ID A0A084WIB1_ANOSI Unreviewed; 608 AA.
AC A0A084WIB1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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};
GN ORFNames=ZHAS_00017991 {ECO:0000313|EMBL:KFB49955.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB49955.1};
RN [1] {ECO:0000313|EMBL:KFB49955.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC017991-PA}
RP IDENTIFICATION.
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}.
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; ATLV01023925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525347; KFB49955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084WIB1; -.
DR STRING; 74873.A0A084WIB1; -.
DR EnsemblMetazoa; ASIC017991-RA; ASIC017991-PA; ASIC017991.
DR VEuPathDB; VectorBase:ASIC017991; -.
DR VEuPathDB; VectorBase:ASIS014020; -.
DR OMA; DHSNFNY; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000030765; 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:SF134; N-ACETYLGALACTOSAMINYLTRANSFERASE 4-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, ECO:0000256|RuleBase:RU361242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 461..589
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 608 AA; 69871 MW; 5ED25791224E3AB0 CRC64;
MRRNLRTLVK YVFVSGGVLL FLTLIIRSFS VDSKAQSLNG LFGQAESLLQ HARQGSFFNE
PAKNVHQKRI DWHNYELIHE EAKRVGIGEQ GKAGHLSEKE AEMKDKLFKK NGFNAVLSDL
ISLNRSLPDI RHRGCRKKQY LSELPTVSVV VPFYNEHWST LLRTAASVLL RSPPELIAEV
ILVDDCSTKE FLKDQLDQFV AENMPKVKIV RLPERSGLIT ARLAGAKVAT ADVLIFLDSH
TEANVNWLPP LLEPIAEDYR TCVCPFIDVI DWDNFEYRAQ DEGARGAFDW KFFYKRLPLL
PKDLQNPTEP FESPVMAGGL FAISAKFFWE LGGYDEGLDI WGGEQYELSF KIWQCGGRMY
DAPCSRVGHI YRGYAPFGNP RKKDFLTRNY KRVAEVWMDE YKEYLYMRDP KKYENTDVGD
ISKQLAIREK LQCKPFKWFM THVAFDLVEK YPPIEPPDFA NGAIQSVAHP ALCVDTLNNG
EKGTIGLYSC AEDKKQPQSN QFFQLSWHRD LRIKFGEMCW DVSESVPNAK ILLYHCHGGQ
GNQLWRYEPD SQMLKQGKNN RCLDMDPNTR AVFVNPCDGA NPRQKWRWGF VNTTSIDQWD
TYGAKVIE
//
