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Database: UniProt
Entry: A0A1S3A4S6_ERIEU
LinkDB: A0A1S3A4S6_ERIEU
Original site: A0A1S3A4S6_ERIEU 
ID   A0A1S3A4S6_ERIEU        Unreviewed;       603 AA.
AC   A0A1S3A4S6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=GALNT9 {ECO:0000313|RefSeq:XP_007529342.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007529342.1};
RN   [1] {ECO:0000313|RefSeq:XP_007529342.1}
RP   IDENTIFICATION.
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_007529342.1; XM_007529280.2.
DR   AlphaFoldDB; A0A1S3A4S6; -.
DR   GeneID; 103119037; -.
DR   CTD; 50614; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   InParanoid; A0A1S3A4S6; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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:SF28; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9; 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, ECO:0000256|RuleBase:RU361242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          465..595
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   603 AA;  67603 MW;  11E6137E25B02889 CRC64;
     MAVARKIKTL LTVNILVFVG IVLFSAYCRL QARSEGLVQL VPGARGGHGQ DGQVGSLGAR
     EAILQRLDHL EEVVYSQLNG LAKPIGLVEG PGGLGQGGVA ATLHEDSAES EGRFEDFGYN
     AQLSARISLD RTIPDYRPKK CRQLAYPQDL PQVSVVFIFV NEALSVILRS VHSVVNRTPS
     QLLKEVILVD DSSDHTELKS SLDRYVRQRY PGLVKVLRTS RREGLIRARL LGWRAATAPV
     VGFFDAHVEF STGWAEPALT RIREDRRRVV LPAIDNIRFD TFEVQQFASA AHGYTWGLWC
     MYITPPRAWL EQGDEAAPIR TPAMIGCSFM VDREYFRDIG LLDPGMEVYG AENIELGMRV
     WQCGGSMEVL PCSRVAHIER SRKPYSSDID YYAKRNALRT AEVWMDGFKS HVYMAWNLPL
     ANPGVDFGDV SERQALRQRL KCRSFQWYLE NVYPEMRTYN DTLTYGEVRN SKASGYCLDQ
     GAEDDDQAIL YPCHGMSSQL VRYSTAGLLQ LGPLGSTAFL PDAKCLVDEG LTHTPALRSC
     EDVARPSQRL WDFTQGGPIV SRDSGRCLEV EVSKDAHFGL RLVVQRCSGQ KWTIRNWIKP
     PRH
//
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