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 16-JAN-2019, entry version 124. DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A; DE EC=2.4.1.155 {ECO:0000269|PubMed:7615638, ECO:0000269|PubMed:8340368}; DE AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase; DE AltName: Full=GlcNAc-T V {ECO:0000303|PubMed:7615638, ECO:0000303|PubMed:8340368}; DE Short=GNT-V; DE AltName: Full=Mannoside acetylglucosaminyltransferase 5; DE AltName: Full=N-acetylglucosaminyl-transferase V {ECO:0000303|PubMed:8340368}; DE Contains: DE RecName: Full=Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A {ECO:0000305}; DE AltName: Full=Secreted beta-1,6-N-acetylglucosaminyltransferase V {ECO:0000305}; DE Short=Secreted GNT-V {ECO:0000305}; DE Flags: Precursor; GN Name=Mgat5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 375-386; 546-557 AND RP 592-607, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE RP SPECIFICITY. 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 FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=7615638; RA Demetriou M., Nabi I.R., Coppolino M., Dedhar S., Dennis J.W.; RT "Reduced contact-inhibition and substratum adhesion in epithelial RT cells expressing GlcNAc-transferase V."; RL J. Cell Biol. 130:383-392(1995). RN [3] 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 (GlcNAc) CC in beta 1-6 linkage to the alpha-linked mannose of biantennary N- CC linked oligosaccharides (PubMed:8340368, PubMed:7615638). CC Catalyzes an important step in the biosynthesis of branched, CC complex-type N-glycans, such as those found on EGFR, TGFR (TGF- CC beta receptor) and CDH2 (By similarity). Via its role in the CC biosynthesis of complex N-glycans, plays an important role in the CC activation of cellular signaling pathways, reorganization of the CC actin cytoskeleton, cell-cell adhesion and cell migration CC (PubMed:7615638). MGAT5-dependent EGFR N-glycosylation enhances CC the interaction between EGFR and LGALS3 and thereby prevents rapid CC EGFR endocytosis and prolongs EGFR signaling. Required for CC efficient interaction between TGFB1 and its receptor. Enhances CC activation of intracellular signaling pathways by several types of CC growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5- CC dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic CC cell-cell adhesion and contributes to the regulation of downstream CC signaling pathways. Promotes cell migration. Contributes to the CC regulation of the inflammatory response. MGAT5-dependent TCR N- CC glycosylation enhances the interaction between TCR and LGALS3, CC limits agonist-induced TCR clustering, and thereby dampens TCR- CC mediated responses to antigens. Required for normal leukocyte CC evasation and accumulation at sites of inflammation (By CC similarity). Inhibits attachment of monocytes to the vascular CC endothelium and subsequent monocyte diapedesis (By similarity). CC {ECO:0000250|UniProtKB:Q09328, ECO:0000250|UniProtKB:Q8R4G6, CC ECO:0000269|PubMed:7615638, ECO:0000269|PubMed:8340368}. CC -!- FUNCTION: Secreted alpha-1,6-mannosylglycoprotein 6-beta-N- CC acetylglucosaminyltransferase A: Promotes proliferation of CC umbilical vein endothelial cells and angiogenesis, at least in CC part by promoting the release of the growth factor FGF2 from the CC extracellular matrix. {ECO:0000250|UniProtKB:Q09328}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha- CC D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D- CC Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl- CC [protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man- CC (1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man- CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}- CC L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:16921, Rhea:RHEA- CC COMP:14374, Rhea:RHEA-COMP:14377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:139507, CC ChEBI:CHEBI:139510; EC=2.4.1.155; CC Evidence={ECO:0000269|PubMed:7615638, CC ECO:0000269|PubMed:8340368}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:7615638, ECO:0000269|PubMed:8340368}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P97259}; Single-pass type II membrane CC protein {ECO:0000250|UniProtKB:Q09328}. CC -!- SUBCELLULAR LOCATION: Secreted alpha-1,6-mannosylglycoprotein 6- CC beta-N-acetylglucosaminyltransferase A: Secreted CC {ECO:0000250|UniProtKB:Q09328}. CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level). CC Detected in kidney. {ECO:0000269|PubMed:8340368}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q09328}. CC -!- PTM: A secreted form is released from the membrane after cleavage CC by gamma-secretase. {ECO:0000250|UniProtKB:Q09328}. 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 SMR; Q08834; -. 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; ENSGT00940000155430; -. DR HOGENOM; HOG000006557; -. DR HOVERGEN; HBG052469; -. DR InParanoid; Q08834; -. DR KO; K00744; -. DR OMA; GKVDNFW; -. DR OrthoDB; 179031at2759; -. 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; Expressed in 9 organ(s), highest expression level in brain. DR ExpressionAtlas; Q08834; baseline and differential. DR Genevisible; Q08834; RN. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB. DR InterPro; IPR027833; DUF4525. DR InterPro; IPR026116; GlyclTrfase_18. DR Pfam; PF15027; DUF4525; 1. DR Pfam; PF15024; Glyco_transf_18; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane; KW Reference proteome; Secreted; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 740 Alpha-1,6-mannosylglycoprotein 6-beta-N- FT acetylglucosaminyltransferase A. FT /FTId=PRO_0000080524. FT CHAIN 31 740 Secreted alpha-1,6-mannosylglycoprotein FT 6-beta-N-acetylglucosaminyltransferase A. FT {ECO:0000250|UniProtKB:Q09328}. FT /FTId=PRO_0000445694. 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 REGION 212 740 Sufficient for catalytic activity. FT {ECO:0000250|UniProtKB:Q09328}. FT REGION 377 378 Substrate binding. FT {ECO:0000250|UniProtKB:Q09328}. FT BINDING 525 525 UDP-GlcNAc. FT {ECO:0000250|UniProtKB:Q09328}. FT BINDING 553 553 Substrate. FT {ECO:0000250|UniProtKB:Q09328}. FT CARBOHYD 109 109 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 114 114 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 117 117 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 333 333 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 432 432 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 446 446 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 144 182 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 155 195 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 171 337 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 371 625 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 648 723 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 652 725 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 659 712 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 680 701 {ECO:0000250|UniProtKB:Q09328}. FT DISULFID 736 739 {ECO:0000250|UniProtKB:Q09328}. 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 //