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Protein O-mannosyl-transferase 1 (EC 2.4.1.109) (Dolichyl-phosphate-mannose--protein mannosyltransferase 1)

 POMT1_HUMAN             Reviewed;         747 AA.
Q9Y6A1; B3KQG0; B4DIF0; Q5JT01; Q5JT06; Q5JT08; Q8NC91; Q8TCA9;
Q9NX32; Q9NX82; Q9UNT2;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
03-MAY-2011, sequence version 3.
27-SEP-2017, entry version 162.
RecName: Full=Protein O-mannosyl-transferase 1;
EC=2.4.1.109;
AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
Name=POMT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2),
ALTERNATIVE SPLICING, AND VARIANT ARG-251.
TISSUE=Fetal brain;
PubMed=10366449; DOI=10.1006/geno.1999.5819;
Perez Jurado L.A., Coloma A., Cruces J.;
"Identification of a human homolog of the Drosophila rotated abdomen
gene (POMT1) encoding a putative protein O-mannosyl-transferase, and
assignment to human chromosome 9q34.1.";
Genomics 58:171-180(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 53-747 (ISOFORM 1), AND VARIANT
ARG-251.
TISSUE=Hippocampus, Ileal mucosa, Signet-ring cell carcinoma, and
Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND VARIANTS MDDGA1 ARG-76 AND ASP-428.
PubMed=12369018; DOI=10.1086/342975;
Beltran-Valero de Bernabe D., Currier S., Steinbrecher A., Celli J.,
van Beusekom E., van der Zwaag B., Kayserili H., Merlini L.,
Chitayat D., Dobyns W.B., Cormand B., Lehesjoki A.-E., Cruces J.,
Voit T., Walsh C.A., van Bokhoven H., Brunner H.G.;
"Mutations in the O-mannosyltransferase gene POMT1 give rise to the
severe neuronal migration disorder Walker-Warburg syndrome.";
Am. J. Hum. Genet. 71:1033-1043(2002).
[8]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=14699049; DOI=10.1073/pnas.0307228101;
Manya H., Chiba A., Yoshida A., Wang X., Chiba Y., Jigami Y.,
Margolis R.U., Endo T.;
"Demonstration of mammalian protein O-mannosyltransferase activity:
coexpression of POMT1 and POMT2 required for enzymatic activity.";
Proc. Natl. Acad. Sci. U.S.A. 101:500-505(2004).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-471.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
VARIANT MDDGA1 LEU-421 DEL.
PubMed=15037715; DOI=10.1212/01.WNL.0000115386.28769.65;
Kim D.-S., Hayashi Y.K., Matsumoto H., Ogawa M., Noguchi S.,
Murakami N., Sakuta R., Mochizuki M., Michele D.E., Campbell K.P.,
Nonaka I., Nishino I.;
"POMT1 mutation results in defective glycosylation and loss of
laminin-binding activity in alpha-DG.";
Neurology 62:1009-1011(2004).
[11]
VARIANT MDDGA1 ARG-537.
PubMed=15637732; DOI=10.1002/ajmg.a.30487;
Currier S.C., Lee C.K., Chang B.S., Bodell A.L., Pai G.S., Job L.,
Lagae L.G., Al-Gazali L.I., Eyaid W.M., Enns G., Dobyns W.B.,
Walsh C.A.;
"Mutations in POMT1 are found in a minority of patients with Walker-
Warburg syndrome.";
Am. J. Med. Genet. A 133:53-57(2005).
[12]
VARIANT MDDGC1 PRO-200.
PubMed=15792865; DOI=10.1016/j.nmd.2005.01.013;
Balci B., Uyanik G., Dincer P., Gross C., Willer T., Talim B.,
Haliloglu G., Kale G., Hehr U., Winkler J., Topaloglu H.;
"An autosomal recessive limb girdle muscular dystrophy (LGMD2) with
mild mental retardation is allelic to Walker-Warburg syndrome (WWS)
caused by a mutation in the POMT1 gene.";
Neuromuscul. Disord. 15:271-275(2005).
[13]
VARIANTS MDDGB1 ARG-65; MET-140 DEL; CYS-582 AND HIS-590, VARIANTS
MDDGA1 CYS-105; HIS-105 AND VAL-207, AND VARIANTS PHE-285 AND LYS-522.
