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Database: UniProt
Entry: U3K814_FICAL
LinkDB: U3K814_FICAL
Original site: U3K814_FICAL 
ID   U3K814_FICAL            Unreviewed;       667 AA.
AC   U3K814;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=GALNT18 {ECO:0000313|Ensembl:ENSFALP00000011168.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000011168.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000011168.1}
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361242}.
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DR   AlphaFoldDB; U3K814; -.
DR   STRING; 59894.ENSFALP00000011168; -.
DR   Ensembl; ENSFALT00000011213.2; ENSFALP00000011168.1; ENSFALG00000010702.2.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000155456; -.
DR   HOGENOM; CLU_013477_4_0_1; -.
DR   OMA; WHRGNKS; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000016665; 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:0006493; P:protein O-linked glycosylation; 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:SF37; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 18; 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:UP000016665};
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        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   TRANSMEM        69..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          530..659
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   667 AA;  77031 MW;  2DFD2C3A9B6A5A6E CRC64;
     MVGGEYFFIL WIRELSAWRW TDIGVLSVSG KGGEKDFFPS RLIFVFWITG FFGAIWRDLR
     MVCTRKTKTL VSTCVILSGM TNIVCLLYVG WVTNYIASVY VKVQEPISEK KLEEDKGDTL
     RIIERLDHLE NVIKQHIQEA PPKLEENPGE AFTDSSLFAH WGQELSPEHR RLALKQFQYY
     GYNAYLSDRL PLDRALPDLR PSACRNLTFP ENLPEVSIVF IFVNEALSVI LRSIHSAMAR
     TPAHLLKEII LVDDNSNNEE LKEKLQQYVD EVNAHKPGFI KVVRHSRQEG LIRSRVSGWR
     AASAPVVALF DAHVEFNVGW AEPVLTRIKE NRKRVISPSF DNIKYDNFEI EEYPLSAQGF
     DWELWCRYLN PPKSWWKLEN TTAPIRSPAL IGCFIVDREY FQEIGLLDEG MEVYGGENVE
     LGIRVWQCGG SVEVLPCSRI AHIERAHKPY TEDLTAHVRR NALRVAEVWM DEFKSHVYMA
     WNIPQEDSGI DIGDISERKA LRKKLQCKTF RWYLVSVYPE MRMYSDTVAY GVLQNSLKSD
     LCLDQGPDTE NIPIMYICHG MTPQNVYYTS SQQLHVGVLS PTIDDDDNRC LVDVNSRPRL
     IECNYAKAKR MKLYWQFTQG GPIQNRKSKR CLELQENNEN EFGFQLVLQK CTGQRWSITN
     VLRSLSS
//
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