ID G1PAU9_MYOLU Unreviewed; 632 AA.
AC G1PAU9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-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=GALNT8 {ECO:0000313|Ensembl:ENSMLUP00000007437.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000007437.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000007437.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000007437.2}
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; AAPE02031467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02031468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02031469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006096154.1; XM_006096092.2.
DR AlphaFoldDB; G1PAU9; -.
DR STRING; 59463.ENSMLUP00000007437; -.
DR Ensembl; ENSMLUT00000008147.2; ENSMLUP00000007437.2; ENSMLUG00000008140.2.
DR GeneID; 102430967; -.
DR KEGG; mlf:102430967; -.
DR CTD; 26290; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000160161; -.
DR HOGENOM; CLU_013477_4_1_1; -.
DR InParanoid; G1PAU9; -.
DR OMA; MTFWRKR; -.
DR OrthoDB; 202750at2759; -.
DR TreeFam; TF352661; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001074; 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:SF50; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 8-RELATED; 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.
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:UP000001074};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 494..623
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 632 AA; 72008 MW; 6B0BA95EB065E34D CRC64;
MMLRRHLCKV LCIGLTLVIV YNLLLVVYTK MTLQKLILGG VQKELHLPLS EWNGTVIKKL
SHLESELQHL KESMKLAMKQ QENVDDTLKR VRDEQPVQKA VEAKASETKK HRPREKLFPN
SPLFKQWGED LSEAQQKRAQ DLFQKFGYNV YLSNLLPLNR SIPDTRHSRC LQKTYSSQLP
SLSVILIFTN EALSIIQRAI TSIINRTPSR LLKEIILVDD FSSNEELKAN LDELIKLYNQ
KYPGLLKIVR HTKRQGLAQA RNTGREAATA EVVAILDAHI EVNAGWAEPI LARIQEDHTV
IVSPVFDKIH FDTFELEKYG LAVDGFNWEL WCRYDSLPKA WIDLNDVTAP VKSPSIMGIL
AANRLFLGKI GSVDGGMLVY GGENVELSLR VWQCGGRIEV LPCSRIAHIE RNHKPYALDL
TPAMKRNALR VAEIWMDEYK YMVYLAWNIP LQNSGIDYGD ISSRMALREN LKCKTFDWYL
KNVYPALKPI HNIVGYGRIK NSLSENDCLD RGPFKGKTPI MYFCNEYSPQ KVYYHLTGEL
YVGSLIAEAN AEDCCLTDPG SGENPTLEPC SKAAQNGLHI YWDFKPGKAL INRATKRCLE
IKKASSYYMP VLRPCTTQVW TIQHTIGTWG SN
//