GLT35_DROME
ID GLT35_DROME Reviewed; 632 AA.
AC Q8MVS5; Q8MVS2; Q8MVS3; Q8MVS4; Q8SYF1; Q965E4; Q9V3C9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 35A;
DE EC=2.4.1.41 {ECO:0000269|PubMed:11925446, ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:12829714};
DE AltName: Full=Protein l(2)35Aa;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 35A;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 35A;
DE Short=pp-GaNTase 35A;
DE AltName: Full=dGalNAc-T1;
GN Name=Pgant35A {ECO:0000312|FlyBase:FBgn0001970};
GN ORFNames=CG7480 {ECO:0000312|FlyBase:FBgn0001970};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF ARG-227.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=11925446; DOI=10.1074/jbc.m201807200;
RA Ten Hagen K.G., Tran D.T.;
RT "A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential
RT for viability in Drosophila melanogaster.";
RL J. Biol. Chem. 277:22616-22622(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-227.
RX PubMed=11925450; DOI=10.1074/jbc.m202684200;
RA Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A.,
RA Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R.,
RA Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A.,
RA Clausen H.;
RT "Functional conservation of subfamilies of putative UDP-N-
RT acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in
RT Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of
RT l(2)35Aa is essential in Drosophila.";
RL J. Biol. Chem. 277:22623-22638(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, 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 [8]
RP FUNCTION, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [10]
RP MUTAGENESIS OF ASP-243.
RX PubMed=20422447; DOI=10.1007/s10719-010-9290-5;
RA Bennett E.P., Chen Y.W., Schwientek T., Mandel U., Schjoldager K.T.,
RA Cohen S.M., Clausen H.;
RT "Rescue of Drosophila Melanogaster l(2)35Aa lethality is only mediated by
RT polypeptide GalNAc-transferase pgant35A, but not by the evolutionary
RT conserved human ortholog GalNAc-transferase-T11.";
RL Glycoconj. J. 27:435-444(2010).
RN [11]
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 [12]
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).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25253852; DOI=10.1523/jneurosci.1484-14.2014;
RA Dani N., Zhu H., Broadie K.;
RT "Two protein N-acetylgalactosaminyl transferases regulate synaptic
RT plasticity by activity-dependent regulation of integrin signaling.";
RL J. Neurosci. 34:13047-13065(2014).
CC -!- FUNCTION: Polypeptide N-acetylgalactosaminyltransferases catalyze the
CC transfer of an N-acetyl-D-galactosamine residue to a serine or
CC threonine residue on the protein receptor (PubMed:11925450,
CC PubMed:12829714). Displays the same enzyme activity toward MUC1, MUC4,
CC and EA2 (PubMed:11925450, PubMed:12829714). Not involved in
CC glycosylation of erythropoietin (EPO) (PubMed:11925450). It can both
CC act as a peptide transferase that transfers GalNAc onto unmodified
CC peptide substrates, and as a glycopeptide transferase that requires the
CC prior addition of a GalNAc on a peptide before adding additional GalNAc
CC moieties (PubMed:11925450, PubMed:12829714). Protein modification by
CC this enzyme might be important for cytokinesis and tube formation
CC during embryogenesis (PubMed:16251381, PubMed:20807760). Together with
CC Pgant3, regulates integrin levels and activity-dependent integrin
CC signaling at the synapse in neurons and muscles (PubMed:25253852).
CC {ECO:0000269|PubMed:11925450, ECO:0000269|PubMed:12829714,
CC ECO:0000269|PubMed:16251381, ECO:0000269|PubMed:20807760,
CC ECO:0000269|PubMed:25253852}.
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:11925446, ECO:0000269|PubMed:11925450,
CC 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:11925446, ECO:0000269|PubMed:11925450,
CC ECO:0000269|PubMed:12829714};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.5 uM for UDP-GalNAc {ECO:0000269|PubMed:11925446};
CC KM=0.35 mM for EA2 acceptor peptide {ECO:0000269|PubMed:11925446};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:11925446, ECO:0000305|PubMed:11925450,
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 at high level in ovaries. Expressed at
CC low level in testis. Expressed at higher level in adult females than
CC males. During oogenesis, it is detected in germ cells and follicle
CC epithelia of all developmental stages. Initially expressed during early
CC stages of oogenesis in region I and reaches high levels in regions IIa
CC and IIb of the germarium. Highly expressed in stage 2 egg chambers.
