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Database: UniProt
Entry: A0A2U3YTI2_LEPWE
LinkDB: A0A2U3YTI2_LEPWE
Original site: A0A2U3YTI2_LEPWE 
ID   A0A2U3YTI2_LEPWE        Unreviewed;       475 AA.
AC   A0A2U3YTI2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=LOC102744372 {ECO:0000313|RefSeq:XP_006747035.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006747035.1};
RN   [1] {ECO:0000313|RefSeq:XP_006747035.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006747035.1};
RG   RefSeq;
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   RefSeq; XP_006747035.1; XM_006746972.1.
DR   AlphaFoldDB; A0A2U3YTI2; -.
DR   STRING; 9713.A0A2U3YTI2; -.
DR   GeneID; 102744372; -.
DR   KEGG; lww:102744372; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000245341; Unplaced.
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:SF58; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 6; 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:UP000245341};
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          349..475
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          445..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  54350 MW;  99940F01DB85A9E3 CRC64;
     MKTQNRSQEI VCDGSIRCVD QKFRRCPPLP TTSVIIVFHN EAWSTLLRTV YSVLHTAPAI
     LLKEIILVDD ASTDDYLKEQ LEQYVKKLQV VRVVRQEERK GLITARLLGA SVAQAEVLTF
     LDAHCECFHG WLEPLLARIA EEETAVVSPD IVTIDLNTFE FSKPVQRGRV HSRGNFDWSL
     TFGWETLPAH EKQRRKDETY PIKSPTFAGG LFSISKSYFE HIGTYDNQME IWGGENVEMS
     FRVWQCGGQL EIIPCSVVGH VFRTKSPHTF PKGISVIARN QVRLAEVWMD GYKEIFYRRN
     MQAAKMAQEK SFGDISERLK LKEQLHCRNF SWFLNNIYPE MFVPDLKPTF YGAIRNLGIN
     QCLDVGENNH GGKPLIMYTC HGLGGNQYFE YTTQRDLRHN IAKQLCLHAS ADTLGLRNCH
     FTGKNSQVPK DEEWELTQDQ LIRNSGSGTC LTSEDKKPAM ASCNPSDPHQ HWLFN
//
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