ID GALT5_DROME Reviewed; 630 AA.
AC Q6WV17; Q0E8T2; Q95T43; Q9VMU3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 5;
DE Short=pp-GaNTase 5;
DE EC=2.4.1.41 {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:18669915};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 5;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5;
GN Name=Pgant5 {ECO:0000312|FlyBase:FBgn0031681};
GN ORFNames=CG31651 {ECO:0000312|FlyBase:FBgn0031681};
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM A).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 14-630 (ISOFORM A), FUNCTION, CATALYTIC
RP ACTIVITY, 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, 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).
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 EA2 as
CC substrate (PubMed:12829714). In the larval midgut, required for O-
CC glycosylation of apical and luminal proteins within copper cells
CC enabling proper gut acidification (PubMed:22157008).
CC {ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:18669915,
CC ECO:0000269|PubMed:22157008}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q6WV17-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q6WV17-2; Sequence=VSP_034631;
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. During embryonic stages 9-11, expressed in the primordium of
CC the foregut, midgut and hindgut. Expressed in salivary glands from
CC embryonic stage 12 onwards. During embryonic stages 12-13, expressed in
CC the posterior midgut and hindgut. During embryonic stages 14-17,
CC expressed in the hindgut and the posterior spiracles. Expression is
CC also detected in the epidermis and antennomaxillary complex at
CC embryonic stages 16-17. In third instar larvae, ubiquitously expressed
CC in wing, 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 are first detected during embryonic stages 9-11.
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: Lethal (PubMed:22157008). RNAi-mediated knockdown
CC in the whole body, embryonic mesoderm, respiratory system or digestive
CC system and reproductive tract is lethal (PubMed:22157008). RNAi-
CC mediated knockdown in the larval digestive system, results in loss of
CC gut acidification and disruption of protein O-glycosylation in copper
CC cells (PubMed:22157008). RNAi-mediated knockdown in hemocytes,
CC amnioserosa, endoderm, mesoderm or nervous system causes no defect
CC (PubMed:22157008). {ECO:0000269|PubMed:22157008}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25377.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF52218.2; -; Genomic_DNA.
DR EMBL; AE014134; ABI31292.1; -; Genomic_DNA.
DR EMBL; AY060338; AAL25377.1; ALT_SEQ; mRNA.
DR EMBL; AY268066; AAQ56702.1; -; mRNA.
DR RefSeq; NP_001036338.1; NM_001042873.2. [Q6WV17-2]
DR RefSeq; NP_608906.2; NM_135062.4. [Q6WV17-1]
DR AlphaFoldDB; Q6WV17; -.
DR SMR; Q6WV17; -.
DR BioGRID; 77405; 1.
DR IntAct; Q6WV17; 2.
DR STRING; 7227.FBpp0078663; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyCosmos; Q6WV17; 1 site, No reported glycans.
DR GlyGen; Q6WV17; 1 site.
DR SwissPalm; Q6WV17; -.
DR PaxDb; 7227-FBpp0078663; -.
DR EnsemblMetazoa; FBtr0079026; FBpp0078663; FBgn0031681. [Q6WV17-1]
DR EnsemblMetazoa; FBtr0111024; FBpp0110323; FBgn0031681. [Q6WV17-2]
DR GeneID; 326151; -.
DR KEGG; dme:Dmel_CG31651; -.
DR UCSC; CG31651-RB; d. melanogaster.
DR AGR; FB:FBgn0031681; -.
DR CTD; 326151; -.
DR FlyBase; FBgn0031681; Pgant5.
DR VEuPathDB; VectorBase:FBgn0031681; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000169874; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q6WV17; -.
DR OMA; VAEVWMC; -.
DR OrthoDB; 202750at2759; -.
DR PhylomeDB; Q6WV17; -.
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; 326151; 0 hits in 1 CRISPR screen.
DR ChiTaRS; pgant5; fly.
DR GenomeRNAi; 326151; -.
DR PRO; PR:Q6WV17; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031681; Expressed in wing disc and 45 other cell types or tissues.
DR Genevisible; Q6WV17; DM.
DR GO; GO:0012505; C:endomembrane system; HDA: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: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:SF140; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 5; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..630
FT /note="Polypeptide N-acetylgalactosaminyltransferase 5"
FT /id="PRO_0000059159"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..630
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 500..622
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 186..296
FT /note="Catalytic subdomain A"
FT REGION 356..418
FT /note="Catalytic subdomain B"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 401..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 513..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 553..568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 594..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 398..457
FT /note="IWQCGGILEIIPCSHVGHVFRDKSPYTFPGGVAKIVLHNAARVAEVWLDEWR
FT DFYYSMST -> VWMCGGVLEIAPCSRVGHVFRKSTPYTFPGGTTEIVNHNNARLVEVW
FT LDDWKEFYYSFYP (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_034631"
FT CONFLICT 591
FT /note="T -> S (in Ref. 4; AAQ56702)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 630 AA; 72097 MW; A822748C9EC96175 CRC64;
MTFSTFTRKM RGRMRSNTCR IVLLTSLVWV IFDFVLIARY SDCIGKDGWR CKRSGEYDVE
LPNAERLVDD NQLVDDNEIN TEKSLDGESG GALIMGQGFA SGGISMTYPS VVLKKWFLAP
SVQEAKGKPG EMGKPVKIPA DMKDLMKEKF KENQFNLLAS DMISLNRSLT DVRHEGCRRK
HYASKLPTTS IVIVFHNEAW TTLLRTVWSV INRSPRALLK EIILVDDASE RDFLGKQLEE
YVAKLPVKTF VLRTEKRSGL IRARLLGAEH VSGEVITFLD AHCECTEGWL EPLLARIVQN
RRTVVCPIID VISDETFEYI TASDSTWGGF NWKLNFRWYR VPSREMARRN NDRTAPLRTP
TMAGGLFSID KDYFYEIGSY DEGMDIWGGE NLEMSFRIWQ CGGILEIIPC SHVGHVFRDK
SPYTFPGGVA KIVLHNAARV AEVWLDEWRD FYYSMSTGAR KASAGDVSDR KALRDRLKCK
SFRWYLENVY PESLMPLDYY YLGEIRNAET ETCLDTMGRK YNEKVGISYC HGLGGNQVFA
YTKRQQIMSD DLCLDASSSN GPVNMVRCHN MGGNQEWVYD AEEKWIRHTN TGQCLQRATR
DDANTPLLRP CSYGKGQQWL MESKFKWQAH
//
