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
//