POMT1_HUMAN
ID POMT1_HUMAN Reviewed; 747 AA.
AC Q9Y6A1; B3KQG0; B4DIF0; Q5JT01; Q5JT06; Q5JT08; Q8NC91; Q8TCA9; Q9NX32;
AC Q9NX82; Q9UNT2;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Protein O-mannosyl-transferase 1;
DE EC=2.4.1.109 {ECO:0000269|PubMed:14699049, ECO:0000269|PubMed:28512129};
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
GN Name=POMT1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE
RP SPLICING, AND VARIANT ARG-251.
RC TISSUE=Fetal brain;
RX PubMed=10366449; DOI=10.1006/geno.1999.5819;
RA Perez Jurado L.A., Coloma A., Cruces J.;
RT "Identification of a human homolog of the Drosophila rotated abdomen gene
RT (POMT1) encoding a putative protein O-mannosyl-transferase, and assignment
RT to human chromosome 9q34.1.";
RL Genomics 58:171-180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 53-747 (ISOFORM 1), AND VARIANT ARG-251.
RC TISSUE=Hippocampus, Ileal mucosa, Signet-ring cell carcinoma, and
RC Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND VARIANTS MDDGA1 ARG-76 AND ASP-428.
RX PubMed=12369018; DOI=10.1086/342975;
RA Beltran-Valero de Bernabe D., Currier S., Steinbrecher A., Celli J.,
RA van Beusekom E., van der Zwaag B., Kayserili H., Merlini L., Chitayat D.,
RA Dobyns W.B., Cormand B., Lehesjoki A.-E., Cruces J., Voit T., Walsh C.A.,
RA van Bokhoven H., Brunner H.G.;
RT "Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe
RT neuronal migration disorder Walker-Warburg syndrome.";
RL Am. J. Hum. Genet. 71:1033-1043(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14699049; DOI=10.1073/pnas.0307228101;
RA Manya H., Chiba A., Yoshida A., Wang X., Chiba Y., Jigami Y.,
RA Margolis R.U., Endo T.;
RT "Demonstration of mammalian protein O-mannosyltransferase activity:
RT coexpression of POMT1 and POMT2 required for enzymatic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:500-505(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-471.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28512129; DOI=10.1074/jbc.m117.794487;
RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Yang Z., Harrison O.J., Brasch J.,
RA Shapiro L., Honig B., Vakhrushev S.Y., Clausen H., Halim A.;
RT "Mammalian O-mannosylation of cadherins and plexins is independent of
RT protein O-mannosyltransferases 1 and 2.";
RL J. Biol. Chem. 292:11586-11598(2017).
RN [11]
RP VARIANT MDDGA1 LEU-421 DEL.
RX PubMed=15037715; DOI=10.1212/01.wnl.0000115386.28769.65;
RA Kim D.-S., Hayashi Y.K., Matsumoto H., Ogawa M., Noguchi S., Murakami N.,
RA Sakuta R., Mochizuki M., Michele D.E., Campbell K.P., Nonaka I.,
RA Nishino I.;
RT "POMT1 mutation results in defective glycosylation and loss of laminin-
RT binding activity in alpha-DG.";
RL Neurology 62:1009-1011(2004).
RN [12]
RP VARIANT MDDGA1 ARG-537.
RX PubMed=15637732; DOI=10.1002/ajmg.a.30487;
RA Currier S.C., Lee C.K., Chang B.S., Bodell A.L., Pai G.S., Job L.,
RA Lagae L.G., Al-Gazali L.I., Eyaid W.M., Enns G., Dobyns W.B., Walsh C.A.;
RT "Mutations in POMT1 are found in a minority of patients with Walker-Warburg
RT syndrome.";
RL Am. J. Med. Genet. A 133:53-57(2005).
RN [13]
RP VARIANT MDDGC1 PRO-200.
RX PubMed=15792865; DOI=10.1016/j.nmd.2005.01.013;
RA Balci B., Uyanik G., Dincer P., Gross C., Willer T., Talim B.,
RA Haliloglu G., Kale G., Hehr U., Winkler J., Topaloglu H.;
RT "An autosomal recessive limb girdle muscular dystrophy (LGMD2) with mild
RT mental retardation is allelic to Walker-Warburg syndrome (WWS) caused by a
RT mutation in the POMT1 gene.";
RL Neuromuscul. Disord. 15:271-275(2005).