PubMed=16575835; DOI=10.1002/humu.20313;
van Reeuwijk J., Maugenre S., van den Elzen C., Verrips A.,
Bertini E., Muntoni F., Merlini L., Scheffer H., Brunner H.G.,
Guicheney P., van Bokhoven H.;
"The expanding phenotype of POMT1 mutations: from Walker-Warburg
syndrome to congenital muscular dystrophy, microcephaly, and mental
retardation.";
Hum. Mutat. 27:453-459(2006).
[14]
VARIANTS MDDGB1 ARG-65; HIS-590 AND THR-669.
PubMed=16717220; DOI=10.1212/01.wnl.0000216145.66476.36;
D'Amico A., Tessa A., Bruno C., Petrini S., Biancheri R., Pane M.,
Pedemonte M., Ricci E., Falace A., Rossi A., Mercuri E.,
Santorelli F.M., Bertini E.;
"Expanding the clinical spectrum of POMT1 phenotype.";
Neurology 66:1564-1567(2006).
[15]
VARIANTS MDDGB1 ARG-65 AND ARG-537.
PubMed=19299310; DOI=10.1212/01.wnl.0000346518.68110.60;
Mercuri E., Messina S., Bruno C., Mora M., Pegoraro E., Comi G.P.,
D'Amico A., Aiello C., Biancheri R., Berardinelli A., Boffi P.,
Cassandrini D., Laverda A., Moggio M., Morandi L., Moroni I., Pane M.,
Pezzani R., Pichiecchio A., Pini A., Minetti C., Mongini T.,
Mottarelli E., Ricci E., Ruggieri A., Saredi S., Scuderi C., Tessa A.,
Toscano A., Tortorella G., Trevisan C.P., Uggetti C., Vasco G.,
Santorelli F.M., Bertini E.;
"Congenital muscular dystrophies with defective glycosylation of
dystroglycan: a population study.";
Neurology 72:1802-1809(2009).
-!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of
serine or threonine residues. Coexpression of both POMT1 and POMT2
is necessary for enzyme activity, expression of either POMT1 or
POMT2 alone is insufficient. {ECO:0000269|PubMed:12369018,
ECO:0000269|PubMed:14699049}.
-!- CATALYTIC ACTIVITY: Dolichyl D-mannosyl phosphate + protein =
dolichyl phosphate + O-D-mannosylprotein.
{ECO:0000269|PubMed:14699049}.
-!- ENZYME REGULATION: Slightly activated by Mg(2+) and inhibited by
both Ca(+) and Mn(2+). EDTA ha no effect on activity in vitro.
{ECO:0000269|PubMed:14699049}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Interacts with POMT2. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14699049}; Multi-pass membrane protein
{ECO:0000269|PubMed:14699049}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9Y6A1-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6A1-2; Sequence=VSP_007591;
Name=3;
IsoId=Q9Y6A1-3; Sequence=VSP_007590, VSP_007591;
Name=4;
IsoId=Q9Y6A1-4; Sequence=VSP_041024, VSP_007591;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis,
heart and pancreas. Detected at lower levels in kidney, skeletal
muscle, brain, placenta, lung and liver.
-!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with
mental retardation B1 (MDDGB1) [MIM:613155]: An autosomal
recessive disorder characterized by congenital muscular dystrophy
associated with mental retardation and mild structural brain
abnormalities. {ECO:0000269|PubMed:16575835,
ECO:0000269|PubMed:16717220, ECO:0000269|PubMed:19299310}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with
brain and eye anomalies A1 (MDDGA1) [MIM:236670]: An autosomal
recessive disorder characterized by congenital muscular dystrophy
associated with cobblestone lissencephaly and other brain
anomalies, eye malformations, profound mental retardation, and
death usually in the first years of life. Included diseases are
the more severe Walker-Warburg syndrome and the slightly less
severe muscle-eye-brain disease. {ECO:0000269|PubMed:12369018,
ECO:0000269|PubMed:15037715, ECO:0000269|PubMed:15637732,
ECO:0000269|PubMed:16575835}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C1
(MDDGC1) [MIM:609308]: An autosomal recessive degenerative
myopathy associated with mild mental retardation without any
obvious structural brain abnormality. An abnormal alpha-
dystroglycan pattern in observed in the muscle.
