GLT11_DROME
ID GLT11_DROME Reviewed; 557 AA.
AC Q8IA41; Q9VUT5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative inactive polypeptide N-acetylgalactosaminyltransferase 11;
DE Short=pp-GaNTase 11;
DE AltName: Full=Inactive UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11;
DE AltName: Full=Inactive protein-UDP acetylgalactosaminyltransferase 11;
GN Name=pgant11 {ECO:0000312|FlyBase:FBgn0036528};
GN ORFNames=CG7579 {ECO:0000312|FlyBase:FBgn0036528};
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].
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 [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).
CC -!- FUNCTION: Probable inactive glycosyltransferase. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
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}.
CC -!- CAUTION: Although strongly related to polypeptide N-
CC acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-
CC Xaa-His motif in positions 199-201 and the conserved His residue in
CC position 330 which are involved in the binding to the cofactor Mn(2+).
CC This suggests that it may have lost its activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF49588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF326979; AAO13781.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49588.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_648799.1; NM_140542.2.
DR AlphaFoldDB; Q8IA41; -.
DR SMR; Q8IA41; -.
DR STRING; 7227.FBpp0075334; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8IA41; 4 sites.
DR PaxDb; Q8IA41; -.
DR PRIDE; Q8IA41; -.
DR EnsemblMetazoa; FBtr0075581; FBpp0075334; FBgn0036528.
DR GeneID; 39714; -.
DR KEGG; dme:Dmel_CG7579; -.
DR UCSC; CG7579-RA; d. melanogaster.
DR FlyBase; FBgn0036528; CG7579.
DR VEuPathDB; VectorBase:FBgn0036528; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000166027; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8IA41; -.
DR OrthoDB; 276134at2759; -.
DR PhylomeDB; Q8IA41; -.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR BioGRID-ORCS; 39714; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39714; -.
DR PRO; PR:Q8IA41; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036528; Expressed in male reproductive gland and 3 other tissues.
DR Genevisible; Q8IA41; DM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0009312; P:oligosaccharide biosynthetic process; ISS: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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Lectin; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..557
FT /note="Putative inactive polypeptide N-
FT acetylgalactosaminyltransferase 11"
FT /id="PRO_0000059165"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..557
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 456..557
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 109..215
FT /note="Catalytic subdomain A"
FT REGION 271..333
FT /note="Catalytic subdomain B"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 316..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 437..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 472..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 511..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 557 AA; 64539 MW; B6F58FBAF8DB5F75 CRC64;
MKSLLFGTPC SCAIFILVYC IITLFIWFLY TDNLSNAIVD FEYFSIKNLG ELGKEAHLQM
TETDLVDAQL QNEKYQYNAW LSERIPLKRT LEDYRDPQCL KINYSSEKTV TVSIVIAIQQ
EHPHTLLRGI YSVITQTSPY LLKEIVLVHD GHPDLDLIRH IHHKLPIVIQ LEMESSKGII
HARLTGAGVA TGDILVFLNG HMEVTRGWLP PLLEPILLNN QTVTEPIVDA ISRESFAYRK
LVEPEQLAFD WQLDHIFLPL DQHSWNSLPK PYPSSQLEGR VFAIDRKWFW HLGGWDEGLR
DYGGDALELS LKVWQCGGLI LAVPCSRVGI IYKRDELEAQ MAPNRNPSLQ VQKNFKRVVD
VWLDEYKLHF YRYNPKLRNL TAESLDKPRD LRRRLNCKSF EWYRSQVAPQ IRNHFLHAGL
TNYPIGKIMP FVAPHFCLSI KGGFPVIRKC HSTNFEDWTL TSRCQLKHGN MCLDVDYKNN
VRATKCTKKL SKNPWHYNYQ HSSFVSNGNK CLQIDVNKVG LILSACDSDV TEQRWMFTKV
QDFKLDHMRD ICLSVNH
