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Database: UniProt
Entry: A0A3Q2E789_CYPVA
LinkDB: A0A3Q2E789_CYPVA
Original site: A0A3Q2E789_CYPVA 
ID   A0A3Q2E789_CYPVA        Unreviewed;       618 AA.
AC   A0A3Q2E789;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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:ENSCVAP00000028188.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000028188.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000028188.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={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}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000256|RuleBase:RU361242}.
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DR   RefSeq; XP_015231684.1; XM_015376198.1.
DR   AlphaFoldDB; A0A3Q2E789; -.
DR   STRING; 28743.ENSCVAP00000028188; -.
DR   Ensembl; ENSCVAT00000019948.1; ENSCVAP00000028188.1; ENSCVAG00000015059.1.
DR   GeneID; 107085707; -.
DR   KEGG; cvg:107085707; -.
DR   CTD; 26290; -.
DR   GeneTree; ENSGT00940000160161; -.
DR   OMA; MTFWRKR; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000265020; 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; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
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   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|RuleBase:RU361242};
KW   Glycosyltransferase {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|RuleBase:RU361242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242}.
FT   DOMAIN          159..287
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          472..596
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|Pfam:PF00652"
FT   COILED          56..93
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   618 AA;  71096 MW;  A16DC8928E200B8A CRC64;
     MRSGWFKAFL MVIAVASGLV YLSSIKAELS THSERLHRAQ HNESLRGQGM MMMRRMEMME
     KDINRLMSLM KHYEKKEQGL DKAKKEKKRV MKLFPDSHLF RKWGDDLSEE EQKEAEDLFQ
     RYGYNAFLSD RLPINREIPD TRPPRCAEKR YPEDLPSLSV ILIYLDEALS VIKRAIRSII
     DRTPPRLLLE IILVDDHSSN DDLLGKLDEY ISSIHEERPG LVKKIHHSEQ LGLTQARLSG
     WKAAVGDVVA ILDAHIEVHV QWAEPLLARI KEDRTVILTP VFDKISFDDL IPIPYGTSAH
     GFDWAMWCMY EGFRPEWYAL RDDSQPGKSP SVMGILVAER KFFGEIGSLD GGMKIYGGEN
     VELGIRVWLC GGSIEIIPCS RIAHIERFHK PYARDLSSFV RRNALRVAEV WLDDYKYNVE
     VAWNLPIGNH GIDIGDVSER KKLKEKLKCK PFQWYLDNVY PMLEPMSNLL GYGALINDLL
     PDQCVDRGPV PGFIPILHGC HFFTPQHCHY HTDGTLHIGG FKSHKYDSSD CLLDPGLGAL
     PGLYQCRMAE QKKLHMFWDF KQGGQIQNRE TKRCLEISMR GLNLKLVLQQ CSGQRWKLQH
     VVDVTAQKLH RLSEKLVL
//
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