RN [14]
RP VARIANTS MDDGB1 ARG-65; MET-140 DEL; CYS-582 AND HIS-590, VARIANTS MDDGA1
RP CYS-105; HIS-105 AND VAL-207, AND VARIANTS PHE-285 AND LYS-522.
RX PubMed=16575835; DOI=10.1002/humu.20313;
RA van Reeuwijk J., Maugenre S., van den Elzen C., Verrips A., Bertini E.,
RA Muntoni F., Merlini L., Scheffer H., Brunner H.G., Guicheney P.,
RA van Bokhoven H.;
RT "The expanding phenotype of POMT1 mutations: from Walker-Warburg syndrome
RT to congenital muscular dystrophy, microcephaly, and mental retardation.";
RL Hum. Mutat. 27:453-459(2006).
RN [15]
RP VARIANTS MDDGB1 ARG-65; HIS-590 AND THR-669.
RX PubMed=16717220; DOI=10.1212/01.wnl.0000216145.66476.36;
RA D'Amico A., Tessa A., Bruno C., Petrini S., Biancheri R., Pane M.,
RA Pedemonte M., Ricci E., Falace A., Rossi A., Mercuri E., Santorelli F.M.,
RA Bertini E.;
RT "Expanding the clinical spectrum of POMT1 phenotype.";
RL Neurology 66:1564-1567(2006).
RN [16]
RP VARIANTS MDDGB1 ARG-65 AND ARG-537.
RX PubMed=19299310; DOI=10.1212/01.wnl.0000346518.68110.60;
RA Mercuri E., Messina S., Bruno C., Mora M., Pegoraro E., Comi G.P.,
RA D'Amico A., Aiello C., Biancheri R., Berardinelli A., Boffi P.,
RA Cassandrini D., Laverda A., Moggio M., Morandi L., Moroni I., Pane M.,
RA Pezzani R., Pichiecchio A., Pini A., Minetti C., Mongini T., Mottarelli E.,
RA Ricci E., Ruggieri A., Saredi S., Scuderi C., Tessa A., Toscano A.,
RA Tortorella G., Trevisan C.P., Uggetti C., Vasco G., Santorelli F.M.,
RA Bertini E.;
RT "Congenital muscular dystrophies with defective glycosylation of
RT dystroglycan: a population study.";
RL Neurology 72:1802-1809(2009).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. Coexpression of both POMT1 and POMT2 is
CC necessary for enzyme activity, expression of either POMT1 or POMT2
CC alone is insufficient (PubMed:12369018, PubMed:14699049,
CC PubMed:28512129). Essentially dedicated to O-mannosylation of alpha-
CC DAG1 and few other proteins but not of cadherins and protocaherins
CC (PubMed:28512129). {ECO:0000269|PubMed:12369018,
CC ECO:0000269|PubMed:14699049, ECO:0000269|PubMed:28512129}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:14699049, ECO:0000269|PubMed:28512129};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:14699049, ECO:0000269|PubMed:28512129};
CC -!- ACTIVITY REGULATION: Slightly activated by Mg(2+) and inhibited by both
CC Ca(+) and Mn(2+). EDTA ha no effect on activity in vitro.
CC {ECO:0000269|PubMed:14699049}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with POMT2. {ECO:0000305}.
CC -!- INTERACTION:
CC Q9Y6A1-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12337033, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14699049}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14699049}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9Y6A1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6A1-2; Sequence=VSP_007591;
CC Name=3;
CC IsoId=Q9Y6A1-3; Sequence=VSP_007590, VSP_007591;
CC Name=4;
CC IsoId=Q9Y6A1-4; Sequence=VSP_041024, VSP_007591;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, heart
CC and pancreas. Detected at lower levels in kidney, skeletal muscle,
CC brain, placenta, lung and liver.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with impaired
CC intellectual development B1 (MDDGB1) [MIM:613155]: An autosomal
CC recessive disorder characterized by congenital muscular dystrophy
CC associated with intellectual disability and mild structural brain
CC abnormalities. {ECO:0000269|PubMed:16575835,
CC ECO:0000269|PubMed:16717220, ECO:0000269|PubMed:19299310}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC and eye anomalies A1 (MDDGA1) [MIM:236670]: An autosomal recessive
CC disorder characterized by congenital muscular dystrophy associated with
CC cobblestone lissencephaly and other brain anomalies, eye malformations,
CC profound intellectual disability, and death usually in the first years
CC of life. Included diseases are the more severe Walker-Warburg syndrome
CC and the slightly less severe muscle-eye-brain disease.
