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Database: UniProt
Entry: M7BH27_CHEMY
LinkDB: M7BH27_CHEMY
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ID   M7BH27_CHEMY            Unreviewed;       951 AA.
AC   M7BH27;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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};
DE   Flags: Fragment;
GN   ORFNames=UY3_05597 {ECO:0000313|EMBL:EMP37211.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP37211.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(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}.
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DR   EMBL; KB523027; EMP37211.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BH27; -.
DR   STRING; 8469.M7BH27; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd11304; Cadherin_repeat; 3.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 3.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR032455; Cadherin_C.
DR   InterPro; IPR020894; Cadherin_CS.
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:SF18; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 12; 1.
DR   Pfam; PF00028; Cadherin; 3.
DR   Pfam; PF16492; Cadherin_C_2; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 3.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 3.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS00232; CADHERIN_1; 1.
DR   PROSITE; PS50268; CADHERIN_2; 3.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043};
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:UP000031443};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|RuleBase:RU361242, ECO:0000313|EMBL:EMP37211.1};
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        334..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          1..97
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          98..207
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          214..325
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMP37211.1"
SQ   SEQUENCE   951 AA;  107704 MW;  5887EED1CBD9B2BF CRC64;
     IPEDSSPETA VALFSVRDRD SGDNGRTVCS IQDNVPFALK STLKNYYELV TQKPLDREKV
     PEYNISITAT DRGTPRLTSV RIIRVQLSDI NDNPPVFNES SYVMYLKENN HPGLLIGTVH
     AADLDTEQNA KVTYSALLGN IGDLPFSSSI SINSENGNVY ALQSLDYEQT RDFQVTVRAA
     DGGSPPLSSE VIVRVVIIDE NNNAPFILYP LQNSSSPAND LVPRSAEAGY LVTKVVAVDG
     DSGQNSWLSY QLLKATDPGL FAVGLQTGEV KTSRPITSPD SVKQKLIVLV RDNGEPPRST
     TSTLNVLLVD GFSDAYMQLL DVPQEEEEQD TLTLYLVISL SFISFLFLVS VVTIIAIRLY
     KTRQCRERYV PSSRNFYCEP NFPTNPADRS VTGTLPQSYC YEVCLTTGSG TSEFKFLRPL
     VPSLPADPSA ADGSILDSQI NSQLKKEKES LREIQTNTAA TLKHNVMRSV PSQEEAALKK
     MKGTCPNMQD LQLKSENERL RASLSQEQRI AADRFQQQMG SLNARLKEQT KVIRLQEKTQ
     VDEKEIAYLK KLHWCKEKKY DYHNLPKTSV VIAFYNEAWS TLLRTVHSVL ETSPDILLEE
     VILVDDYSDK DHLKKPLENY VAGLRKVRLI RANKREGLVR ARLLGASLAK GDVLTFLDCH
     CECHEGWLEP LLERSPTMAG GLFAVSKKYF DYLGSYDTGM EVWGGENLEF SFRIWQCGGS
     LEIHPCSHVG HVFPKQAPYS RAKALANSVR AAEVWMDEYK ELYYHRNPHA RMEPYGDVTE
     RRLLREKLKC KDFKWFLENI YPELHVPEDR PGFFGMLQNR GMANYCFDYN PPNEHEVTGH
     RIILYPCHGM GQNQFFEYTS HNEIRYNTRQ PEACAAVDSE TDYLTMYLCQ DSVQNIPENQ
     KFVFREDGTL FHVQTQKCLQ AESNSYNGNP APLLRPCSNS EYQKWFFKER S
//
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