ID A0A0V1MTX5_9BILA Unreviewed; 346 AA.
AC A0A0V1MTX5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 Name=gly-10 {ECO:0000313|EMBL:KRZ75071.1};
GN ORFNames=T10_8941 {ECO:0000313|EMBL:KRZ75071.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ75071.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ75071.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ75071.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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|RuleBase:RU361242}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU361242}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU361242}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|RuleBase:RU361242}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ75071.1}.
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DR EMBL; JYDO01000042; KRZ75071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MTX5; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
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|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|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361242};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Transferase {ECO:0000256|RuleBase:RU361242, ECO:0000313|EMBL:KRZ75071.1}.
FT DOMAIN 224..346
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 346 AA; 40697 MW; 00A82EE9DDAB2ED1 CRC64;
MFMDAHSEVG YNWLPPLLEP IKLHYRTVTC PFIDVIDCDT FAFRAQDEGA RGSFDWKFHY
KRLPLLNNTG AEPFESPIMA GGYFAISKRW FDELGRYDDQ LMIWGAEQYE LSFKLWQCHG
RMIDIPCSRI AHIYRCKYAP FEDPGIGNFL ERNYKRVAET WMDEYKEYLY LRLPRLRNVD
PGDLTKQRKV RQRLKCNGFD WFMKNVMFDQ PKHYPLVEPP DVMSGRIKNK RTGRCIDVQN
AGLQPELTTS QCKDYLKRQE FVLSWRSEIF QRLGENCLDS MNHGLRGTVH LFACHGGGGN
QNWTYSLNTT MHLQMTASNL CLDTDNTGRL FLNTCHLVDS QQWFWS
//