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Database: UniProt
Entry: A0A1S3FCM0_DIPOR
LinkDB: A0A1S3FCM0_DIPOR
Original site: A0A1S3FCM0_DIPOR 
ID   A0A1S3FCM0_DIPOR        Unreviewed;       623 AA.
AC   A0A1S3FCM0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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|RefSeq:XP_012874231.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012874231.1};
RN   [1] {ECO:0000313|RefSeq:XP_012874231.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012874231.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_012874231.1; XM_013018777.1.
DR   AlphaFoldDB; A0A1S3FCM0; -.
DR   STRING; 10020.ENSDORP00000014397; -.
DR   GeneID; 105987510; -.
DR   KEGG; dord:105987510; -.
DR   CTD; 11226; -.
DR   InParanoid; A0A1S3FCM0; -.
DR   OMA; SWFLHNI; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000081671; Unplaced.
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:UP000081671};
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..623
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   623 AA;  71456 MW;  621B6A2C194EE009 CRC64;
     MRLLRRRHMP LRLAMVGSAF MFFLFIRQKD VSSKEQATEK PWLKSLVGQK DHVLDLMLGA
     VNNFRDSMPK LQIGAPEPQQ PVLSTNQSCL PGFYTHAELK PFWERPPQDP NSPGADGYAF
     KKSKWTPLEI QEKEDGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLPTTS
     VIIVFHNEAW STLLRTVYSV LHTSPAIFLK EIILVDDAST EEYLKEKLER YVQQLQIVRV
     VRQEERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT
     IDLNTFKFSK PVQTGRVHSR GNFDWSLTFG WETLPAHEKQ RRKDETYPIK SPTFAGGLFS
     ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG
     TSVIARNQVR LAEVWMDNYK KIFYRRNLQA AKMAQEKSFG DISERLQLRE QLHCRNFSWF
     LHNIYPEMFV PDLNPTFYGA IKNLGTEQCL DVGENNRSGG KPLIMYFCHG LGGNQYFEYT
     TQKDLRHNIA KQLCLHASDS TLGLRSCHFT GKNSQVPKDE EWEFTQDQLI RNSGSGTCLT
     SQDKKPAMAP CNPRDPHQLW LFV
//
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