ID   GALT1_DROME             Reviewed;         601 AA.
AC   Q6WV20; Q0E964; Q9V7C8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1;
DE            Short=pp-GaNTase 1;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:12829714};
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 1;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1;
GN   Name=Pgant1 {ECO:0000303|PubMed:12829714,
GN   ECO:0000312|FlyBase:FBgn0034025};
GN   Synonyms=GalNAc-T1 {ECO:0000312|FlyBase:FBgn0034025};
GN   ORFNames=CG8182 {ECO:0000312|FlyBase:FBgn0034025};
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, 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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Farkas R., Medvedova L., Mechler B.M.;
RT   "Cloning of Drosophila protein-UDP acetylgalactosaminyltransferase.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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;
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   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).
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 the monoglycosylated Muc5AC-3 as
CC       substrate (PubMed:12829714). {ECO:0000269|PubMed:12829714}.
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 {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in developing oocytes and egg chambers.
CC       No expression observed during embryonic stages 9-11. During embryonic
CC       stages 12-13, specific expression is observed in the developing
CC       tracheal branches and brain. During embryonic stages 14-17, expression
CC       is restricted to the dorsal longitudinal trachea. In third instar
CC       larvae imaginal wing disk, expressed in clusters of cells in the
CC       presumptive pleura and notum. In eye-antennal imaginal disk, shows a
CC       very distinct band of expression at the morphogenetic furrow and weaker
CC       expression in the presumptive eye posterior to the furrow, no
CC       expression is detected in the presumptive antennal or head region
CC       anterior to the furrow. No expression observed in leg or haltere
CC       imaginal disks. {ECO:0000269|PubMed:12829714,
CC       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   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY268063; AAQ56699.1; -; mRNA.
DR   EMBL; AF218236; AAG13184.1; -; mRNA.
DR   EMBL; AE013599; AAM70974.1; -; Genomic_DNA.
DR   EMBL; AY113411; AAM29416.1; -; mRNA.
DR   RefSeq; NP_611043.1; NM_137199.3.
DR   RefSeq; NP_725472.1; NM_166099.2.
DR   AlphaFoldDB; Q6WV20; -.
DR   SMR; Q6WV20; -.
DR   BioGRID; 62452; 2.
DR   IntAct; Q6WV20; 1.
DR   STRING; 7227.FBpp0086464; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q6WV20; 1 site, No reported glycans.
DR   GlyGen; Q6WV20; 1 site.
DR   PaxDb; 7227-FBpp0086464; -.
DR   DNASU; 36717; -.
DR   EnsemblMetazoa; FBtr0087331; FBpp0086464; FBgn0034025.
DR   EnsemblMetazoa; FBtr0087332; FBpp0086465; FBgn0034025.
DR   GeneID; 36717; -.
DR   KEGG; dme:Dmel_CG8182; -.
DR   AGR; FB:FBgn0034025; -.
DR   CTD; 36717; -.
DR   FlyBase; FBgn0034025; Pgant1.
DR   VEuPathDB; VectorBase:FBgn0034025; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   InParanoid; Q6WV20; -.
DR   OMA; DLKFHPD; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q6WV20; -.
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   SignaLink; Q6WV20; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 36717; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36717; -.
DR   PRO; PR:Q6WV20; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0034025; Expressed in wing disc and 50 other cell types or tissues.
DR   ExpressionAtlas; Q6WV20; baseline and differential.
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: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; 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:SF43; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 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; Q6WV20; 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..601
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 1"
FT                   /id="PRO_0000059155"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..601
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          472..600
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          148..260
FT                   /note="Catalytic subdomain A"
FT   REGION          327..389
FT                   /note="Catalytic subdomain B"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..381
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        372..450
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        485..504
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        528..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        571..588
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   CONFLICT        146
FT                   /note="D -> E (in Ref. 1; AAQ56699)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   601 AA;  68961 MW;  81BAF81E04C35BC2 CRC64;
     MLPRFRSFYG KLIIFILVAL CFILYSKVQQ NGSPEEPPVA PLVRAAALRG HGRERFEAYS
     DSENEIARPA TQSPYEQIIQ LDLQKQKVGL GEQGVAVHLS GAAKERGDEI YKKIALNEEL
     SEQLTYNRSV GDHRNPLCAK QRFDSDSLPT ASVVIIFFNE PYSVLLRTVH STLSTCNEKA
     LKEIILVDDG SDNVELGAKL DYYVRTRIPS GKVTILRLKN RLGLIRARLA GARIATGDVL
     IFLDAHCEGN IGWCEPLLQR IKESRTSVLV PIIDVIDAND FQYSTNGYKS FQVGGFQWNG
     HFDWINLPER EKQRQRRECK QEREICPAYS PTMAGGLFAI DRRYFWEVGS YDEQMDGWGG
     ENLEMSFRIW QCGGTIETIP CSRVGHIFRD FHPYKFPNDR DTHGINTARM ALVWMDEYIN
     IFFLNRPDLK FHADIGDVTH RVMLRKKLRC KSFEWYLKNI YPEKFVPTKD VQGWGKVHAV
     NSNICLDDLL QNNEKPYNAG LYPCGKVLQK SQLFSFTNTN VLRNELSCAT VQHSESPPYR
     VVMVPCMEND EFNEQWRYEH QHIIHSNTGM CLDHQGLKSL DDAQVAPCDP HSESQRWTIE
     H
//