ID J3S9A5_CROAD Unreviewed; 608 AA.
AC J3S9A5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644, ECO:0000256|RuleBase:RU361242};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361242};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729 {ECO:0000313|EMBL:AFJ50973.1};
RN [1] {ECO:0000313|EMBL:AFJ50973.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:AFJ50973.1};
RX PubMed=23025625; DOI=10.1186/1471-2164-13-312;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [2] {ECO:0000313|EMBL:JAI12003.1}
RP NUCLEOTIDE SEQUENCE.
RA Margres M.J., Wray K.P., McGivern J.J., Seavy M., Sanader D., Facente J.,
RA Rokyta D.R.;
RT "The extremes of toxin expression variation revealed in two sympatric snake
RT species.";
RL Submitted (MAY-2014) 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|ARBA:ARBA00004922, 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}. 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; JU175449; AFJ50973.1; -; mRNA.
DR EMBL; GBEX01002557; JAI12003.1; -; mRNA.
DR AlphaFoldDB; J3S9A5; -.
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:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
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|ARBA:ARBA00022676,
KW 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, 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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 476..607
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 608 AA; 69696 MW; 4EA0B6D03530EB40 CRC64;
MGSVTLRYFC YGCLFTSVTW TVLLFVYFNF SEETQSFKNV PIKGLEPQKP LSRRFHPQLV
NGRGQMQESK PRYGKIRNPL GNAAQDLPKS DTEFSPEMGM IFNEQDQEVR DLGYQKHAFN
VLISNRLGYH RDVPDTRDRK CKEKIYPHDL PSASIIICFY NEAFSALLRT IHSVLDRTPS
HLLHEIILVD DRSELADLKE DLDIYLTKDL PNKVKLVRNE NREGLIRGRM VGASHATGKV
LVFLDSHCEV NEMWLQPLLT PIQESRRTVV CPVIDIISAD TLTYSSSPVV RGGFNWGLHF
KWDLVPLLEM EGPEQATAPI KSPTMAGGLF AMDREYFNAL GQYDSGMDIW GGENLEISFR
IWMCGGKLVI IPCSRVGHIF RKRRPYGSPG GQDTMAHNSL RLAHVWMDEY KEQYFALRPE
LRTRNYGNIT DRVELRKKLN CKSFKWYLDN VYPEMQISGP NAKVQPPIFF NKGQKRPKLL
QQGRLYHLQT NKCLVAQSNP SQKGGLVVVK ECDYSNKNQI WMYNEDHELI LNNLLCLDVS
ETRTSDPPRL MKCHGSGGSQ QWLLGKNNRL YQVSVGQCMK VVDPLNLKGY VTMAICDGSS
LQQWRLEN
//
