ID   Q08DM9_BOVIN            Unreviewed;       556 AA.
AC   Q08DM9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361242};
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
GN   Name=GALNT13 {ECO:0000313|EMBL:AAI23663.1};
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 {ECO:0000313|EMBL:AAI23663.1};
RN   [1] {ECO:0000313|EMBL:AAI23663.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI23663.1};
RC   TISSUE=Cerebral cortex {ECO:0000313|EMBL:AAI23663.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (SEP-2006) 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 residue to a
CC       serine or threonine residue on the protein receptor. Has a broad
CC       spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-
CC       derived peptides. {ECO:0000256|ARBA:ARBA00045388}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU361242};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361242}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU361242}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU361242}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004447}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000256|ARBA:ARBA00005680,
CC       ECO:0000256|RuleBase:RU361242}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00174}.
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DR   EMBL; BC123662; AAI23663.1; -; mRNA.
DR   RefSeq; NP_001070354.1; NM_001076886.1.
DR   AlphaFoldDB; Q08DM9; -.
DR   SMR; Q08DM9; -.
DR   STRING; 9913.ENSBTAP00000049644; -.
DR   PaxDb; 9913-ENSBTAP00000049644; -.
DR   GeneID; 532545; -.
DR   KEGG; bta:532545; -.
DR   CTD; 114805; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005562; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000158904; -.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   OrthoDB; 330637at2759; -.
DR   Reactome; R-BTA-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   Bgee; ENSBTAG00000005562; Expressed in adenohypophysis and 51 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   CDD; cd23467; beta-trefoil_Ricin_GALNT13; 1.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   FunFam; 2.80.10.50:FF:000014; Polypeptide N-acetylgalactosaminyltransferase; 1.
DR   FunFam; 3.90.550.10:FF:000005; Polypeptide N-acetylgalactosaminyltransferase; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00174}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361242};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU361242};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000256|PROSITE-
KW   ProRule:PRU00174};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361242};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361242};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361242}.
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          427..550
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   DISULFID        441..458
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00174"
SQ   SEQUENCE   556 AA;  64063 MW;  8AFC23FC9CAD4DCB CRC64;
     MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM
     GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTRVY PDELPNTSVV
     IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KNLEVPVKII
     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
     CLDVSRLNGP VIMLKCHHMR GNQLWEYDAE RLTLRHVNSN QCLDEPSEED KMVPTMQDCS
     GTRSQQWLLR NMTLGA
//