GALT2_DROME
ID GALT2_DROME Reviewed; 633 AA.
AC Q6WV19; Q7KU27; Q7YU21; Q9VQQ2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2;
DE Short=pp-GaNTase 2;
DE EC=2.4.1.41 {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:18669915};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 2;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2;
GN Name=Pgant2 {ECO:0000303|PubMed:12829714, ECO:0000312|FlyBase:FBgn0031530};
GN ORFNames=CG3254 {ECO:0000312|FlyBase:FBgn0031530};
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=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-633, FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, TISSUE 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 [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, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18669915; DOI=10.1093/glycob/cwn073;
RA Gerken T.A., Ten Hagen K.G., Jamison O.;
RT "Conservation of peptide acceptor preferences between Drosophila and
RT mammalian polypeptide-GalNAc transferase ortholog pairs.";
RL Glycobiology 18:861-870(2008).
RN [7]
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 [8]
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: 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 PubMed:18669915). It can both act as a peptide transferase that
CC transfers GalNAc onto unmodified peptide substrates, and as a
CC glycopeptide transferase that requires the prior addition of a GalNAc
CC on a peptide before adding additional GalNAc moieties. Prefers the
CC monoglycosylated Muc5AC-3 as substrate (PubMed:12829714). O-
CC glycosylation modification of proteins by this enzyme might be
CC important for cytokinesis (PubMed:20807760).
CC {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:18669915,
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, ECO:0000269|PubMed:18669915};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:12829714, ECO:0000305|PubMed:18669915}.
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 during embryonic, larval, pupal and adult stages. Weakly
CC expressed in the male and female body and correspondingly low levels
CC during early embryonic stages. Significantly expressed from embryonic
CC stage 8-12 hours and reaches maximal levels in the pupae and male head.
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 is viable.
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; AE014134; AAF51113.3; -; Genomic_DNA.
DR EMBL; BT010030; AAQ22499.1; -; mRNA.
DR EMBL; AY268064; AAQ56700.1; -; mRNA.
DR RefSeq; NP_608773.2; NM_134929.4.
DR RefSeq; NP_995625.2; NM_205903.3.
DR AlphaFoldDB; Q6WV19; -.
DR SMR; Q6WV19; -.
DR STRING; 7227.FBpp0292961; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR PaxDb; Q6WV19; -.
DR PRIDE; Q6WV19; -.
DR EnsemblMetazoa; FBtr0077592; FBpp0099799; FBgn0031530.
DR EnsemblMetazoa; FBtr0303992; FBpp0292961; FBgn0031530.
DR GeneID; 33556; -.
DR KEGG; dme:Dmel_CG3254; -.
DR CTD; 33556; -.
DR FlyBase; FBgn0031530; Pgant2.
DR VEuPathDB; VectorBase:FBgn0031530; -.
DR eggNOG; KOG3738; Eukaryota.
DR GeneTree; ENSGT00940000156958; -.
DR HOGENOM; CLU_013477_0_2_1; -.
DR InParanoid; Q6WV19; -.
DR OMA; QEWAFSK; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q6WV19; -.
DR BRENDA; 2.4.1.41; 1994.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 33556; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33556; -.
DR PRO; PR:Q6WV19; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031530; Expressed in adult clypeo-labral primordium and 31 other tissues.
DR Genevisible; Q6WV19; DM.
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 GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA: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; Glycosyltransferase; Golgi apparatus; Lectin; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..633
FT /note="Polypeptide N-acetylgalactosaminyltransferase 2"
FT /id="PRO_0000059156"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..633
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 508..630
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..306
FT /note="Catalytic subdomain A"
FT REGION 366..428
FT /note="Catalytic subdomain B"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 192..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 411..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 521..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 561..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 602..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 134
FT /note="P -> L (in Ref. 4; AAQ56700)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="H -> R (in Ref. 3; AAQ22499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 70736 MW; 8DA64F627BCB08DB CRC64;
MRRNIKLIVF VSIIWMFVMV YYFQSSTEKV ENRALRLREV ATAMQQYQDD SSSAAAASTA
RQWAPAGGGA GPGAAAGAAG SGADDPGGNV ILIGSVKDFE RNAVHGLKLN GIVALEETSQ
GLSGGTGGPG GRLPVAPSGR GTEVEYFNEA GYIRAGALRN GEDPYIRNRF NQEASDALPS
NRDIPDTRNP MCRTKKYRED LPETSVIITF HNEARSTLLR TIVSVLNRSP EHLIREIVLV
DDYSDHPEDG LELAKIDKVR VIRNDKREGL VRSRVKGADA AVSSVLTFLD SHVECNEMWL
EPLLERVRED PTRVVCPVID VISMDNFQYI GASADLRGGF DWNLIFKWEY LSPSERAMRH
NDPTTAIRTP MIAGGLFVID KAYFNKLGKY DMKMDVWGGE NLEISFRVWQ CGGSLEIIPC
SRVGHVFRKR HPYTFPGGSG NVFARNTRRA AEVWMDDYKQ HYYNAVPLAK NIPFGNIDDR
LALKEKLHCK PFKWYLENVY PDLQAPDPQE VGQFRQDSTE CLDTMGHLID GTVGIFPCHN
TGGNQEWAFT KRGEIKHDDL CLTLVTFARG SQVVLKACDD SENQRWIMRE GGLVRHYKIN
VCLDSRDQSQ QGVSAQHCNS ALGTQRWSFG KYA
