ID A0A194RMQ9_PAPMA Unreviewed; 708 AA.
AC A0A194RMQ9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=RR48_10653 {ECO:0000313|EMBL:KPJ18709.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ18709.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ18709.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ18709.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ18709.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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; KQ459989; KPJ18709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194RMQ9; -.
DR InParanoid; A0A194RMQ9; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053240; 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:SF140; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 5; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|RuleBase:RU361242, ECO:0000313|EMBL:KPJ18709.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 567..690
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 708 AA; 80471 MW; 3C5C351EB6452064 CRC64;
MFRSKIRIHT CRIILLTSLV WLLVDVALLA IYSDCFGDGC SKKTSEVVVR SKDTEDLRGK
RGAIAAGLRS KVEDEETNLE ENELEQDIGD DGLMLPPYPK SRLKRWSVVP PVRPQGDSPG
EMGKAVNIPI EQEKLMLDKF QENQFNLLAS DMISLNRSLT DVRFEKCKGK QYPDLLPTTS
VVIVFHNEAW TTLIRTIWST INRSPRPLLK EIILVDDASE KEHLGKKLED YIKTLPVPTH
LFRTENRSGL IRARLLGAKH VQGDVITFLD AHCECTEGWL EPLLARIVED RTTVVCPIID
VISDTTFEYI QASDMTWGGF NWKLNFRWYR VPEREMSRRG GDRTAPLRTP TMAGGLFAID
REYFYKIGSY DEGMDIWGGE NLEMSFRVWQ CGGSLEIVPC SHVGHVFRDK SPYSFPGGVQ
NIVLHNAARV AEVWMDEWGE FYYAMNPALG VRDVSGDVVV GRAGQVWQCG GRLEIAPCAH
VGHVFRKTTP YSFPGGTGRV VNHNNARLAE VWLDEWKHFY YNINPGALNV PVGDVSERKA
LRQRLKCKSF RWYLENIYPE SQMPLDYYFL GEIRNAETSN CLDTLGGKAG QPLGMGYCHG
MGGNQVFAYT KRKQIMSDDN CLDAAHPRGP VKLIRCHGMR GNQEWTYDVK TRTIKHSNTG
MCLEKPESGD VWKPVLRPCS RARGQQWLMQ VDFKWQARHG SRLADRPS
//
