ID A0A182SLY8_9DIPT Unreviewed; 574 AA.
AC A0A182SLY8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 Anopheles maculatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; Anopheles maculatus group.
OX NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM009403-PA, ECO:0000313|Proteomes:UP000075901};
RN [1] {ECO:0000313|Proteomes:UP000075901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles maculatus species B.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMAM009403-PA}
RP IDENTIFICATION.
RC STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM009403-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182SLY8; -.
DR EnsemblMetazoa; AMAM009403-RA; AMAM009403-PA; AMAM009403.
DR VEuPathDB; VectorBase:AMAM009403; -.
DR OrthoDB; 3447101at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000075901; Unassembled WGS sequence.
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:SF131; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9-RELATED; 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|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};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|RuleBase:RU361242};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 454..567
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 574 AA; 65372 MW; C26D92D5B4EA6472 CRC64;
MKLLKRCFLQ NTCLVFSLVA LTYWIVTVEH DPANETAALE KELSYILNNA GDPARAFDPN
GTPGDMGMPV ILPEELSPEL SALVRKGWNE QGLNQFVSDM IPLRRRLPDV RDGWCRSEEQ
ARRERNIGPG TLPPSAIVIV FYNEAWSVLL RTVHSVIDRT PTELIDEIVL VDDCSTMNHL
KGQLDSYIAS LDKVRLVRSS ERLGLIRARL LGAKSTTANI ITFLDAHCEV IEGWLEALIA
HVASDETMIA IPAIDWIHEN TLALNAQSSV KYFGSFDWSL NFQWHARERR LKESSKNGTV
FIHPAAPYDT PTMAGGLFTI HRTFFQRLGW YDEGMEIYGG ENMELSFKAW MCGGKLQIVA
CSRVAHIQKR GHPYLREIVG GLALVKRNSI RLAEVWLDEY ADYYYETFGG RAKRGNFGDV
SARKALRQQL QCKPFRWYLE HVFPEQFDPS KAVAHGEIRF GGKTQYPLCL DWPTQLTLIG
CHGTGGHQLW YLTKQGEVTR DDNCLDYDGK ALVMYRCHGM GGNQAWSWDP DSKLLKKLSF
DRCLQWDRNF SLTVCDPNEP SQKWMMQNFK PNNL
//
