ID A0A087XI24_POEFO Unreviewed; 568 AA.
AC A0A087XI24;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 52.
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};
GN Name=GALNT16 {ECO:0000313|Ensembl:ENSPFOP00000005427.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000005427.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000005427.2}
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 EMBL; AYCK01013018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01013019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007569541.1; XM_007569479.2.
DR AlphaFoldDB; A0A087XI24; -.
DR STRING; 48698.ENSPFOP00000005427; -.
DR Ensembl; ENSPFOT00000005436.2; ENSPFOP00000005427.2; ENSPFOG00000005089.2.
DR GeneID; 103150045; -.
DR KEGG; pfor:103150045; -.
DR CTD; 57452; -.
DR eggNOG; KOG3738; Eukaryota.
DR GeneTree; ENSGT00940000158846; -.
DR OMA; VKMELCN; -.
DR OrthoDB; 202750at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000028760; 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: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:SF3; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 16; 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:UP000028760};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 444..565
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 32..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64431 MW; 5A6C7D17D49C07A1 CRC64;
MRRIRANAIA ILTVAWILGT FYYLWQDSKP ASTPSSSASQ ARGRGHGQKL VPGRLEIHRD
DRTIPLIVTQ PPRGEQQSQL LGGFDEKTYL AAKQLKPGDD PYREHAFNLQ ESDRLGSERA
IRDTRHYRCA SLTYDAELPS TSIIITFHNE ARSTLLRTIK SVLMRSPPSL IQEIILIDDF
STDPEDCQLL SQIPKVRCLR NSRREGLIRS RVRGANTASA TILTFLDSHC EVNADWLQPM
IQRVKEDHTR VVSPIIDVIS LDNFAYLAAS ADLRGGFDWS LHFKWEQIPI EQKMARSDPT
QPIRTPVIAG GIFVMDKSWF NHLGQYDTHM DIWGGENFEL SFRVWMCGGS LEILPCSRVG
HVFRKRHPYD FPEGNALTYI KNTRRAAEVW MDEYKQYYYS ARPSAQGKAF GSIADRLTLR
RKLNCKPFRW YMENVYPELR VPEQEAVSSV LKQGGMCLET RGRDGLGLAE CRGAGTNRPQ
SQKWELVEPL IRQQDLCLAI SAFTAGSKVK MELCNSKEPR QKWKPKGPAL QHMVSGLCLD
SQSTSGPLVI AQCRPQVAGQ SWEPQVII
//
