ID H2QIU5_PANTR Unreviewed; 940 AA.
AC H2QIU5; A0A2J8PPS5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 81.
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|EMBL:JAA26756.1,
GN ECO:0000313|Ensembl:ENSPTRP00000021450.2,
GN ECO:0000313|VGNC:VGNC:10822};
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:ENSPTRP00000021450.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000021450.2, 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:JAA26756.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA35646.1}, and Skin
RC {ECO:0000313|EMBL:JAA26756.1};
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:ENSPTRP00000021450.2}
RP IDENTIFICATION.
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 EMBL; AACZ04058430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABD01006344; JAA26756.1; -; mRNA.
DR EMBL; GABE01009093; JAA35646.1; -; mRNA.
DR RefSeq; XP_525944.2; XM_525944.5.
DR STRING; 9598.ENSPTRP00000021450; -.
DR PaxDb; 9598-ENSPTRP00000021450; -.
DR Ensembl; ENSPTRT00000023260.3; ENSPTRP00000021450.2; ENSPTRG00000012550.3.
DR GeneID; 470563; -.
DR KEGG; ptr:470563; -.
DR CTD; 11227; -.
DR VGNC; VGNC:10822; GALNT5.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000159241; -.
DR HOGENOM; CLU_013477_1_0_1; -.
DR OrthoDB; 202750at2759; -.
DR TreeFam; TF313267; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012550; Expressed in lung and 6 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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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 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-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 129..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 106597 MW; E0B089D15F04FBB3 CRC64;
MNRIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTRVIKEDIV RRERIGFRVQ
PDQGKIFYSS IKEMKPPLRG HGKGAWGKEN VRKTEESVLK VEVDLDQTQR ERKMQNALGR
GKVVPLWHPA HLQTLPVTPN KQKTDRRGTK PEASSHQGTP KQMTAQGAPK TSFIAAKGTQ
VVKISVHMGR VSLKQEPRKS HSPSSDTSKL AAERDLNVTI SLSTDRPKQR PQAVAKERAH
PASTAVPKSG EVMALNKTKT QSKEVNANKH KANTSLPFPK FIVNSNRLRK QSINETPLGS
LPKDDGARGA HGKKLNFSES HLVIITKEEE QKADPKEVSN SKTKTIFPKV LGKSQSKHIS
RNRSEMSFSS LAPHRVPLSQ TNHALTGGLE PAKINITAKA PPTEYNQSHI KALLPEDSGM
HQVLRIDVTL SPRDPKAPGQ FGRPVVVPHG KEKEAERRWK EGNFNVYLSD LIPVDRAIED
TRPAGCAEQL VHNNLPTTSV IMCFVDEVWS TLLRSVHSVL NRSPPHLIKE ILLVDDFSTK
DYLKDNLDKY MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP
LLERVYLSRK KVACPVIEVI NDKDMSYMTV DNFQRGIFVW PMNFGWRTIP PDVIAKNRIK
ETDTIRCPVM AGGLFSIDKS YFFELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR
VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ
RELRKKLKCK SFKWYLENVF PDLRAPIVRA SGVLINVALG KCISIENTTV ILEDCDGSKE
LQQFNYTWLR LIKCGEWCIA PNPDKGAVRL HPCDNRNKGL KWLHKSTLVF HPELVNHIVF
ENNQQLLCLE GNFSQKILKV AACDPVKPYQ KWKFEKYYEA
//
