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Database: UniProt
Entry: A0A2I0MQM8_COLLI
LinkDB: A0A2I0MQM8_COLLI
Original site: A0A2I0MQM8_COLLI 
ID   A0A2I0MQM8_COLLI        Unreviewed;       649 AA.
AC   A0A2I0MQM8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=GALNT15 {ECO:0000313|EMBL:PKK31995.1};
GN   ORFNames=A306_00002693 {ECO:0000313|EMBL:PKK31995.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK31995.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK31995.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK31995.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKK31995.1}.
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DR   EMBL; AKCR02000004; PKK31995.1; -; Genomic_DNA.
DR   RefSeq; XP_005504468.2; XM_005504411.2.
DR   AlphaFoldDB; A0A2I0MQM8; -.
DR   STRING; 8932.A0A2I0MQM8; -.
DR   InParanoid; A0A2I0MQM8; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000053872; 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:SF36; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 15; 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:UP000053872};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|RuleBase:RU361242, ECO:0000313|EMBL:PKK31995.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          519..641
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          114..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  73833 MW;  45A72821E8BAB952 CRC64;
     MRRQLHSASM FLRKKCRYGS RKLQFLLLLL MLGFLLLMVT TLNPPPSNQS KEGTFQPVEF
     NPREGYQVDF VETQEMLDTQ EESQQYYPLD GLSPFISLRE DELIAAVVSP TGRRNHSKAR
     KGYRVVKQQS RRPEARAEGD AESPQLPARP LQPAEGAAAG QRPLGLETHG FNEALSERIS
     LRRDLPEVRH PLCLQQEYDS SLPTASVIIC FHDEAWSTLL RTVHSIMDTA PKASLKDIIL
     VDDLSQQGPL KSALSEYISK LDGVKLIRSN KRLGVIRGRM LGAARATGDV LVFMDSHCEC
     QKGWLEPLLA RLSSNRNSVV SPVIDVIDWK TFQYYHSVGL HRGVFDWKLD FHWEPVPERE
     EKVRQSPISP IRSPVVAGAV VAMDRHYFQN TGAYDSDMTM WGAENLELSI RTWLCGGSVE
     IIPCSRVGHV YRNHFPRAFS YEEAIVRNKI RIAETWLGSF KDNFYKHDTV AFLISKAEKP
     DCSERLQLQK RLGCRSFQWF ISNVYPELSQ LEDTPRFSGK LYNTGVGFCA DYRPASAAAE
     GSIELSPCSD SLTQHFEYNS MKEIRLGSAP LFCFDVRHGK VIPQNCTKET DDSQQRWEVQ
     ENGMIVHVLS GKCIEASKSD DEKDLFLCVC NKNANQVWQF EHSHVLRQR
//
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