UniProt: A0A3Q3AMS7

Database: UniProt
Entry: A0A3Q3AMS7_KRYMA

LinkDB:  A0A3Q3AMS7_KRYMA 
Original site:  A0A3Q3AMS7_KRYMA

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Ontology (4)   
   GO (4)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (19)   

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ID   A0A3Q3AMS7_KRYMA        Unreviewed;       604 AA.
AC   A0A3Q3AMS7;
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=GALNT9 {ECO:0000313|Ensembl:ENSKMAP00000012749.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000012749.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000012749.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|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_017270191.1; XM_017414702.1.
DR   AlphaFoldDB; A0A3Q3AMS7; -.
DR   STRING; 37003.ENSKMAP00000012749; -.
DR   Ensembl; ENSKMAT00000012939.1; ENSKMAP00000012749.1; ENSKMAG00000009543.1.
DR   GeneID; 108235006; -.
DR   KEGG; kmr:108235006; -.
DR   CTD; 50614; -.
DR   GeneTree; ENSGT00940000156599; -.
DR   OMA; QYVHRRY; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000264800; 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:SF28; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9; 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, ECO:0000256|RuleBase:RU361242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, 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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          466..596
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   604 AA;  68824 MW;  396B2C92B3D68751 CRC64;
     MAVARKIKTL LTVNILVFVG IILFSVYCRI QDRSEELIQI GRVSEQRLRA RNGKVSNLVD
     RQSILQRLER LEDVVYNQLN GLAKPIGLVE GPGGLGQGGA AATLGEDSRD AEGKYEEYGY
     NAQLSDRISL DRSIPDYRPK KCKQLTYPED LPQISVVFIF VNEALSVILR SVHSVVNHTP
     AHLLKEIILV DDNSDSVELK FNLDQYVNKR YPGLVKIVRN SKREGLIRAR IHGWNAATAP
     VVGFFDAHVE FNTGWSEPIL TRMKEDHTRI ILPAIDNIKY NTFEVQQYAN AAHGYNWGLW
     CMYIIPPQEW LDKGDETAPI RTPAMIGCSF VVDREYFGEI GLLDPGMEVY GGENIELGMR
     VWQCGGSMEV LPCARVAHIE RTKKPYNNDI DYYAKRNALR AAEVWMDEYK SHVYMAWNIP
     MNNPGVDFGD VSDRLALRKK MQCRSFRWYL EHVYPEMRIY NNTITYGEVR NSKASGYCLD
     QGSEDDDKAI LYPCHGMSSQ LARYSTEGLL QLGPLGSTTF LPDTKCLIDD GRGRTPSLKK
     CDVVSRISQR LWDFTQNGPI INRDTGRCLE VEMSKDANFG LRLVVQRCSG QKWIIRNWIK
     HPRH
//

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