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N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-) (Protein-UDP acetylgalactosaminyltransferase 7) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7) (pp-GaNTase 7) (dGalNAc-T2)

 GALT7_DROME             Reviewed;         591 AA.
Q8MV48; A4V4R2; Q5U0W9; Q95RJ3; Q95TN2; Q9VWT6;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
07-JUN-2017, entry version 121.
RecName: Full=N-acetylgalactosaminyltransferase 7;
EC=2.4.1.-;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7;
Short=pp-GaNTase 7;
AltName: Full=dGalNAc-T2;
Name=GalNAc-T2; Synonyms=pgant7; ORFNames=CG6394;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ENZYME ACTIVITY.
PubMed=11925450; DOI=10.1074/jbc.M202684200;
Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M.,
Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A.,
Haselmann K., Zubarev R., Roepstorff P., Burchell J.M.,
Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.;
"Functional conservation of subfamilies of putative UDP-N-
acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in
Drosophila, Caenorhabditis elegans, and mammals. One subfamily
composed of l(2)35Aa is essential in Drosophila.";
J. Biol. Chem. 277:22623-22638(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=Canton-S; TISSUE=Embryo;
PubMed=12829714; DOI=10.1074/jbc.M303836200;
Ten Hagen K.G., Tran D.T., Gerken T.A., Stein D.S., Zhang Z.;
"Functional characterization and expression analysis of members of the
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from
Drosophila melanogaster.";
J. Biol. Chem. 278:35039-35048(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-591.
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16251381; DOI=10.1093/glycob/cwj051;
Tian E., Ten Hagen K.G.;
"Expression of the UDP-GalNAc: polypeptide N-
acetylgalactosaminyltransferase family is spatially and temporally
regulated during Drosophila development.";
Glycobiology 16:83-95(2006).
-!- FUNCTION: Glycopeptide transferase involved in O-linked
oligosaccharide biosynthesis, which catalyzes the transfer of an
N-acetyl-D-galactosamine residue to an already glycosylated
peptide. In contrast to other proteins of the family, it does not
act as a peptide transferase that transfers GalNAc onto serine or
threonine residue on the protein receptor, but instead requires
the prior addition of a GalNAc on a peptide before adding
additional GalNAc moieties. Some peptide transferase activity is
however not excluded, considering that its appropriate peptide
substrate may remain unidentified. Prefers the monoglycosylated
Muc5AC-3 as substrate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in developing oocytes and egg
chambers. During embryonic stages 9-11, expressed in the
primordium of the foregut, midgut and hindgut. Expressed in the
salivary glands from embryonic stage 12 onwards. During embryonic
stages 12-13, expressed in the posterior midgut and hindgut.
During embryonic stages 14-15, expression continues in the
hindgut. During embryonic stages 16-17, expressed in the
antennomaxillary complex. In third instar larvae, ubiquitously
expressed in wing, with increased expression in the notum and
ventral wing pouch, eye-antennal, leg and haltere imaginal disks.
{ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:16251381}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed throughout embryonic, larval, pupal and adult stages,
with increasing levels during larval development.
{ECO:0000269|PubMed:12829714, ECO:0000269|PubMed:16251381}.
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL13889.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL28887.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF493067; AAM62412.1; -; mRNA.
EMBL; AY268068; AAQ56704.1; -; mRNA.
EMBL; AE014298; AAF48851.1; -; Genomic_DNA.
EMBL; AE014298; AAN09470.1; -; Genomic_DNA.
EMBL; BT016123; AAV37008.1; -; mRNA.
EMBL; AY058660; AAL13889.1; ALT_INIT; mRNA.
EMBL; AY061339; AAL28887.1; ALT_INIT; mRNA.
RefSeq; NP_001285406.1; NM_001298477.1.
RefSeq; NP_573301.2; NM_133073.3.
RefSeq; NP_728178.1; NM_167623.2.
