ID U5EGM3_9DIPT Unreviewed; 631 AA.
AC U5EGM3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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};
DE Flags: Fragment;
OS Corethrella appendiculata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Chaoboridae;
OC Corethrella.
OX NCBI_TaxID=1370023 {ECO:0000313|EMBL:JAB56486.1};
RN [1] {ECO:0000313|EMBL:JAB56486.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:JAB56486.1};
RA Ribeiro J.M.C., Chagas A.C., Pham V.M., Lounibos L.P., Calvo E.;
RT "An insight into the sialome of the frog biting fly, Corethrella
RT appendiculata.";
RL Insect Biochem. Mol. Biol. 44:23-32(2014).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361242};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU361242}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU361242}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GANO01003385; JAB56486.1; -; mRNA.
DR AlphaFoldDB; U5EGM3; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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:SF63; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE; 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|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|RuleBase:RU361242};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|RuleBase:RU361242, ECO:0000313|EMBL:JAB56486.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 502..629
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB56486.1"
SQ SEQUENCE 631 AA; 72636 MW; 6573EA6F0D6B36B4 CRC64;
IMGKSFFYGI IVASVTWSIV VYLYWTLTST TDSVKTTSLS LTSLNNDFDK KNHLHSNNIN
LLANDDVHSK ANVDKSINLF KEKFKRYKKE KKDREISRRL IEELKPILPN GTDEFGMVKN
SEEQFIRDIG YRKHAFNVLV SNKIGLIRDI PDTRHHLCSK LLYDQPLPTA SIVMCFYNEH
LMTLVRSVNT ILKRTPDQLL KEIILVDDFS DLDDLQNELD KKINELNSNK IKLLRNLKRE
GLMRSRVYGA RSASGDVVVF LDSHIEVNTK WIEPLLSRIK TNRTILTMPV IDIINSDTFS
YSKSPLVRGG FNWGLHFKWD NLPKGTLNKD LDFIGPFASP TMAGGLFAID RNYFQEIGEY
DMGMDIWGGE NLEISFRTWQ CGGSIELHPC SRIGHVFRKR RPYGAPNGVD TMIRNSLRLA
NVWMDDYKDF FMKQQPTAKN IAYGDISERK ELRLKLKCKP FSWYLKNIYP ELEIPGEKHS
NKTLSMPAFE PWHSRKRNYT NNFQIRLTNT TLCLTTIGLK EKSLWKKGSL LELNPCLRVK
KQMWYETERN ELILAQLLCL EAPNNSVVPI INKCHEMGAD QEWKHRKSNG TPIYNLAAGT
CLKAKSATKS SSVHLSICSN DPLSTWDLVG F
//