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Database: UniProt
Entry: A0A1D1VBL3_RAMVA
LinkDB: A0A1D1VBL3_RAMVA
Original site: A0A1D1VBL3_RAMVA 
ID   A0A1D1VBL3_RAMVA        Unreviewed;       655 AA.
AC   A0A1D1VBL3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {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=RvY_10089-1 {ECO:0000313|EMBL:GAU99029.1};
GN   Synonyms=RvY_10089.1 {ECO:0000313|EMBL:GAU99029.1};
GN   ORFNames=RvY_10089 {ECO:0000313|EMBL:GAU99029.1};
OS   Ramazzottius varieornatus (Water bear) (Tardigrade).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX   NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU99029.1, ECO:0000313|Proteomes:UP000186922};
RN   [1] {ECO:0000313|EMBL:GAU99029.1, ECO:0000313|Proteomes:UP000186922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU99029.1,
RC   ECO:0000313|Proteomes:UP000186922};
RX   PubMed=27649274; DOI=10.1038/ncomms12808;
RA   Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA   Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA   Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA   Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA   Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT   "Extremotolerant tardigrade genome and improved radiotolerance of human
RT   cultured cells by tardigrade-unique protein.";
RL   Nat. Commun. 7:12808-12808(2016).
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|RuleBase:RU361242}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU361242}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
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:GAU99029.1}.
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DR   EMBL; BDGG01000005; GAU99029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D1VBL3; -.
DR   STRING; 947166.A0A1D1VBL3; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186922; 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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:SF131; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9-RELATED; 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|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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|RuleBase:RU361242};
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        25..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          495..619
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          51..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   655 AA;  74724 MW;  38AA4AFAD8342A6F CRC64;
     MATSAAVFLR NTVRQYRLMR IRAPYLVKYA VLSFFVFICL YAVLSRISGK QPSSADYEEP
     HRAQEKQEVQ ESQAQAAPPS LRDRKGAKDR KSEDKNVILA PVHVDVDNIQ ETKHEGPGEM
     GEPVKIDREK LGPAEQEAYD KGFEKNSFNQ YASDMISVHR SLTDMRPKAC LEAARSYRKD
     LPDCSVIICF HNEAWSTLLR SVHSVLNRSP AHLLKEVILV DDASEHEFLK DQLDDYFAKY
     PKVKIVRSPL RVGLIKARLL GYEQATGQVL TFLDSHIEAT KGWLEPLLDR IARDKTNVVW
     PVIDIISDKT LMYKNDPDAG SQVGGFDWGL QFNWHMIPDR DAKKRKNKSS PVRSPTMAGG
     LFAIDKAYFE KLGTYDPDFD IWGGENLEIS FKTWMCGGTL EMIPCSRVGH IFRDKSPYKW
     RTGQDVLKKN LVRLAEVWMD DLKQNYYDRI NNELGDFGDI SERVALRKRL GCKSFQWYID
     NVYPELFIPD QAKAYGEVRN AALAGAYCMD GDPDSVNKTV SIYPCHNLGG NQYWSYSNES
     EIRRDDYCVD NAWASSETSR LILVPCHGAK GNQEWIHDRK TGLFTNPTAD LCMESNHSKM
     TIKLAPCDAN KEEQKWTWKN YREDKAKSTK KAKIKTTAPP ENLPEGEQEG QEAPE
//
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