CC {ECO:0000269|PubMed:12369018, ECO:0000269|PubMed:15037715,
CC ECO:0000269|PubMed:15637732, ECO:0000269|PubMed:16575835}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C1 (MDDGC1)
CC [MIM:609308]: An autosomal recessive degenerative myopathy associated
CC with mild intellectual disability without any obvious structural brain
CC abnormality. An abnormal alpha-dystroglycan pattern in observed in the
CC muscle. {ECO:0000269|PubMed:15792865}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91135.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91190.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF095136; AAD41245.1; -; mRNA.
DR EMBL; AF095150; AAD41246.1; -; Genomic_DNA.
DR EMBL; AF095138; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095139; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095140; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095141; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095142; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095143; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095144; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095145; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095146; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095147; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095148; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AF095149; AAD41246.1; JOINED; Genomic_DNA.
DR EMBL; AK000391; BAA91135.1; ALT_INIT; mRNA.
DR EMBL; AK000475; BAA91190.1; ALT_INIT; mRNA.
DR EMBL; AK295561; BAG58462.1; -; mRNA.
DR EMBL; AK074874; BAG52022.1; -; mRNA.
DR EMBL; AK074888; BAC11269.1; -; mRNA.
DR EMBL; AL358781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87978.1; -; Genomic_DNA.
DR EMBL; BC022877; AAH22877.3; -; mRNA.
DR EMBL; BC065268; AAH65268.1; -; mRNA.
DR CCDS; CCDS43894.1; -. [Q9Y6A1-2]
DR CCDS; CCDS43895.1; -. [Q9Y6A1-3]
DR CCDS; CCDS48045.1; -. [Q9Y6A1-4]
DR CCDS; CCDS6943.1; -. [Q9Y6A1-1]
DR RefSeq; NP_001070833.1; NM_001077365.1. [Q9Y6A1-2]
DR RefSeq; NP_001070834.1; NM_001077366.1. [Q9Y6A1-3]
DR RefSeq; NP_001129585.1; NM_001136113.1. [Q9Y6A1-2]
DR RefSeq; NP_001129586.1; NM_001136114.1. [Q9Y6A1-4]
DR RefSeq; NP_009102.3; NM_007171.3. [Q9Y6A1-1]
DR RefSeq; XP_005272213.1; XM_005272156.1.
DR AlphaFoldDB; Q9Y6A1; -.
DR SMR; Q9Y6A1; -.
DR BioGRID; 115834; 57.
DR IntAct; Q9Y6A1; 28.
DR STRING; 9606.ENSP00000361302; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyGen; Q9Y6A1; 3 sites.
DR iPTMnet; Q9Y6A1; -.
DR PhosphoSitePlus; Q9Y6A1; -.
DR BioMuta; POMT1; -.
DR DMDM; 332278226; -.
DR EPD; Q9Y6A1; -.
DR jPOST; Q9Y6A1; -.
DR MassIVE; Q9Y6A1; -.
DR MaxQB; Q9Y6A1; -.
DR PaxDb; Q9Y6A1; -.
DR PeptideAtlas; Q9Y6A1; -.
DR PRIDE; Q9Y6A1; -.
DR ProteomicsDB; 86636; -. [Q9Y6A1-1]
DR ProteomicsDB; 86637; -. [Q9Y6A1-2]
DR ProteomicsDB; 86638; -. [Q9Y6A1-3]
DR ProteomicsDB; 86639; -. [Q9Y6A1-4]
DR Antibodypedia; 31602; 191 antibodies from 27 providers.
DR DNASU; 10585; -.
DR Ensembl; ENST00000341012.13; ENSP00000343034.7; ENSG00000130714.19. [Q9Y6A1-3]
DR Ensembl; ENST00000372228.9; ENSP00000361302.3; ENSG00000130714.19. [Q9Y6A1-1]
DR Ensembl; ENST00000402686.8; ENSP00000385797.4; ENSG00000130714.19. [Q9Y6A1-2]
DR Ensembl; ENST00000676640.1; ENSP00000503281.1; ENSG00000130714.19. [Q9Y6A1-2]
DR Ensembl; ENST00000677216.1; ENSP00000503772.1; ENSG00000130714.19. [Q9Y6A1-4]
DR Ensembl; ENST00000679023.1; ENSP00000503718.1; ENSG00000130714.19. [Q9Y6A1-3]
DR Ensembl; ENST00000679189.1; ENSP00000503356.1; ENSG00000130714.19. [Q9Y6A1-4]
DR GeneID; 10585; -.
