GALT7_RAT
ID GALT7_RAT Reviewed; 657 AA.
AC Q9R0C5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=N-acetylgalactosaminyltransferase 7;
DE EC=2.4.1.41 {ECO:0000250|UniProtKB:Q86SF2};
DE AltName: Full=Polypeptide GalNAc transferase 7;
DE Short=GalNAc-T7;
DE Short=pp-GaNTase 7;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7;
GN Name=Galnt7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Sublingual gland;
RX PubMed=10488133; DOI=10.1074/jbc.274.39.27867;
RA Ten Hagen K.G., Tetaert D., Hagen F.K., Richet C., Beres T.B., Gagnon J.,
RA Balys M.M., VanWuyckhuyse B., Bedi G.S., Degand P., Tabak L.A.;
RT "Characterization of a UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase that displays glycopeptide N-
RT acetylgalactosaminyltransferase activity.";
RL J. Biol. Chem. 274:27867-27874(1999).
CC -!- FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide
CC biosynthesis, which catalyzes the transfer of an N-acetyl-D-
CC galactosamine residue to an already glycosylated peptide. In contrast
CC to other proteins of the family, it does not act as a peptide
CC transferase that transfers GalNAc onto serine or threonine residue on
CC the protein receptor, but instead requires the prior addition of a
CC GalNAc on a peptide before adding additional GalNAc moieties. Some
CC peptide transferase activity is however not excluded, considering that
CC its appropriate peptide substrate may remain unidentified.
CC {ECO:0000250|UniProtKB:Q86SF2}.
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:0000250|UniProtKB:Q86SF2};
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:0000250|UniProtKB:Q86SF2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q86SF2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in sublingual gland. Expressed at
CC lower level in stomach, small intestiine and colon.
CC {ECO:0000269|PubMed:10488133}.
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: Was originally termed Galnt6/pp-GaNTase 6.
CC {ECO:0000305|PubMed:10488133}.
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DR EMBL; AF076167; AAC99426.1; -; mRNA.
DR RefSeq; NP_075215.1; NM_022926.1.
DR AlphaFoldDB; Q9R0C5; -.
DR SMR; Q9R0C5; -.
DR STRING; 10116.ENSRNOP00000016474; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR PaxDb; Q9R0C5; -.
DR GeneID; 29750; -.
DR KEGG; rno:29750; -.
DR UCSC; RGD:620362; rat.
DR CTD; 51809; -.
DR RGD; 620362; Galnt7.
DR VEuPathDB; HostDB:ENSRNOG00000012037; -.
DR eggNOG; KOG3737; Eukaryota.
DR InParanoid; Q9R0C5; -.
DR OMA; EMNNIHT; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q9R0C5; -.
DR TreeFam; TF352176; -.
DR BRENDA; 2.4.1.41; 5301.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9R0C5; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000012037; Expressed in stomach and 20 other tissues.
DR Genevisible; Q9R0C5; RN.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISO:RGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:RGD.
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; Glycosyltransferase; Golgi apparatus; Lectin; Manganese;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..657
FT /note="N-acetylgalactosaminyltransferase 7"
FT /id="PRO_0000059118"
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..657
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 532..652
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 30..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..317
FT /note="Catalytic subdomain A"
FT REGION 381..443
FT /note="Catalytic subdomain B"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 197..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 426..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 545..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 585..600
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 625..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 657 AA; 75335 MW; 952DE15F0758A625 CRC64;
MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDPSPLSR MREDRDVNNP LPNRGGNGLA
PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG GDSQKDIMQR QYLTFKPQTF
TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG ENAKPLVLGP EYKQAAQASI KEFGFNMAAS
DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA
EIVLIDDFSN KEHLKEKLTE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
DAHCEVAVNW YAPLVAPISK DRTICTVPII DVINGNTYEI IPQGGGDEDG YARGAWDWSM
LWKRVPLTPR EKRLRKTKTE PYRSPAMAGG LFAIERDFFF ELGLYDPGLQ IWGGENFEIS
YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPLYVGSSP TLKNYVRVVE VWWDEYKDYF
YASRPESKAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITAHYPLPPR NVEWGEIRGL
ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGP DGSKVMITHC
NLNEFKEWQY FKNLHRFTHI ASGKCLDRSE VLHQVFISSC DNGKMTQKWE MNNIHSV
