ID A0A2I3SR16_PANTR Unreviewed; 576 AA.
AC A0A2I3SR16; A0A2J8M6H4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=GALNT2 {ECO:0000313|EMBL:JAA10977.1,
GN ECO:0000313|Ensembl:ENSPTRP00000079461.1,
GN ECO:0000313|VGNC:VGNC:11437};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000079461.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000079461.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA10977.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA10977.1}, Skin
RC {ECO:0000313|EMBL:JAA26812.1}, and Smooth vascular
RC {ECO:0000313|EMBL:JAA20234.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000079461.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00000440};
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; AACZ04026622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01000361; JAA10977.1; -; mRNA.
DR EMBL; GABF01001911; JAA20234.1; -; mRNA.
DR EMBL; GABD01006288; JAA26812.1; -; mRNA.
DR RefSeq; XP_003308857.1; XM_003308809.3.
DR STRING; 9598.ENSPTRP00000079461; -.
DR PaxDb; 9598-ENSPTRP00000003539; -.
DR Ensembl; ENSPTRT00000095670.1; ENSPTRP00000079461.1; ENSPTRG00000002093.5.
DR GeneID; 457808; -.
DR KEGG; ptr:457808; -.
DR CTD; 2590; -.
DR VGNC; VGNC:11437; GALNT2.
DR GeneTree; ENSGT00940000156958; -.
DR OrthoDB; 202750at2759; -.
DR TreeFam; TF313267; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000002093; Expressed in fibroblast and 22 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0016266; P:O-glycan processing; IEA:Ensembl.
DR GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IEA:Ensembl.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IEA:Ensembl.
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:SF119; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 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 2: Evidence at transcript level;
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:UP000002277};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..576
FT /note="Polypeptide N-acetylgalactosaminyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015081665"
FT DOMAIN 446..571
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 58..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 65018 MW; 2F1E11B5CD30DACE CRC64;
MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGGG GGGAGRKEDW NEIDPIKKKD
LHHSNGEEKA QSMETLPPGK VRWPDFNQEA YVGGTMVRSG QDPYARNKFN QVESDKLRMD
RAIPDTRHDQ CQRKQWRVDL PATSVVITFH NEARSALLRT VVSVLKKSPP HLIKEIILVD
DYSNDPEDGA LLGKIEKVRV LRNDRREGLM RSRVRGADAA QAKVLTFLDS HCECNEHWLE
PLLERVAEDR TRVVSPIIDV INMDNFQYVG ASADLKGGFD WNLVFKWDYM TPEQRRSRQG
NPVAPIKTPM IAGGLFVMDK FYFEELGKYD MMMDVWGGEN LEISFRVWQC GGSLEIIPCS
RVGHVFRKQH PYTFPGGSGT VFARNTRRAA EVWMDEYKNF YYAAVPSARN VPYGNIQSRL
ELRKKLSCKP FKWYLENVYP ELRVPDHQDI AFGALQQGTN CLDTLGHFAD GVVGVYECHN
AGGNQEWALT KEKSVKHMDL CLTVVDRAPG SLIKLQGCRE NDSRQKWEQI EGNSKLRHVG
SNLCLDSRTA KSGGLSVEVC GPALSQQWKF TLNLQQ
//
