GALT6_DROME
ID GALT6_DROME Reviewed; 666 AA.
AC Q6WV16; Q0E8I9; Q95R40; Q9VZX5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=N-acetylgalactosaminyltransferase 6;
DE EC=2.4.1.41 {ECO:0000269|PubMed:12829714};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
DE Short=pp-GaNTase 6;
GN Name=Pgant6 {ECO:0000312|FlyBase:FBgn0035375};
GN ORFNames=CG2103 {ECO:0000312|FlyBase:FBgn0035375};
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 [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 [3]
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 [4]
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 [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.
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 [7]
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:12829714). In contrast to other proteins of the family, it does
CC not act as a peptide transferase that transfers GalNAc onto serine or
CC threonine residue on the protein receptor, but instead requires the
CC prior addition of a GalNAc on a peptide before adding additional GalNAc
CC moieties (PubMed:12829714). Some peptide transferase activity is
CC however not excluded, considering that its appropriate peptide
CC substrate may remain unidentified (PubMed:12829714). Prefers the
CC diglycosylated Muc5AC-3/13 as substrate (PubMed:12829714). 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:12829714,
CC 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: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 during oogenesis, in the somatically
CC derived follicle cells that surround the developing oocyte, which are
CC involved in the maturation of the oocyte and construction of the egg
CC shell, as well as playing a role in subsequent embryonic pattern
CC formation. Expressed in the salivary glands from embryonic stage 12
CC onwards, becoming stronger at stage 13. During embryonic stages 12-13,
CC also expressed in the posterior midgut and hindgut. During embryonic
CC stages 14-15, expression continues in the hindgut. Expression is
CC detected in the epidermis and antennomaxillary complex during embryonic
CC stages 16-17. In third instar larvae, ubiquitously expressed in wing,
CC eye-antennal, leg and haltere imaginal disks.
CC {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:16251381}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic, larval, pupal and
CC adult stages, with increasing levels during larval development.
CC Transcripts first detected during embryonic stages 12-13.
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 reduces viability.
CC {ECO:0000269|PubMed:22157008}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
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DR EMBL; AY268067; AAQ56703.1; -; mRNA.
DR EMBL; AE014296; AAF47689.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47690.1; -; Genomic_DNA.
DR EMBL; AY061629; AAL29177.1; -; mRNA.
DR RefSeq; NP_001261342.1; NM_001274413.1.
DR RefSeq; NP_647749.2; NM_139492.3.
DR RefSeq; NP_728779.1; NM_167966.2.
DR AlphaFoldDB; Q6WV16; -.
DR SMR; Q6WV16; -.
DR BioGRID; 63848; 4.
DR STRING; 7227.FBpp0072842; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q6WV16; 4 sites.
DR PaxDb; Q6WV16; -.
DR PRIDE; Q6WV16; -.
DR EnsemblMetazoa; FBtr0072972; FBpp0072842; FBgn0035375.
DR EnsemblMetazoa; FBtr0072973; FBpp0072843; FBgn0035375.
DR EnsemblMetazoa; FBtr0333442; FBpp0305633; FBgn0035375.
DR GeneID; 38346; -.
DR KEGG; dme:Dmel_CG2103; -.
DR CTD; 38346; -.
DR FlyBase; FBgn0035375; Pgant6.
DR VEuPathDB; VectorBase:FBgn0035375; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000166027; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q6WV16; -.
DR OMA; DHSNFNY; -.
DR OrthoDB; 276134at2759; -.
DR PhylomeDB; Q6WV16; -.
DR BRENDA; 2.4.1.41; 1994.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 38346; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38346; -.
DR PRO; PR:Q6WV16; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035375; Expressed in thoracico-abdominal ganglion (Drosophila) and 37 other tissues.
DR ExpressionAtlas; Q6WV16; baseline and differential.
DR Genevisible; Q6WV16; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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..666
FT /note="N-acetylgalactosaminyltransferase 6"
FT /id="PRO_0000059160"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..666
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 518..648
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 90..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..311
FT /note="Catalytic subdomain A"
FT REGION 367..429
FT /note="Catalytic subdomain B"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 192..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 412..491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 531..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 577..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 621..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 95..96
FT /note="EV -> DA (in Ref. 1; AAQ56703)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="Q -> R (in Ref. 1; AAQ56703 and 4; AAL29177)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="E -> K (in Ref. 4; AAL29177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 76972 MW; CAECA6CE4860600C CRC64;
MRRPNLKWIV KASLLLLISL TLFVLITSWI SSTPYTNKPV HHGVEPVPEK AGLSGDVKVK
VPAIKQPEPQ KPQEPDFEED PELQKIDEPE PVEEEVDNPH PADDEPQQQP QEELQMAAPA
DASVKKDWHD YTFMEKDAKR VGLGEGGKAS TLDDESQRDL EKRMSLENGF NALLSDSISV
NRSVPDIRHP LCRKKEYVAK LPTVSVIIIF YNEYLSVLMR SVHSLINRSP PELMKEIILV
DDHSDREYLG KELETYIAEH FKWVRVVRLP RRTGLIGARA AGARNATAEV LIFLDSHVEA
NYNWLPPLLE PIALNKRTAV CPFIDVIDHT NFHYRAQDEG ARGAFDWEFF YKRLPLLPED
LKHPADPFKS PIMAGGLFAI SREFFWELGG YDEGLDIWGG EQYELSFKIW MCGGEMYDAP
CSRIGHIYRG PRNHQPSPRK GDYLHKNYKR VAEVWMDEYK NYLYSHGDGL YESVDPGDLT
EQKAIRTKLN CKSFKWFMEE VAFDLMKTYP PVDPPSYAMG ALQNVGNQNL CLDTLGRKKH
NKMGMYACAD NIKTPQRTQF WELSWKRDLR LRRKKECLDV QIWDANAPVW LWDCHSQGGN
QYWYYDYRHK QLKHGTEGRR CLELLPFSQE VVANKCDTDN RFQQWNFGSF NKTALDNYSQ
DLVLSL
