(data stored in ACNUC18858 zone)

SWISSPROT: GCNT4_DANRE

ID   GCNT4_DANRE             Reviewed;         428 AA.
AC   Q71SG7; A5WWG0; Q6DHL9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4;
DE            EC=2.4.1.102 {ECO:0000250|UniProtKB:Q9P109};
GN   Name=gcnt4; ORFNames=si:ch211-129a6.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Schwientek T., Clausen H.;
RT   "Core 2 b-1,6-N-acetylglucosaminyltransferase.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C.,
RA   Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C.,
RA   Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N.,
RA   Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L.,
RA   Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S.,
RA   Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A.,
RA   Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glycosyltransferase that mediates core 2 O-glycan branching,
CC       an important step in mucin-type biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9P109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC         = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC         (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC         UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-
CC         COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102;
CC         Evidence={ECO:0000250|UniProtKB:Q9P109};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC         glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-
CC         glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC         [protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923,
CC         Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607;
CC         EC=2.4.1.102; Evidence={ECO:0000250|UniProtKB:Q9P109};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC       {ECO:0000305}.
DR   EMBL; AF300969; AAQ14484.1; -; mRNA.
DR   EMBL; BX511209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU062416; CAN88495.1; -; Genomic_DNA.
DR   EMBL; BC075950; AAH75950.1; -; mRNA.
DR   RefSeq; NP_963877.1; NM_201583.1.
DR   SMR; Q71SG7; -.
DR   STRING; 7955.ENSDARP00000050987; -.
DR   CAZy; GT14; Glycosyltransferase Family 14.
DR   PaxDb; Q71SG7; -.
DR   PRIDE; Q71SG7; -.
DR   Ensembl; ENSDART00000050988; ENSDARP00000050987; ENSDARG00000035198.
DR   GeneID; 324510; -.
DR   KEGG; dre:324510; -.
DR   CTD; 324510; -.
DR   ZFIN; ZDB-GENE-030131-3231; gcnt4a.
DR   eggNOG; KOG0799; Eukaryota.
DR   eggNOG; ENOG410XQ7M; LUCA.
DR   GeneTree; ENSGT00940000159721; -.
DR   HOGENOM; HOG000293251; -.
DR   InParanoid; Q71SG7; -.
DR   KO; K09663; -.
DR   OMA; YVKLPVR; -.
DR   OrthoDB; 868849at2759; -.
DR   PhylomeDB; Q71SG7; -.
DR   TreeFam; TF315534; -.
DR   Reactome; R-DRE-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q71SG7; -.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000035198; Expressed in 23 organ(s), highest expression level in spleen.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003829; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR003406; Glyco_trans_14.
DR   Pfam; PF02485; Branch; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q71SG7.
DR   SWISS-2DPAGE; Q71SG7.
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..428
FT                   /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-
FT                   1,6-N-acetylglucosaminyltransferase 4"
FT                   /id="PRO_0000288556"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..428
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..214
FT                   /evidence="ECO:0000250"
FT   DISULFID        148..369
FT                   /evidence="ECO:0000250"
FT   DISULFID        169..196
FT                   /evidence="ECO:0000250"
FT   DISULFID        378..410
FT                   /evidence="ECO:0000250"
FT   CONFLICT        65
FT                   /note="D -> E (in Ref. 1; AAQ14484 and 2; BX511209)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  49928 MW;  4A4DB04D9212DC69 CRC64;
     MRRCAVLHRL RCKFYVFVVS LFVVVKLVYL KISMDNSIYI EPYGVTRRSL KPQPLDGINC
     TAIYDLEPVE IGKSLEMRRK KIVEVDDGRI ASFTADCKSY IEQRRYNEVL VTDEECNFPI
     AYSLVVHKNS AMVERILRAI YAPQNIYCIH YDQKSTKDFI AAMKNLESCF PNVFIASKIE
     SVQYAHITRL KADLNCLSDL LSSEVKWKYV INLCGQDFPL KSNYELVTEL RKLNGANMLE
     TSRPSKVKKQ RFQFRYQLKD VSYEYQKMPV KTSIAKDPPP HNIEMFVGSA YFVLSRDFVT
     YVMNNQLAKD FLQWSVDTYS PDEHFWASMA RVPGVPGELA RSEPDVSDLK SRTRLVKWNY
     LEERLYPKCT GTHRRSVCIY GAAELRWLLE DGHWFANKFD PKVDPVIIKC LEEKLEEKQL
     QQCLRRVS
//

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