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   24-JAN-2024, entry version 137.
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   GlyCosmos; Q8IA44; 6 sites, No reported glycans.
DR   GlyGen; Q8IA44; 6 sites.
DR   PaxDb; 7227-FBpp0075330; -.
DR   EnsemblMetazoa; FBtr0075577; FBpp0075330; FBgn0036527.
DR   GeneID; 39713; -.
DR   KEGG; dme:Dmel_CG7304; -.
DR   UCSC; CG7304-RA; d. melanogaster.
DR   AGR; FB:FBgn0036527; -.
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; 3536486at2759; -.
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 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: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; 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; Q8IA44; DM.
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
//