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   24-JAN-2024, entry version 119.
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   GlyCosmos; Q6UE39; 3 sites, No reported glycans.
DR   GlyGen; Q6UE39; 3 sites.
DR   PhosphoSitePlus; Q6UE39; -.
DR   PaxDb; 10116-ENSRNOP00000042772; -.
DR   Ensembl; ENSRNOT00055002491; ENSRNOP00055001878; ENSRNOG00055001533.
DR   Ensembl; ENSRNOT00060013254; ENSRNOP00060010066; ENSRNOG00060007989.
DR   Ensembl; ENSRNOT00065013110; ENSRNOP00065009689; ENSRNOG00065008243.
DR   GeneID; 311039; -.
DR   KEGG; rno:311039; -.
DR   UCSC; RGD:735044; rat.
DR   AGR; RGD:735044; -.
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   OrthoDB; 202750at2759; -.
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 cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; 2.80.10.50; -; 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   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF47; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 13; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   Genevisible; Q6UE39; RN.
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
//