ID   GALT8_DROME             Reviewed;         590 AA.
AC   Q9VUT6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 8;
DE            Short=pp-GaNTase 8;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:12829714};
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 8;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8;
GN   Name=Pgant8 {ECO:0000312|FlyBase:FBgn0036529};
GN   ORFNames=CG7297 {ECO:0000312|FlyBase:FBgn0036529};
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;
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, PATHWAY, TISSUE SPECIFICITY, AND
RP   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).
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. It can both act as
CC       a peptide transferase that transfers GalNAc onto unmodified peptide
CC       substrates, and as a glycopeptide transferase that requires the prior
CC       addition of a GalNAc on a peptide before adding additional GalNAc
CC       moieties. Prefers both EA2 and the diglycosylated Muc5AC-3/13 as
CC       substrates, albeit at very low levels fro Muc5AC-3/13.
CC       {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       During embryonic stages 9-11, expressed in the primordium of the
CC       foregut, midgut and hindgut. During embryonic stages 12-13, expressed
CC       in the posterior midgut and hindgut. During embryonic stages 14-15,
CC       expression continues in the hindgut. No expression detected during
CC       embryonic stages 16-17 or in third instar larvae imaginal disks.
CC       {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:16251381}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Weakly
CC       expressed during early embryonic stages but increases during 12-24
CC       hours of embryogenesis through larval development and continues to be
CC       expressed throughout adulthood, albeit at slightly lower levels in
CC       males than females. {ECO:0000269|PubMed:12829714,
CC       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; AE014296; AAF49587.1; -; Genomic_DNA.
DR   EMBL; AY070966; AAL48588.1; -; mRNA.
DR   RefSeq; NP_648800.1; NM_140543.4.
DR   AlphaFoldDB; Q9VUT6; -.
DR   SMR; Q9VUT6; -.
DR   STRING; 7227.FBpp0075331; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q9VUT6; 2 sites, No reported glycans.
DR   GlyGen; Q9VUT6; 2 sites.
DR   PaxDb; 7227-FBpp0075331; -.
DR   DNASU; 39715; -.
DR   EnsemblMetazoa; FBtr0075578; FBpp0075331; FBgn0036529.
DR   GeneID; 39715; -.
DR   KEGG; dme:Dmel_CG7297; -.
DR   AGR; FB:FBgn0036529; -.
DR   CTD; 39715; -.
DR   FlyBase; FBgn0036529; Pgant8.
DR   VEuPathDB; VectorBase:FBgn0036529; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000166027; -.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   InParanoid; Q9VUT6; -.
DR   OMA; SRGFFDW; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q9VUT6; -.
DR   Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 39715; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 39715; -.
DR   PRO; PR:Q9VUT6; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036529; Expressed in embryonic/larval hemocyte (Drosophila) and 20 other cell types or tissues.
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:SF134; N-ACETYLGALACTOSAMINYLTRANSFERASE 4-RELATED; 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; Q9VUT6; 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..590
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 8"
FT                   /id="PRO_0000059162"
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..590
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          446..573
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          127..236
FT                   /note="Catalytic subdomain A"
FT   REGION          291..353
FT                   /note="Catalytic subdomain B"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        117..345
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        336..419
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        459..475
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        502..517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        546..561
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ   SEQUENCE   590 AA;  68100 MW;  B18B759A9FC2B021 CRC64;
     MCLDIWRHKK KVLPLLLLMA IGSIIYYLYT LKLEGERDES ATSTTSRLER DIRDLQAVFE
     SEVIPDLGAL GRPARGNWTE EQLEAIAKSQ RETGYNAWLS KRISPERSLY DMRHRSCKKL
     KYPMEKLPSV SVVITYHNEE ASVLLRTLSS LRSRTPIQLL REVILVDDGS TQADEKLNDF
     IKIKFLNMVQ HRRITTQVGL MHARVVGAEL ALADVLVFLD SHVEVTKGWL EPLIAPILED
     NRTCTTPIID TIDFDNFAYR RGKPSRGFFN WEFNYIQLPL LKEEAVAMPA PHKNPIMNGG
     LFAIGREWFS ELGGYDKGLK IWGAEQFELS LKLWLCGGQI LEVPCSRVGH LFRDGNFQIR
     YTNKDKNSEK KLISRNYRRV AEIWLDEYKD KLFANMPHLT VIPVGNLAEQ RDLKNRLHCK
     PFKWFLDNLA TDFLNLYPIL DPAEYASGVL QSISSPKLCL DRKDPSHGQP KLAPCSSDHV
     FPSPEQYWSL TNHRELRSGF YCLEVRNHGV NVHIYQCHGQ SGNQFWSFDS KTHQVISGQQ
     QNFRHCLEAQ PELNAVTSSV CDPKNHKQQW KFGYLNSQRL QHFWDNVKTQ
//