ID A0A3B4CHU9_PYGNA Unreviewed; 1023 AA.
AC A0A3B4CHU9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644};
DE EC=2.4.1.41 {ECO:0000256|ARBA:ARBA00012644};
GN Name=GALNT5 {ECO:0000313|Ensembl:ENSPNAP00000010064.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010064.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000010064.1}
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680}.
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DR RefSeq; XP_017547015.1; XM_017691526.1.
DR AlphaFoldDB; A0A3B4CHU9; -.
DR STRING; 42514.ENSPNAP00000010064; -.
DR Ensembl; ENSPNAT00000035570.1; ENSPNAP00000010064.1; ENSPNAG00000015565.1.
DR GeneID; 108423898; -.
DR GeneTree; ENSGT00940000159241; -.
DR OMA; KWEFTRY; -.
DR OrthoDB; 202750at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C: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:SF130; 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; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 894..1018
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 104..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 113719 MW; C92A693903695525 CRC64;
MKLRKYFRGS GRVFAFVFVA SVVWLLFDMA ALKLSISEVN TELLKELVVK ERELNKRQAT
KGAKVADRDF KHPLQKVQAD LGEGKKSDSF ETKVIEVYRK PGRFRGNVEP KKDNATLTGP
KGGERTGVNE KKREENSLKK HNSGKDTAVR NPIPPQQQAR TGTKEKEGRI APSHTKAPPA
VREEKRPQEV LEEKTVKLQG SETKDTEVGL AQDTKVGLAP DTKVGLAPDA KVGLAQDTKV
GLAQDTKVGL AQDTKVGLAQ DTKVGLAQDT KVGLAQDTKV GLAQDTKVGL AQDTKVGLAQ
DTKVGLAQDT KVGLAQDTKV GLAQDTKVGL AQDTKVGLAQ DTKVGLAQDT KVGLAQDTKV
GLAQDTKVGL AQDTKVGLAQ DTKVGLAQDT KVQDIKIPVD SGLLKKTNNN STLKTAKQGA
RPTASAKKGI TVIPIQRLHE GKGVIVFKND KHIKKNDLAQ VLLEDKHKSS QQDGALNPGK
LPAGEPVKLL NASVVRRSAG LHKVMALDVT VRPRDVRAIG QFGHAAVVPL DRQEESRRRW
SEGYFNVFLS EQIPVDRAIP DTRPPACSEN LVHDHLPTTS VIFCFVDEVW STLLRSVHSV
LNRSPPHLLK EVLLVDDSST KDYLKEKLDV YMSQFPKVRI IRLKERQGLI RARLAGAAEA
KGDVLTFLDS HVECNVGWLE PLLERLYNDR RKVVCPVIDV ISDKDMSYVL VDSFQRGIFK
WPLVFGWSTL PEDYVKKKHM KDSDPIRCPV MAGGLFSIDK KYFYELGAYD PGLDVWGGEN
MEISFKIWMC GGEIEIIPCS RVGHIFRGEN PYQFPKDRQK TVERNLARVA EVWLDEYKEV
FYGYGYLHLL DKNVIDVGNL TAQIQLREKL KCKSFKWYLD NVYPELEAPE VKAEGLVFNV
GTRKCLALNN GSLSFEICDL SKQSQHFNYS WVRTVRQNAF CVAPLGTGTG MTMEQCDNTK
PHLRWLHKAN KVLPEHLIAE VSPRGMFQRV CLEGGPKADS VYLKACDTSS PFQKWQFTHY
YAQ
//