UniGene; Dm.7692; -.
ProteinModelPortal; Q8MV48; -.
SMR; Q8MV48; -.
BioGrid; 59149; 4.
IntAct; Q8MV48; 4.
MINT; MINT-325977; -.
STRING; 7227.FBpp0074396; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
PaxDb; Q8MV48; -.
PRIDE; Q8MV48; -.
EnsemblMetazoa; FBtr0074624; FBpp0074395; FBgn0030930.
EnsemblMetazoa; FBtr0074625; FBpp0074396; FBgn0030930.
EnsemblMetazoa; FBtr0346082; FBpp0311917; FBgn0030930.
GeneID; 32836; -.
KEGG; dme:Dmel_CG6394; -.
UCSC; CG6394-RB; d. melanogaster.
CTD; 32836; -.
FlyBase; FBgn0030930; GalNAc-T2.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
InParanoid; Q8MV48; -.
KO; K00710; -.
OMA; NFEYRPV; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q8MV48; -.
Reactome; R-DME-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
GenomeRNAi; 32836; -.
PRO; PR:Q8MV48; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0030930; -.
ExpressionAtlas; Q8MV48; differential.
Genevisible; Q8MV48; DM.
GO; GO:0012505; C:endomembrane system; IDA:FlyBase.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005795; C:Golgi stack; NAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 591 N-acetylgalactosaminyltransferase 7.
/FTId=PRO_0000059161.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 591 Lumenal. {ECO:0000255}.
DOMAIN 466 585 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 141 251 Catalytic subdomain A.
REGION 313 375 Catalytic subdomain B.
METAL 235 235 Manganese. {ECO:0000250}.
METAL 237 237 Manganese. {ECO:0000250}.
METAL 372 372 Manganese. {ECO:0000250}.
BINDING 182 182 Substrate. {ECO:0000250}.
BINDING 212 212 Substrate. {ECO:0000250}.
BINDING 344 344 Substrate. {ECO:0000250}.
BINDING 375 375 Substrate. {ECO:0000250}.
BINDING 380 380 Substrate. {ECO:0000250}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 576 576 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 132 367 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 358 441 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 479 496 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 519 532 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 558 573 {ECO:0000255|PROSITE-ProRule:PRU00174}.
CONFLICT 84 84 P -> S (in Ref. 1; AAM62412).
{ECO:0000305}.
SEQUENCE 591 AA; 68333 MW; 6CC2F7DC38E4CF17 CRC64;
MRVSTIRSGR ICRLALCLLV LLPLLYLLAN WSDHHKRVQE AYHTRFGGPK FAHQRLEGRP
REVPKLVDGL GNFEPKDVKP RSGPGENGEA HSLSPDKKHM SDASEMEYGM NIACSDEISM
HRSVRDTRLE ECRHWDYPFD LPRTSVIIVF HNEGFSVLMR TVHSVIDRSP THMLHEIILV
DDFSDKENLR SQLDEYVLQF KGLVKVIRNK EREGLIRTRS RGAMEATGEV IVFLDAHCEV
NTNWLPPLLA PIYRDRTVMT VPIIDGIDHK NFEYRPVYGT DNHFRGIFEW GMLYKENEVP
RREQRRRAHN SEPYRSPTHA GGLFAINREY FLELGAYDPG LLVWGGENFE LSFKIWQCGG
SIEWVPCSRV GHVYRGFMPY NFGKLASKKK GPLITINYKR VIETWFDDTH KEYFYTREPL
ARYLDMGDIS EQLALKKRLN CKSFQWFMDH IAYDVYDKFP GLPANLHWGE LRSVASDGCL
DSMGHQPPAI MGLTYCHGGG NNQLVRLNAA GQLGVGERCV EADRQGIKLA VCRLGTVDGP
WQYNEHTKHL MHRVHKKCMA LHPATQQLSL GHCDVNDSYQ QWWFKEIRPR W


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