ID MGT5A_RAT Reviewed; 740 AA. AC Q08834; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 15-MAR-2017, entry version 116. DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A; DE EC=2.4.1.155; DE AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase; DE AltName: Full=GlcNAc-T V; DE Short=GNT-V; DE AltName: Full=Mannoside acetylglucosaminyltransferase 5; DE AltName: Full=N-acetylglucosaminyl-transferase V; GN Name=Mgat5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 375-386; 546-557 RP AND 592-607. RC TISSUE=Kidney; RX 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). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16641100; DOI=10.1073/pnas.0600895103; RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: RT regulation of aquaporin-2 phosphorylation at two sites."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). 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: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type CC II membrane protein. CC -!- SIMILARITY: Belongs to the glycosyltransferase 18 family. CC {ECO:0000305}. 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; -; mRNA. DR PIR; A47134; A47134. DR RefSeq; NP_075583.1; NM_023095.1. DR RefSeq; XP_008767721.2; XM_008769499.2. DR RefSeq; XP_017454423.1; XM_017598934.1. DR UniGene; Rn.53998; -. DR STRING; 10116.ENSRNOP00000004995; -. DR ChEMBL; CHEMBL1795132; -. DR CAZy; GT18; Glycosyltransferase Family 18. DR iPTMnet; Q08834; -. DR PhosphoSitePlus; Q08834; -. DR PaxDb; Q08834; -. DR PRIDE; Q08834; -. DR Ensembl; ENSRNOT00000004995; ENSRNOP00000004995; ENSRNOG00000003614. DR GeneID; 65271; -. DR KEGG; rno:65271; -. DR UCSC; RGD:620100; rat. DR CTD; 4249; -. DR RGD; 620100; Mgat5. DR eggNOG; ENOG410IDYS; Eukaryota. DR eggNOG; ENOG410XTV7; LUCA. DR GeneTree; ENSGT00390000012263; -. DR HOGENOM; HOG000006557; -. DR HOVERGEN; HBG052469; -. DR InParanoid; Q08834; -. DR KO; K00744; -. DR OMA; GKVDNFW; -. DR OrthoDB; EOG091G044F; -. DR PhylomeDB; Q08834; -. DR TreeFam; TF313714; -. DR Reactome; R-RNO-975577; N-Glycan antennae elongation. DR UniPathway; UPA00378; -. DR PRO; PR:Q08834; -. DR Proteomes; UP000002494; Chromosome 13. DR Bgee; ENSRNOG00000003614; -. DR ExpressionAtlas; Q08834; baseline. DR Genevisible; Q08834; RN. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. 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:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR InterPro; IPR027833; DUF4525. DR InterPro; IPR026116; GlyclTrfase_18. DR PANTHER; PTHR15075; PTHR15075; 1. DR Pfam; PF15027; DUF4525; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome; KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 740 Alpha-1,6-mannosylglycoprotein 6-beta-N- FT acetylglucosaminyltransferase A. FT /FTId=PRO_0000080524. FT TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 14 30 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 31 740 Lumenal. {ECO:0000255}. FT CARBOHYD 109 109 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 114 114 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 117 117 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 333 333 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 432 432 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 446 446 N-linked (GlcNAc...). {ECO:0000255}. 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 //