ID K9ILB6_DESRO Unreviewed; 559 AA.
AC K9ILB6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA48205.1};
RN [1] {ECO:0000313|EMBL:JAA48205.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA48205.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
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 EMBL; GABZ01005320; JAA48205.1; -; mRNA.
DR AlphaFoldDB; K9ILB6; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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:SF123; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 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,
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 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 426..551
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 64144 MW; FA53A48CDCE5F40E CRC64;
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV
VIVFHNEAWS TLLRTVHSVT DRSPRHMLEE IVLVDDASER DFLKRPLESY VKKLKVPVHV
IRMEQRSGLI RARLKGASVS KGQVITFLDA HCECTVGWLE PLLARIKQDR KTVVCPIIDV
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDVASRI GLRHKLQCKP FSWYLENIYP
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATED DSQVPSIRDC
TGSRSQQWLL RNVTLPEIF
//