CC Remains highly expressed during later stages of oogenesis. During
CC embryonic stages 9-11, expressed in the primordium of the foregut,
CC midgut and hindgut. Expressed in salivary glands from embryonic stage
CC 12 onwards. During embryonic stages 12-13, expressed in the posterior
CC midgut and hindgut. During embryonic stages 14-15, expression continues
CC in the hindgut. During embryonic stages 16-17, expressed in the dorsal
CC longitudinal trachea and posterior spiracles. In third instar larvae,
CC ubiquitously expressed in wing, eye-antennal, leg and haltere imaginal
CC disks. {ECO:0000269|PubMed:11925450, 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:11925446, ECO:0000269|PubMed:11925450,
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: Mutant larval shows down-regulation of synaptic
CC O-linked glycosylation, integrin level and signaling via Ten-m and if.
CC Synapses show smaller synaptic boutons, expanded activity-dependent
CC postsynaptic pockets which affect synaptic plasticity and synaptic
CC strength in both the pre-synaptic and post-synaptic assembly, no
CC differences in neuromuscular junction morphology (PubMed:25253852).
CC Simultaneous knockout of Pgant3, restores normal synaptic strength
CC (PubMed:25253852). RNAi-mediated knockdown is lethal (PubMed:22157008).
CC RNAi-mediated knockdown in the mesoderm, respiratory system, digestive
CC system or reproductive tract results in a reduction in viability
CC (PubMed:22157008). {ECO:0000269|PubMed:22157008,
CC ECO:0000269|PubMed:25253852}.
CC -!- MISCELLANEOUS: The human ortholog GALNT11 (AC Q8NCW6) is not able to
CC rescue lethality caused by the SF32 mutation.
CC {ECO:0000305|PubMed:20422447}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK66862.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF478697; AAM62405.1; -; mRNA.
DR EMBL; AF478698; AAM62406.1; -; Genomic_DNA.
DR EMBL; AF478699; AAM62407.1; -; Genomic_DNA.
DR EMBL; AF478700; AAM62408.1; -; Genomic_DNA.
DR EMBL; AF158747; AAK66862.1; ALT_INIT; mRNA.
DR EMBL; AE014134; AAF53391.1; -; Genomic_DNA.
DR EMBL; AY071591; AAL49213.1; -; mRNA.
DR RefSeq; NP_652069.2; NM_143812.4.
DR AlphaFoldDB; Q8MVS5; -.
DR SMR; Q8MVS5; -.
DR BioGRID; 71677; 1.
DR IntAct; Q8MVS5; 3.
DR STRING; 7227.FBpp0080202; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8MVS5; 2 sites.
DR PaxDb; Q8MVS5; -.
DR PRIDE; Q8MVS5; -.
DR DNASU; 48775; -.
DR EnsemblMetazoa; FBtr0080629; FBpp0080202; FBgn0001970.
DR GeneID; 48775; -.
DR KEGG; dme:Dmel_CG7480; -.
DR CTD; 48775; -.
DR FlyBase; FBgn0001970; Pgant35A.
DR VEuPathDB; VectorBase:FBgn0001970; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000165841; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8MVS5; -.
DR OMA; FQPWHSR; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8MVS5; -.
DR BRENDA; 2.4.1.41; 1994.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR SABIO-RK; Q8MVS5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 48775; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 48775; -.
DR PRO; PR:Q8MVS5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001970; Expressed in hindgut proper primordium (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q8MVS5; baseline and differential.
DR Genevisible; Q8MVS5; 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:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; 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..632
FT /note="Polypeptide N-acetylgalactosaminyltransferase 35A"
FT /id="PRO_0000059168"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..632
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 526..632
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 147..259
FT /note="Catalytic subdomain A"
FT REGION 317..379
FT /note="Catalytic subdomain B"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 136..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 362..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 493..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 539..553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 580..597
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT MUTAGEN 227
FT /note="R->W: In SF32; induces lethality."
FT /evidence="ECO:0000269|PubMed:11925446,
FT ECO:0000269|PubMed:11925450"
FT MUTAGEN 243
FT /note="D->N: Abolishes glycosyltransferase activity. Not
FT able to rescue lethality caused by SF32 mutation."
FT /evidence="ECO:0000269|PubMed:20422447"
FT CONFLICT 72
FT /note="I -> T (in Ref. 1; AAM62405)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="S -> T (in Ref. 6; AAL49213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 71828 MW; E726B9F32481E4E9 CRC64;
MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA TPRAELSYQA
RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ DKYIRDIGYK HHAFNALVSN
NIGLFRAIPD TRHKVCDRQE TTEAENLPQA SIVMCFYNEH KMTLMRSIKT VLERTPSYLL
REIILVDDHS DLPELEFHLH GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV
FLDSHIEVNQ QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW
ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG ENIEISFRAW
QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL AHVWMDQYKD YYLKHEKVPK
TYDYGDISDR LKLRERLQCR DFAWYLKNVY PELHVPGEES KKSAAAPIFQ PWHSRKRNYV
DTFQLRLTGT ELCAAVVAPK VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL
EASGDAQVTV NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS
NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL
