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Database: UniProt
Entry: U5EGM3_9DIPT
LinkDB: U5EGM3_9DIPT
Original site: U5EGM3_9DIPT 
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}.
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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
//
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