GALT6_BOVIN
ID GALT6_BOVIN Reviewed; 622 AA.
AC Q5EA41;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 6;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 6;
DE Short=GalNAc-T6;
DE Short=pp-GaNTase 6;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
GN Name=GALNT6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. May participate in
CC synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2,
CC EA2 and fibronectin peptides (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
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; BT020728; AAX08745.1; -; mRNA.
DR RefSeq; NP_001015534.1; NM_001015534.1.
DR AlphaFoldDB; Q5EA41; -.
DR SMR; Q5EA41; -.
DR STRING; 9913.ENSBTAP00000023861; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR PaxDb; Q5EA41; -.
DR GeneID; 506903; -.
DR KEGG; bta:506903; -.
DR CTD; 11226; -.
DR eggNOG; KOG3736; Eukaryota.
DR InParanoid; Q5EA41; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Polypeptide N-acetylgalactosaminyltransferase 6"
FT /id="PRO_0000059113"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..622
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 496..622
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 103..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..285
FT /note="Catalytic subdomain A"
FT REGION 348..410
FT /note="Catalytic subdomain B"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 393..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 509..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 553..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 597..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 622 AA; 71138 MW; 05010D38D433A376 CRC64;
MRLLRRRHMA VRLVMVGSAF VLFLFILQRD VSGREQATEK PWLRSLVSQK DHVLDLMLGA
VHNLRDSMPK FQIRAPEPQQ TLASTNQSCL PGFYTPAELK PFWERPPQDP NGPGADGKAF
QKKEWTPQET QEKEEGYKKH CFNAFASDRI SLQRALGPDT RPPECVDQKF RRCPPLPATS
VIIVFHNEAW STLLRTVYSV LHTTPAILLK EIILVDDAST DEYLKEPLER YVKQLQVVQV
VRQQERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDE TVVVSPNIVT
IDLNTFEFSK PVQRGRVQSR GNFDWSLTFG WEVLPAREKQ RRKDETYPIK SPTFAGGLFS
ISKSYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG
INVIARNQVR LAEVWMDGYK EIFYRRNLQA AQMAREKSFG DISERLQLRE RLNCHNFSWF
LDNVYPEMFV PDLKPTFFGA LKNLGVDHCL DVGENNNGGK PLILYTCHGL GGNQYFEYTT
QRDLRHNIAK QLCLHASAGT LGLRSCHFTG KNSQVPKDEE WEFTQDQLIR NSGSGTCLTS
KDKKPVMATC NPSDPHQHWL FI
