embryonic stages 9-11, expressed in the primordiums of the CC foregut, midgut and hindgut. During embryonic stages 12-13, expression CC is found uniquely in the posterior spiracle. During embryonic stages CC 14-17, expressed in the pharynx, esophagus and posterior spiracles. CC Expression observed in the epidermis during embryonic stages 16-17. In CC third instar larvae, expressed ubiquitously in wing, with increased CC expression in pleura and notum, eye-antennal, leg and haltere imaginal CC disks. {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. 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: Mutant larval wing disks show a decrease in CC thickness and in the content of O-glycoproteins specifically along the CC basal surface of the columnar epithelial cells (PubMed:18835818, CC PubMed:20371600). Adult mutants display blistered wings CC (PubMed:18835818, PubMed:20371600). Mutant larval shows down-regulation CC of synaptic O-linked glycosylation, integrin level and signaling via CC Ten-m and if. Synapses show smaller synaptic boutons, expanded CC activity-dependent postsynaptic pockets which affect synaptic CC plasticity and synaptic strength in both the pre-synaptic and post- CC synaptic assembly, no differences in neuromuscular junction morphology CC (PubMed:25253852). Simultaneous knockout of Pgant35A, restores normal CC synaptic strength (PubMed:25253852). RNAi-mediated knockdown in the CC developing wing results in a blistered phenotype (PubMed:22157008). CC {ECO:0000269|PubMed:18835818, ECO:0000269|PubMed:20371600, CC ECO:0000269|PubMed:22157008, ECO:0000269|PubMed:25253852}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T CC subfamily. {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; AE013599; AAF59298.1; -; Genomic_DNA. DR EMBL; AF145655; AAD38630.1; -; mRNA. DR RefSeq; NP_610256.1; NM_136412.4. DR AlphaFoldDB; Q9Y117; -. DR SMR; Q9Y117; -. DR BioGRID; 61516; 8. DR IntAct; Q9Y117; 2. DR STRING; 7227.FBpp0088130; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GT27; Glycosyltransferase Family 27. DR GlyCosmos; Q9Y117; 6 sites, No reported glycans. DR GlyGen; Q9Y117; 6 sites. DR PaxDb; 7227-FBpp0088130; -. DR DNASU; 35627; -. DR EnsemblMetazoa; FBtr0089061; FBpp0088130; FBgn0027558. DR GeneID; 35627; -. DR KEGG; dme:Dmel_CG4445; -. DR AGR; FB:FBgn0027558; -. DR CTD; 35627; -. DR FlyBase; FBgn0027558; Pgant3. DR VEuPathDB; VectorBase:FBgn0027558; -. DR eggNOG; KOG3736; Eukaryota. DR HOGENOM; CLU_013477_0_1_1; -. DR InParanoid; Q9Y117; -. DR OMA; LWTYDMD; -. DR OrthoDB; 202750at2759; -. DR PhylomeDB; Q9Y117; -. DR BRENDA; 2.4.1.41; 1994. DR Reactome; R-DME-913709; O-linked glycosylation of mucins. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 35627; 0 hits in 1 CRISPR screen. DR ChiTaRS; pgant3; fly. DR GenomeRNAi; 35627; -. DR PRO; PR:Q9Y117; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0027558; Expressed in seminal fluid secreting gland and 36 other cell types or tissues. DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005795; C:Golgi stack; NAS:UniProtKB. DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:FlyBase. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0016757; F:glycosyltransferase activity; IDA:FlyBase. 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:0031589; P:cell-substrate adhesion; IMP:FlyBase. DR GO; GO:0070278; P:extracellular matrix constituent secretion; IMP:FlyBase. DR GO; GO:0016266; P:O-glycan processing; IDA:FlyBase. DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:FlyBase. DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IMP:FlyBase. DR CDD; cd02510; pp-GalNAc-T; 1. DR CDD; cd00161; RICIN; 1. DR Gene3D; 2.80.10.50; -; 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 PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR11675:SF101; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. DR Genevisible; Q9Y117; DM. 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..667 FT /note="Polypeptide N-acetylgalactosaminyltransferase 3" FT /id="PRO_0000059157" FT TOPO_DOM 1..12 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 13..35 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 36..667 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 513..661 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT REGION 149..259 FT /note="Catalytic subdomain A" FT REGION 321..383 FT /note="Catalytic subdomain B" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 220 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 243 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 352 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 380 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 383 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 388 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 75 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 129 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 279 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 313 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 590 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 140..375 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 366..446 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 526..547 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 572..601 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 626..649 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT MUTAGEN 130 FT /note="R->C: Does not affect subcellular location. Loss of FT catalytic activity." FT /evidence="ECO:0000269|PubMed:20371600" SQ SEQUENCE 667 AA; 76807 MW; B8C6924AA8E19805 CRC64; MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP PKRRSLWPHK NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV VPPRDRFRMQ RFFRLNSFNL LASDRIPLNR TLKDYRTPEC RDKKYASGLP STSVIIVFHN EAWSVLLRTI TSVINRSPRH LLKEIILVDD ASDRSYLKRQ LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT FLDAHCECSR GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR VWGGENVEMS FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD NLARAATVWM DDWQYFIMLY TSGLTLGAKD KVNVTERVAL RERLQCKPFS WYLENIWPEH FFPAPDRFFG KIIWLDGETE CAQAYSKHMK NLPGRALSRE WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS AVTVGDCTSH AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD FKDITQKWGF IPLPWRM //