ID GNT5_RAT STANDARD; PRT; 740 AA. AC Q08834; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase DE V (EC 2.4.1.155) (Alpha-mannoside beta-1,6-N- DE acetylglucosaminyltransferase) (N-acetylglucosaminyl-transferase V) DE (GNT-V) (GlcNAc-T V). GN Name=Mgat5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 375-386; 546-557 AND RP 592-607. RC TISSUE=Kidney; RX MEDLINE=93340130; PubMed=8340368; RA Shoreibah M., Perng G.-S., Adler B., Weinstein J., Basu R., RA Cupples R., Wen D., Browne J.K., Buckhaults P., Fregien N., Pierce M.; RT "Isolation, characterization, and expression of a cDNA encoding N- RT acetylglucosaminyltransferase V."; RL J. Biol. Chem. 268:15381-15385(1993). CC -!- FUNCTION: Catalyzes the addition of N-acetylglucosamine in beta 1- CC 6 linkage to the alpha-linked mannose of biantennary N-linked CC oligosaccharides. It is one of the most important enzymes involved CC in the regulation of the biosynthesis of glycoprotein CC oligosaccharides. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl- CC beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + CC 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- CC mannosyl-R. CC -!- PATHWAY: Glycosylation. CC -!- SUBCELLULAR LOCATION: Type II membrane protein. Golgi. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L14284; AAA41665.1; -. DR PIR; A47134; A47134. DR RGD; 620100; Mgat5. KW Direct protein sequencing; Glycoprotein; Glycosyltransferase; KW Golgi stack; Signal-anchor; Transferase; Transmembrane. FT DOMAIN 1 13 Cytoplasmic (Potential). FT TRANSMEM 14 30 Signal-anchor for type II membrane FT protein (Potential). FT DOMAIN 31 740 Lumenal, catalytic (Potential). FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential). FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential). FT CARBOHYD 117 117 N-linked (GlcNAc...) (Potential). FT CARBOHYD 333 333 N-linked (GlcNAc...) (Potential). FT CARBOHYD 432 432 N-linked (GlcNAc...) (Potential). FT CARBOHYD 446 446 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 740 AA; 84562 MW; C0BD7F820FEA959C CRC64; MAFFSPWKLS SQKLGFFLVT FGFIWGMMLL HFTIQQRTQP ESSSMLREQI LDLSKRYIKA LAEENRNVVD GPYAGVMTAY DLKKTLAVLL DNILQRIGKL ESKVDNLVNG TGANSTNSTT AVPSLVSLEK INVADIINGV QEKCVLPPMD GYPHCEGKIK WMKDMWRSDP CYADYGVDGT SCSFFIYLSE VENWCPRLPW RAKNPYEEAD HNSLAEIRTD FNILYGMMKK HEEFRWMRLR IRRMADAWIQ AIKSLAEKQN LEKRKRKKIL VHLGLLTKES GFKIAETAFS GGPLGELVQW SDLITSLYLL GHDIRISASL AELKEIMKKV VGNRSGCPTV GDRIVELIYI DIVGLAQFKK TLGPSWVHYQ CMLRVLDSFG TEPEFNHASY AQSKGHKTPW GKWNLNPQQF YTMFPHTPDN SFLGFVVEQH LNSSDIHHIN EIKRQNQSLV YGKVDSFWKN KKIYLDIIHT YMEVHATVYG SSTKNIPSYV KNHGILSGRD LQFLLRETKL FVGLGFPYEG PAPLEAIANG CAFLNPKFNP PKSSKNTDFF IGKPTLRELT SQHPYAEVFI GRPHVWTVDL NNREEVEDAV KAILNQKIEP YMPYEFTCEG MLQRINAFIE KQDFCHGQVM WPPLSALQVK LAEPGQSCKQ VCQESQLICE PSFFQHLNKE KDLLKYKVIC QSSELYKDIL VPSFYPKSKH CVFQGDLLLF SCAGAHPTHQ RICPCRDFIK GQVALCKDCL //