GLT12_DROME
ID GLT12_DROME Reviewed; 563 AA.
AC Q8IA44; Q9VUT4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative inactive polypeptide N-acetylgalactosaminyltransferase 12;
DE Short=pp-GaNTase 12;
DE AltName: Full=Inactive UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12;
DE AltName: Full=Inactive protein-UDP acetylgalactosaminyltransferase 12;
GN Name=pgant12; ORFNames=CG7304;
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 [MRNA].
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 His at
CC position 211 which is part of the Asp-Xaa-His motif which binds the
CC cofactor Mn(2+). This suggests that it may have lost its activity.
CC {ECO:0000305}.
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DR EMBL; AF324750; AAN75749.1; -; mRNA.
DR EMBL; AE014296; AAS64999.1; -; Genomic_DNA.
DR RefSeq; NP_996098.1; NM_206376.1.
DR AlphaFoldDB; Q8IA44; -.
DR SMR; Q8IA44; -.
DR IntAct; Q8IA44; 1.
DR STRING; 7227.FBpp0075330; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8IA44; 6 sites.
DR PaxDb; Q8IA44; -.
DR PRIDE; Q8IA44; -.
DR EnsemblMetazoa; FBtr0075577; FBpp0075330; FBgn0036527.
DR GeneID; 39713; -.
DR KEGG; dme:Dmel_CG7304; -.
DR UCSC; CG7304-RA; d. melanogaster.
DR FlyBase; FBgn0036527; CG7304.
DR VEuPathDB; VectorBase:FBgn0036527; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000166027; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8IA44; -.
DR OMA; INLSVMQ; -.
DR OrthoDB; 276134at2759; -.
DR PhylomeDB; Q8IA44; -.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR SignaLink; Q8IA44; -.
DR BioGRID-ORCS; 39713; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39713; -.
DR PRO; PR:Q8IA44; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036527; Expressed in male reproductive gland and 5 other tissues.
DR Genevisible; Q8IA44; 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:0019953; P:sexual reproduction; IEP: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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Lectin; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..563
FT /note="Putative inactive polypeptide N-
FT acetylgalactosaminyltransferase 12"
FT /id="PRO_0000059166"
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..563
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 433..549
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 109..225
FT /note="Catalytic subdomain A"
FT REGION 280..342
FT /note="Catalytic subdomain B"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 446..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 485..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 523..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 563 AA; 65108 MW; F56D71430BD88B36 CRC64;
MEVFASVLNC CFKYIVLPVW IFIVLLLLHR DLSSWDGLMG PLSHPGLGEN GSASYLSVPS
WEIDEYTQGW RYYLYNSWLA ERIPLRRSLP DLRDHRCQKL EYDEDSDEMK PASIIMIFRN
EQLVVLLRTL HSLVERTPKY LYIELILVND HSDTDFWNDK LSLIFFDNYV HRYIHPKARI
LHLPEQVGLI KARNLAASEA KAENLVFVDA QVEFTNGWLS PLLDTIAEQS YTLATPILDN
LDEQTLAYQR SIERRGMYDW SLTRREVPLS RARRSHLPWP YEVAAVRTSV FAIPAVWFQD
ISNFDNNLRG FGAAELELSF KVWCTGGRIV QVPCSRVGHL QPKDEDYLKR YGDLHKMGEQ
KSRNLKRIIE VWTGDLKSAI YKYQPHLLNI SEGDLNEPRK LYKQNECQSF KEFINDITPG
LNHVAALNRT DYASGHVKTL EFPKKCLTIN AKSQNLFLER CSTNNTLQNW TLTYVKDLRV
AGNICAEVRP NLRLGYSFCH SLGGRQSWHY DSVSNQLMSN TKCLEFTDEL NIFLAICDAA
NGKQRWILDN INLSVMQSAN ILV
