ID A0A8I5KTS5_HUMAN Unreviewed; 527 AA. AC A0A8I5KTS5; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 03-AUG-2022, entry version 2. DE RecName: Full=Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase {ECO:0000256|RuleBase:RU368119}; DE Short=POMGnT1 {ECO:0000256|RuleBase:RU368119}; DE EC=2.4.1.- {ECO:0000256|RuleBase:RU368119}; GN Name=POMGNT1 {ECO:0000313|Ensembl:ENSP00000510654}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000510654, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000510654, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., RA Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., RA Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., RA Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000510654} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2022) to UniProtKB. CC -!- FUNCTION: Participates in O-mannosyl glycosylation by catalyzing the CC addition of N-acetylglucosamine to O-linked mannose on glycoproteins. CC Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr CC moiety on alpha-dystroglycan and other O-mannosylated proteins, CC providing the necessary basis for the addition of further carbohydrate CC moieties. Is specific for alpha linked terminal mannose. CC {ECO:0000256|RuleBase:RU368119}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl- CC alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha- CC D-mannosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54128, CC Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:13802, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137323, CC ChEBI:CHEBI:138067; Evidence={ECO:0000256|ARBA:ARBA00001307, CC ECO:0000256|RuleBase:RU368119}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU368119}; CC Note=The manganese ion interacts primarily with the substrate UDP-N- CC acetylglucosamine. {ECO:0000256|RuleBase:RU368119}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368119}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU368119}; Single- CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, CC ECO:0000256|RuleBase:RU368119}. Membrane CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004606}. CC -!- DOMAIN: The stem domain mediates specific interaction with beta-linked CC N-acetylglucosamine moieties of O-glycosylated proteins. It also CC interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O- CC alpha-D-mannosylprotein. {ECO:0000256|RuleBase:RU368119}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family. CC {ECO:0000256|ARBA:ARBA00006492, ECO:0000256|RuleBase:RU368119}. 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; AL672043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000691243.1; ENSP00000510654.1; ENSG00000085998.15. DR HGNC; HGNC:19139; POMGNT1. DR GeneTree; ENSGT00530000063632; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000005640; Chromosome 1. DR CDD; cd13937; PANDER_GnT-1_2_like; 1. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR004139; Glyco_trans_13. DR InterPro; IPR039477; ILEI/PANDER_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR039474; POMGNT1_PANDER-like. DR Pfam; PF03071; GNT-I; 1. DR Pfam; PF15711; ILEI; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 1: Evidence at protein level; KW Glycosyltransferase {ECO:0000256|RuleBase:RU368119}; KW Golgi apparatus {ECO:0000256|RuleBase:RU368119}; KW Manganese {ECO:0000256|RuleBase:RU368119}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU368119}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|MaxQB:A0A8I5KTS5, KW ECO:0007829|PeptideAtlas:A0A8I5KTS5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal-anchor {ECO:0000256|RuleBase:RU368119}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|RuleBase:RU368119}. FT DOMAIN 129..217 FT /note="ILEI" FT /evidence="ECO:0000259|Pfam:PF15711" FT REGION 68..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..96 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 527 AA; 60047 MW; 9E3B7F2395D1A909 CRC64; MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD TRRAISEANE DPEPEQDYDE ALGRLEPPRR RGSGPRRVLD VEVYSSRSKV YVAVDGTTVL EDEAREQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV FGEKHSKSPA LSSWGDPVLL KTDVPLSSAE EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL FGLRGIQHTP ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV DFFSFLSQSI HLLEEDDSLY CISAWNDQGY EHTAEDPALL YRVETMPGLG WVLRRSLYKE ELEPKWPTPE KLWDWDMWMR MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPV //