ID G3SSK4_LOXAF Unreviewed; 940 AA.
AC G3SSK4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=GALNT5 {ECO:0000313|Ensembl:ENSLAFP00000002942.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002942.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000002942.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002942.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000002942.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002942.3};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; G3SSK4; -.
DR STRING; 9785.ENSLAFP00000002942; -.
DR Ensembl; ENSLAFT00000003530.3; ENSLAFP00000002942.3; ENSLAFG00000003531.3.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000159241; -.
DR HOGENOM; CLU_013477_1_0_1; -.
DR InParanoid; G3SSK4; -.
DR OMA; HGMHHVL; -.
DR TreeFam; TF313267; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000007646; 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: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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 809..935
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 134..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 107124 MW; B229419030D624EE CRC64;
MNKIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVLKEDIR RERTGFRVQP
GQMKIFYSNI KETKLPLRWN RKGTLGKENF GKTKESVHKV EDDLDQTWRE RKEQNAPGRG
KAVPLWHPAR LQTLPVTPTK QKTEGPDIKH EMSSHQVRPK QTTARGAQKT PFGEARGTSL
VKISVHTGPV DVNQKVLKSH TVTSDASKEA VETDLNVTVS LNTDRPKQQS QTVANKRTLP
GSPPVPKSGE TLALSKTEIQ SKELNTNKQK ANKGLLFSKF TVSSNRLKKQ SINETQVEGL
PKDERAKLAL GKKLNFSESH VVIITKEEEL KTDTKDVTNS KTKTVFPKVK GESQEKLISR
NRSEASFSSL ALQRATMSEA NQSLAEGLRP AKINLTDKAQ PAEQNLSHVK AHLVEDHGMH
HVLRIDVTLS PRDPKAPGQF GRPVIVPHGK EKEAKRRWKE GNFNVYLSDL IPVDRAIEDT
RPTGCAEQLV HSNLPTTSVI MCFVDEVWST LLRSVHSVLN RSPPHLIKEI LLVDDFSTKD
YLKDNLDKYM SQFPKVRILR LKERHGLIRA RLAGAQNATG DVLTFLDSHV ECNIGWLEPL
LERVYLSRKK VACPVIEVIN DKDMSYMTVD NFQRGVFVWP MNFGWRTIPP DVVAKNRIKE
TDVISRCPVM AGGLFSIDKN YFFELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR
VGHIFRNDNP YTFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ
RELRRKLKCK SFKWYLENVF PDLKAPIVKA GGVLINVALD KCISIENTTA ILEDCDASSK
FQQFNYTWLR LIKHGDWCLA PIPDTGTLRL HPCDNRNKGL KWLHKSTSVF HPELVDHIVF
ENYHQLLCLE GNFPEKTMKA ATCDPKKPNQ KWRFEKYYED
//