GALT3_DROME
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 03-AUG-2022, entry version 154.
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}.
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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 GlyGen; Q9Y117; 6 sites.
DR PaxDb; Q9Y117; -.
DR PRIDE; Q9Y117; -.
DR DNASU; 35627; -.
DR EnsemblMetazoa; FBtr0089061; FBpp0088130; FBgn0027558.
DR GeneID; 35627; -.
DR KEGG; dme:Dmel_CG4445; -.
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; 606683at2759; -.
DR PhylomeDB; Q9Y117; -.
DR BRENDA; 2.4.1.41; 1994.
DR Reactome; R-DME-190372; FGFR3c ligand binding and activation.
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 tissues.
DR Genevisible; Q9Y117; DM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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..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
