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Database: UniProt
Entry: A0A452SMM3_URSAM
LinkDB: A0A452SMM3_URSAM
Original site: A0A452SMM3_URSAM 
ID   A0A452SMM3_URSAM        Unreviewed;       622 AA.
AC   A0A452SMM3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644, 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=GALNT6 {ECO:0000313|Ensembl:ENSUAMP00000033852.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000033852.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000033852.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000256|ARBA:ARBA00005680,
CC       ECO:0000256|RuleBase:RU361242}.
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DR   AlphaFoldDB; A0A452SMM3; -.
DR   STRING; 9643.ENSUAMP00000033852; -.
DR   Ensembl; ENSUAMT00000037703.1; ENSUAMP00000033852.1; ENSUAMG00000025782.1.
DR   GeneTree; ENSGT00940000160845; -.
DR   OMA; SWFLHNI; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018243; P:protein O-linked glycosylation via threonine; IEA:Ensembl.
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:SF58; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 6; 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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|RuleBase:RU361242};
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|RuleBase:RU361242};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361242};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          496..622
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          101..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  70829 MW;  94BDFDD3E61CD09A CRC64;
     MRLLRRRHMA LRLAMVGSAF VLFLFILHRD VSSTEQATEK PWLKSLVSQK DHVLDLMLGA
     VHNLRDSMPK LQIRAPEPQE TPVSANQSCL PGFYTPAELK PFWERPPQDP NSPGADGKAF
     QKDKWTPVET QEKEEGYKKH CFNAFASDRI SLQRALGPDT RPPECVDQKF RRCPPLPTTS
     VIIVFHNEAW STLLRTVYSV LHTSPAILLR EIILVDDAST DDYLKDQLEQ YVKTLQVVRV
     VRQEERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEEE TAVVSPDIVT
     IDLNTFEFSK PVPSGRIHSR GNFDWSLTFG WEALPAHEKQ RRKDETYPVK SPTFAGGLFS
     ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHSFPKG
     ISVIARNQVR LAEVWMDGYK EIFYRRNMQA AKMAQEKSFG DISERLKLRE QLHCHNFSWF
     LTNIYPEMFV PDLKPTFYGA IRNLGINQCL DVGENNHGGK PLIMYTCHGL GGNQYFEYTT
     QRDLRHNIAK QLCLHASAGT LGLRSCHFTG KNSQVPKDEE WELTQDQLIR NSGSGTCLTS
     EDKKPAMASC NPSDPHQHWI FN
//
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