DR KEGG; hsa:10585; -.
DR MANE-Select; ENST00000402686.8; ENSP00000385797.4; NM_001077365.2; NP_001070833.1. [Q9Y6A1-2]
DR UCSC; uc004cau.4; human. [Q9Y6A1-1]
DR CTD; 10585; -.
DR DisGeNET; 10585; -.
DR GeneCards; POMT1; -.
DR HGNC; HGNC:9202; POMT1.
DR HPA; ENSG00000130714; Low tissue specificity.
DR MalaCards; POMT1; -.
DR MIM; 236670; phenotype.
DR MIM; 607423; gene.
DR MIM; 609308; phenotype.
DR MIM; 613155; phenotype.
DR neXtProt; NX_Q9Y6A1; -.
DR OpenTargets; ENSG00000130714; -.
DR Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement.
DR Orphanet; 370968; Congenital muscular dystrophy with intellectual disability.
DR Orphanet; 370980; Congenital muscular dystrophy without intellectual disability.
DR Orphanet; 588; Muscle-eye-brain disease.
DR Orphanet; 86812; POMT1-related limb-girdle muscular dystrophy R11.
DR Orphanet; 899; Walker-Warburg syndrome.
DR PharmGKB; PA33527; -.
DR VEuPathDB; HostDB:ENSG00000130714; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000158049; -.
DR HOGENOM; CLU_008438_1_0_1; -.
DR InParanoid; Q9Y6A1; -.
DR OMA; FWTQNDT; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q9Y6A1; -.
DR TreeFam; TF300552; -.
DR BioCyc; MetaCyc:HS05428-MON; -.
DR BRENDA; 2.4.1.109; 2681.
DR PathwayCommons; Q9Y6A1; -.
DR Reactome; R-HSA-5083629; Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2.
DR Reactome; R-HSA-5083633; Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1.
DR Reactome; R-HSA-5173105; O-linked glycosylation.
DR SignaLink; Q9Y6A1; -.
DR SIGNOR; Q9Y6A1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 10585; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; POMT1; human.
DR GeneWiki; POMT1; -.
DR GenomeRNAi; 10585; -.
DR Pharos; Q9Y6A1; Tbio.
DR PRO; PR:Q9Y6A1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y6A1; protein.
DR Bgee; ENSG00000130714; Expressed in right hemisphere of cerebellum and 176 other tissues.
DR ExpressionAtlas; Q9Y6A1; baseline and differential.
DR Genevisible; Q9Y6A1; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; TAS:ProtInc.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:UniProtKB.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; SSF82109; 1.
DR PROSITE; PS50919; MIR; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital muscular dystrophy; Disease variant;
KW Dystroglycanopathy; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Limb-girdle muscular dystrophy; Lissencephaly;
KW Membrane; Metal-binding; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..747
FT /note="Protein O-mannosyl-transferase 1"
FT /id="PRO_0000121484"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 318..381
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 392..449
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 453..513
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041024"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_007590"
FT VAR_SEQ 234..255
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10366449,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16303743"
FT /id="VSP_007591"
FT VARIANT 65
FT /note="G -> R (in MDDGB1; dbSNP:rs119462983)"
FT /evidence="ECO:0000269|PubMed:16575835,
FT ECO:0000269|PubMed:16717220, ECO:0000269|PubMed:19299310"
FT /id="VAR_065027"
FT VARIANT 76
FT /note="G -> R (in MDDGA1; dbSNP:rs28941782)"
FT /evidence="ECO:0000269|PubMed:12369018"
FT /id="VAR_015734"
FT VARIANT 105
FT /note="R -> C (in MDDGA1; severe Walker-Warburg syndrome;
FT dbSNP:rs1289335417)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065028"
FT VARIANT 105
FT /note="R -> H (in MDDGA1; severe Walker-Warburg syndrome;
