GALT7_PONAB
ID GALT7_PONAB Reviewed; 657 AA.
AC Q5RFJ6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {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 -!- 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}.
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DR EMBL; CR857160; CAH89461.1; -; mRNA.
DR RefSeq; NP_001124628.1; NM_001131156.2.
DR AlphaFoldDB; Q5RFJ6; -.
DR SMR; Q5RFJ6; -.
DR STRING; 9601.ENSPPYP00000016986; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR Ensembl; ENSPPYT00000017673; ENSPPYP00000016986; ENSPPYG00000015203.
DR GeneID; 100171466; -.
DR KEGG; pon:100171466; -.
DR CTD; 51809; -.
DR eggNOG; KOG3737; Eukaryota.
DR GeneTree; ENSGT00940000158105; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q5RFJ6; -.
DR OMA; EMNNIHT; -.
DR OrthoDB; 606683at2759; -.
DR TreeFam; TF352176; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001595; Chromosome 4.
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; IEA:UniProtKB-EC.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:Ensembl.
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_0000294079"
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 31..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 COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 75423 MW; 4D0A39FF18BD31A9 CRC64;
MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP MPNRGGNGLA
PGEDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQEHHAG GDSQKDIMQR QYLTFKPQTF
TYRDPVLRPG ILGNFEPKEP EPPGVVGGPG EKAKPLVLGP EFKQAIQASI KEFGFNMVAS
DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA
EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG YARGAWDWSM
LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF ELGLYDPGLQ IWGGENFEIS
YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF
YASRPESQAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF
ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC
NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE MNNIHSV
