GLT13_RAT
ID GLT13_RAT Reviewed; 556 AA.
AC Q6UE39;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 13;
DE EC=2.4.1.41 {ECO:0000250|UniProtKB:Q8IUC8};
DE AltName: Full=Polypeptide GalNAc transferase 13;
DE Short=GalNAc-T13;
DE Short=pp-GaNTase 13;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 13;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13;
GN Name=Galnt13;
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].
RA Huang C.Q., Wu S.L., Liu S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc)
CC residue from UDP-GalNAc to a serine or threonine residue on the protein
CC receptor (By similarity). Generates GalNAc-O-Ser/Thr structure also
CC known as Tn antigen, which itself is immunogenic but also serves as a
CC precursor for the synthesis of different mucin-type O-glycan core
CC structures (By similarity). Contributes to the synthesis of O-linked
CC glycans on mucins and proteoglycans of the central nervous system (By
CC similarity). Can glycosylate both unmodified peptides and glycopeptides
CC that already contain an O-linked GalNAc sugar. Transfers GalNAc to
CC Thr-/Ser-rich tandem repeats GTTPSPVPTTSTTSAP of MUC5AC. Transfers
CC GalNAc to three consecutive serine/threonine residues on SDC3 forming a
CC triplet-Tn epitope expressed in Purkinje cells of the developing brain
CC (By similarity). May promote neurogenesis through glycosylation and
CC stabilization of PDPN (By similarity). {ECO:0000250|UniProtKB:Q8CF93,
CC ECO:0000250|UniProtKB:Q8IUC8}.
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:Q8IUC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957;
CC Evidence={ECO:0000250|UniProtKB:Q8IUC8};
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:Q8IUC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000250|UniProtKB:Q8IUC8};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8IUC8}.
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; AY371923; AAQ75749.1; -; mRNA.
DR RefSeq; NP_954537.1; NM_199106.1.
DR RefSeq; XP_017447165.1; XM_017591676.1.
DR AlphaFoldDB; Q6UE39; -.
DR SMR; Q6UE39; -.
DR STRING; 10116.ENSRNOP00000042772; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q6UE39; 3 sites.
DR PaxDb; Q6UE39; -.
DR PRIDE; Q6UE39; -.
DR GeneID; 311039; -.
DR KEGG; rno:311039; -.
DR UCSC; RGD:735044; rat.
DR CTD; 114805; -.
DR RGD; 735044; Galnt13.
DR VEuPathDB; HostDB:ENSRNOG00000005335; -.
DR eggNOG; KOG3736; Eukaryota.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q6UE39; -.
DR OMA; NSNQCLA; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q6UE39; -.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6UE39; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005335; Expressed in cerebellum and 4 other tissues.
DR Genevisible; Q6UE39; 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 GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:RGD.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; 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; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..556
FT /note="Polypeptide N-acetylgalactosaminyltransferase 13"
FT /id="PRO_0000059132"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..556
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 428..550
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 114..224
FT /note="Catalytic subdomain A"
FT REGION 284..346
FT /note="Catalytic subdomain B"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 343
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 329..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 441..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 481..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 522..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 556 AA; 63949 MW; 5AEEB9F0F4ECD148 CRC64;
MRRLVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM
GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV
IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII
RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI
SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV
INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD
SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL
CLDVSRLSGP VIMLKCHHMR GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS
GSRSQQWLLR NMTLGT
