ID A0A401S3W2_CHIPU Unreviewed; 597 AA.
AC A0A401S3W2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=chiPu_0003463 {ECO:0000313|EMBL:GCC25058.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC25058.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC25058.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004447}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680,
CC ECO:0000256|RuleBase:RU361242}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:GCC25058.1}.
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DR EMBL; BEZZ01000074; GCC25058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401S3W2; -.
DR STRING; 137246.A0A401S3W2; -.
DR OMA; VAEVWMC; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
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:SF123; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000287033};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT TRANSMEM 43..68
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 464..589
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 597 AA; 67989 MW; 370D6DCA62FEBA13 CRC64;
MRPVAGAGAA AAAVMMMMVL LLGGMEGECQ SIHPHPVRVL LRLFAYCKVV LATSLVWMLL
DMFLLLYFSE CNKCEEKKER GLPAREDVIQ KPQEGPGEMG KPVIISKENQ EKMKEMFKIN
QFNLMASDMI ALNRTLPDVR LDGCKTKVYP DGLPKTSVVI VFHNEAWSTL LRTVHSVIIR
SPRHLLEEII LVDDASERDF LNKPLEKYVK KLQVPIKILR MEQRSGLIRA RLKGAAASTG
QVITFLDAHC ECTQGWLEPL LARIKLDRST VVCPIIDVIS DDTFEYMAGS DMTYGGFNWK
LNFRWYPVPQ REMDRRKGDR TIPVRTPTMA GGLFSIDRDY FELIGTYDAG MDIWGGENLE
ISFRIWQCGG TLEIVTCSHV GHVFRKATPY TFPGGTGQII NKNNRRLAEV WMDDFKNFFY
IISPGVTKVE YGDITARKTL RQKLSCKPFS WYLENVYPDS HIPRHYFSLG EIRNVETNQC
LDNMARKENE KVGIFNCHGM GGNQVFSYTA NKEIRTDDLC LDVSKLNGPI MMLKCHHLKG
NQLWEHDPVK LTLVHVNSNQ CLDKSTEADS QVPTMKDCNG SRSQQWILRN VTLPEVF
//
