ID   A0A8I5KTS5_HUMAN        Unreviewed;       527 AA.
AC   A0A8I5KTS5;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   27-MAR-2024, entry version 11.
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:ENSP00000510654.1};
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:ENSP00000510654.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000510654.1, 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:ENSP00000510654.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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}.
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DR   EMBL; AL672043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; A0A8I5KTS5; -.
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   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd13937; PANDER_GnT-1_2_like; 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   PANTHER; PTHR46396; PROTEIN O-LINKED-MANNOSE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR46396:SF1; PROTEIN O-LINKED-MANNOSE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE 1; 1.
DR   Pfam; PF03071; GNT-I; 1.
DR   Pfam; PF15711; ILEI; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368119};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU368119}; Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Manganese {ECO:0000256|RuleBase:RU368119};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368119};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|EPD:A0A8I5KTS5,
KW   ECO:0007829|MaxQB:A0A8I5KTS5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU368119};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          129..218
FT                   /note="ILEI/PANDER"
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
//