UniProt: A0A3B3XWF5

Database: UniProt
Entry: A0A3B3XWF5_9TELE

LinkDB:  A0A3B3XWF5_9TELE 
Original site:  A0A3B3XWF5_9TELE

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Ontology (4)   
   GO (4)   
Gene (4)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (18)   

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ID   A0A3B3XWF5_9TELE        Unreviewed;       571 AA.
AC   A0A3B3XWF5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000019248.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000019248.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_014852655.1; XM_014997169.1.
DR   AlphaFoldDB; A0A3B3XWF5; -.
DR   STRING; 48701.ENSPMEP00000019248; -.
DR   Ensembl; ENSPMET00000028592.1; ENSPMEP00000019248.1; ENSPMEG00000022290.1.
DR   GeneID; 106923835; -.
DR   CTD; 114805; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000261480; Unplaced.
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:SF47; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 13; 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   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        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          427..551
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   571 AA;  65777 MW;  D10BD0D37CE532C4 CRC64;
     MRRFVYCKVV LTTSLVWVLV DVFLLLYFSE CNKCDERKDR SLLPALRAVI SRSHEGPGEM
     GKAVNIPKDD QGKMKELFKI NQFNLMASDL IALNRSLPDV RLDGCKTKVY PDDLPNTSIV
     IVFHNEAWST LLRTVHSVIN RSPRHLLVEI VLVDDASERD FLRAKLEDYV RTLEVPVKIL
     RMEQRSGLIR ARLRGAAVTT GQVITFLDAH CECTVGWLEP LLARIREDRR AVVCPIIDVI
     SDETFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDKT
     YFEEIGSYDP GMDIWGGENL EMSFRIWQCG GSLEIITCSH VGHVFRKATP YSFPGGTGQV
     INKNNRRLAE VWMDEFKDFF YIISPGVMRV DYGDVSSRKA LREALKCKPF SWYLENIYPD
     SQIPRRYFSL GEIRNVETNQ CVDNMGRKEN EKVGFFNCHG MGGNQVFSYT ADKEIRTDDL
     CLDVSRLNGP VKMLKCHHMK GNQMFEYDAE KHTFLHIITQ SCLTISRLED GTYGPTVEYC
     NNSPLQAWIL HNYTRLEVAR HLYFSPTDYI L
//

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