(data stored in ACNUC18858 zone)

HOGENOM: RAT8_PE1073

ID   RAT8_PE1073                          STANDARD;      PRT;   437 AA.
AC   RAT8_PE1073; Q8CH87;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein
DE   beta-1,6-N-acetylglucosaminyltransferase 3; EC=2.4.1.102; EC=2.4.1
DE   150;AltName: Full=C2GnT-mucin type; Short=C2GnT-M;AltName:
DE   Full=dI/C2/C4GnT; Short=dIGnT; (RAT8.PE1073).
GN   Name=Gcnt3;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT8.PE1073.
CC       Rattus norvegicus chromosome 8 RGSC3.4  sequence 1..129041809 annotated
CC       by Ensembl
CC   -!- ANNOTATIONS ORIGIN:GCNT3_RAT
CC   -!- FUNCTION: Glycosyltransferase that can synthesize all known mucin
CC       beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan
CC       branching, 2 important steps in mucin-type biosynthesis. Has also
CC       I-branching enzyme activity by converting linear into branched
CC       poly-N-acetyllactosaminoglycans, leading to introduce the blood
CC       group I antigen during embryonic development.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + beta-D-
CC       galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D-
CC       galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-
CC       galactosaminyl-R.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + beta-D-
CC       galactosyl-1,4-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-
CC       glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7-8.5;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       II membrane protein (By similarity).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC   -!- GENE_FAMILY: HOG000293251 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000011086;ENSRNOT00000014727;ENSRNOP00000014727.
DR   EMBL; AB098520; - ;
DR   UniProtKB/Swiss-Prot; Q8CH87; -.
DR   EMBL; AB098520; BAC53607.1; -; mRNA.
DR   IPI; IPI00192585; -.
DR   RefSeq; NP_775434.1; NM_173312.1.
DR   UniGene; Rn.43518; -.
DR   ProteinModelPortal; Q8CH87; -.
DR   SMR; Q8CH87; 67-432.
DR   STRING; Q8CH87; -.
DR   CAZy; GT14; Glycosyltransferase Family 14.
DR   PRIDE; Q8CH87; -.
DR   Ensembl; ENSRNOT00000014727; ENSRNOP00000014727; ENSRNOG00000011086.
DR   GeneID; 286976; -.
DR   KEGG; rno:286976; -.
DR   UCSC; NM_173312; rat.
DR   CTD; 9245; -.
DR   RGD; 631333; Gcnt3.
DR   eggNOG; maNOG07131; -.
DR   GeneTree; ENSGT00550000074330; -.
DR   InParanoid; Q8CH87; -.
DR   OMA; GQNSMES; -.
DR   OrthoDB; EOG4X6C8B; -.
DR   PhylomeDB; Q8CH87; -.
DR   BRENDA; 2.4.1.164; 5301.
DR   NextBio; 625213; -.
DR   ArrayExpress; Q8CH87; -.
DR   Genevestigator; Q8CH87; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003829; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IEDR   GO; GO:0008109; F:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity; IDA:RGD.
DR   GO; GO:0008109; F:N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity; IDA:RGD.
DR   InterPro; IPR003406; Glyco_trans_14.
DR   Pfam; PF02485; Branch; 1.
DR   HOGENOMDNA; RAT8.PE1073; -.
KW   ENSRNOG00000011086820036002503210000011;
KW   Gcnt3; GCNT3_RAT; AB098520;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   437 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVSWRRFCWH YHGWTLGCYM LLAIIALKLS LRLKCDFDVM DLDSKEFQSQ YCRDLLYKTL
     ELPAKSSINC SGVIRGEQKA VTQALLNNLE LKRKRQSFTE ADYLSMTADC EHFKTQRKFI
     QVPLSKEEAN FPIAYSMVIH EKIENFERLL RAVYTPQNIY CVHVDQKSSE TFQQAVRAIV
     SCFPNVFIAN KLVSVVYASW SRVQADLNCM EDLLQSPVPW EYLLNTCGTD FPIKTNAEMV
     KALKLLNGQN SMESEVPPPH KTFRWKYHYE VADTLYRTSK EKTPPPNNIT MFTGNAYMVA
     SRDFIEHVLS NSKARQLIEW VKDTYSPDEH LWATLQRASW MPGSDPLHPK FDLSDMRSIA
     RLTKWQDHEG DIENGAPYTS CSGIHQRAIC VYGSGDLHWI LQNHHLLANK FDPKVDDNVL
     QCLEEYLRHK AIYGTEL
//

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