FT dbSNP:rs1554772469)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065029"
FT VARIANT 140
FT /note="Missing (in MDDGB1; dbSNP:rs587777820)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065030"
FT VARIANT 200
FT /note="A -> P (in MDDGC1; a common founder mutation;
FT dbSNP:rs119462982)"
FT /evidence="ECO:0000269|PubMed:15792865"
FT /id="VAR_022661"
FT VARIANT 207
FT /note="G -> V (in MDDGA1; severe Walker-Warburg syndrome)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065031"
FT VARIANT 251
FT /note="Q -> R (in dbSNP:rs2296949)"
FT /evidence="ECO:0000269|PubMed:10366449,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_034390"
FT VARIANT 251
FT /note="Q -> W (requires 2 nucleotide substitutions;
FT dbSNP:rs386738991)"
FT /id="VAR_034389"
FT VARIANT 285
FT /note="L -> F (in dbSNP:rs201073763)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065032"
FT VARIANT 327
FT /note="V -> I (in dbSNP:rs4740164)"
FT /id="VAR_034391"
FT VARIANT 421
FT /note="Missing (in MDDGA1; associated with the loss of
FT function of alpha dystroglycan as a matrix receptor)"
FT /evidence="ECO:0000269|PubMed:15037715"
FT /id="VAR_022662"
FT VARIANT 428
FT /note="V -> D (in MDDGA1)"
FT /evidence="ECO:0000269|PubMed:12369018"
FT /id="VAR_015735"
FT VARIANT 433
FT /note="D -> E (in dbSNP:rs11243406)"
FT /id="VAR_034392"
FT VARIANT 522
FT /note="R -> K (in dbSNP:rs117985576)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065033"
FT VARIANT 537
FT /note="S -> R (in MDDGA1 and MDDGB1; likely benign variant;
FT dbSNP:rs150367385)"
FT /evidence="ECO:0000269|PubMed:15637732,
FT ECO:0000269|PubMed:19299310"
FT /id="VAR_026697"
FT VARIANT 582
FT /note="W -> C (in MDDGB1; dbSNP:rs119462984)"
FT /evidence="ECO:0000269|PubMed:16575835"
FT /id="VAR_065034"
FT VARIANT 590
FT /note="Q -> H (in MDDGB1; dbSNP:rs119462986)"
FT /evidence="ECO:0000269|PubMed:16575835,
FT ECO:0000269|PubMed:16717220"
FT /id="VAR_065035"
FT VARIANT 669
FT /note="A -> T (in MDDGB1; dbSNP:rs119462987)"
FT /evidence="ECO:0000269|PubMed:16717220"
FT /id="VAR_065036"
FT CONFLICT 37
FT /note="P -> Q (in Ref. 6; AAH22877)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> K (in Ref. 1; AAD41245)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="I -> V (in Ref. 2; BAG58462)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="K -> E (in Ref. 6; AAH22877)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="I -> V (in Ref. 6; AAH22877)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="H -> L (in Ref. 3; BAC11269)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..697
FT /note="SI -> NS (in Ref. 1; AAD41245)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="S -> G (in Ref. 2; BAA91135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 84881 MW; 6E1D26C87FF5D9C5 CRC64;
MWGFLKRPVV VTADINLSLV ALTGMGLLSR LWRLTYPRAV VFDEVYYGQY ISFYMKQIFF
LDDSGPPFGH MVLALGGYLG GFDGNFLWNR IGAEYSSNVP VWSLRLLPAL AGALSVPMAY
QIVLELHFSH CAAMGAALLM LIENALITQS RLMLLESVLI FFNLLAVLSY LKFFNCQKHS
PFSLSWWFWL TLTGVACSCA VGIKYMGVFT YVLVLGVAAV HAWHLLGDQT LSNVGADVQC
CMRPACMGQM QMSQGVCVFC HLLARAVALL VIPVVLYLLF FYVHLILVFR SGPHDQIMSS
AFQASLEGGL ARITQGQPLE VAFGSQVTLR NVFGKPVPCW LHSHQDTYPM IYENGRGSSH
QQQVTCYPFK DVNNWWIVKD PRRHQLVVSS PPRPVRHGDM VQLVHGMTTR SLNTHDVAAP
LSPHSQEVSC YIDYNISMPA QNLWRLEIVN RGSDTDVWKT ILSEVRFVHV NTSAVLKLSG
AHLPDWGYRQ LEIVGEKLSR GYHGSTVWNV EEHRYGASQE QRERERELHS PAQVDVSRNL
SFMARFSELQ WRMLALRSDD SEHKYSSSPL EWVTLDTNIA YWLHPRTSAQ IHLLGNIVIW
VSGSLALAIY ALLSLWYLLR RRRNVHDLPQ DAWLRWVLAG ALCAGGWAVN YLPFFLMEKT
LFLYHYLPAL TFQILLLPVV LQHISDHLCR SQLQRSIFSA LVVAWYSSAC HVSNTLRPLT
YGDKSLSPHE LKALRWKDSW DILIRKH