{ECO:0000269|PubMed:15792865}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91135.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA91190.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF095136; AAD41245.1; -; mRNA.
EMBL; AF095150; AAD41246.1; -; Genomic_DNA.
EMBL; AF095138; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095139; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095140; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095141; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095142; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095143; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095144; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095145; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095146; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095147; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095148; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AF095149; AAD41246.1; JOINED; Genomic_DNA.
EMBL; AK000391; BAA91135.1; ALT_INIT; mRNA.
EMBL; AK000475; BAA91190.1; ALT_INIT; mRNA.
EMBL; AK295561; BAG58462.1; -; mRNA.
EMBL; AK074874; BAG52022.1; -; mRNA.
EMBL; AK074888; BAC11269.1; -; mRNA.
EMBL; AL358781; CAI40220.1; -; Genomic_DNA.
EMBL; AL358781; CAI40221.1; -; Genomic_DNA.
EMBL; AL358781; CAI40223.1; -; Genomic_DNA.
EMBL; CH471090; EAW87978.1; -; Genomic_DNA.
EMBL; BC022877; AAH22877.3; -; mRNA.
EMBL; BC065268; AAH65268.1; -; mRNA.
CCDS; CCDS43894.1; -. [Q9Y6A1-2]
CCDS; CCDS43895.1; -. [Q9Y6A1-3]
CCDS; CCDS48045.1; -. [Q9Y6A1-4]
CCDS; CCDS6943.1; -. [Q9Y6A1-1]
RefSeq; NP_001070833.1; NM_001077365.1. [Q9Y6A1-2]
RefSeq; NP_001070834.1; NM_001077366.1. [Q9Y6A1-3]
RefSeq; NP_001129585.1; NM_001136113.1. [Q9Y6A1-2]
RefSeq; NP_001129586.1; NM_001136114.1. [Q9Y6A1-4]
RefSeq; NP_009102.3; NM_007171.3.
RefSeq; XP_005272213.1; XM_005272156.1. [Q9Y6A1-1]
UniGene; Hs.522449; -.
ProteinModelPortal; Q9Y6A1; -.
BioGrid; 115834; 37.
IntAct; Q9Y6A1; 2.
STRING; 9606.ENSP00000361302; -.
CAZy; GT39; Glycosyltransferase Family 39.
iPTMnet; Q9Y6A1; -.
PhosphoSitePlus; Q9Y6A1; -.
BioMuta; POMT1; -.
DMDM; 332278226; -.
PaxDb; Q9Y6A1; -.
PeptideAtlas; Q9Y6A1; -.
PRIDE; Q9Y6A1; -.
Ensembl; ENST00000341012; ENSP00000343034; ENSG00000130714. [Q9Y6A1-3]
Ensembl; ENST00000372228; ENSP00000361302; ENSG00000130714. [Q9Y6A1-1]
Ensembl; ENST00000402686; ENSP00000385797; ENSG00000130714. [Q9Y6A1-2]
Ensembl; ENST00000404875; ENSP00000384531; ENSG00000130714. [Q9Y6A1-4]
Ensembl; ENST00000423007; ENSP00000404119; ENSG00000130714. [Q9Y6A1-2]
GeneID; 10585; -.
KEGG; hsa:10585; -.
UCSC; uc004cau.4; human. [Q9Y6A1-1]
CTD; 10585; -.
DisGeNET; 10585; -.
EuPathDB; HostDB:ENSG00000130714.15; -.
GeneCards; POMT1; -.
GeneReviews; POMT1; -.
HGNC; HGNC:9202; POMT1.
HPA; HPA065252; -.
MalaCards; POMT1; -.
MIM; 236670; phenotype.
MIM; 607423; gene.
MIM; 609308; phenotype.
MIM; 613155; phenotype.
neXtProt; NX_Q9Y6A1; -.
OpenTargets; ENSG00000130714; -.
Orphanet; 86812; Autosomal recessive limb-girdle muscular dystrophy type 2K.
Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement.
Orphanet; 370968; Congenital muscular dystrophy with intellectual disability.
Orphanet; 370980; Congenital muscular dystrophy without intellectual disability.
Orphanet; 588; Muscle-eye-brain disease.
Orphanet; 899; Walker-Warburg syndrome.
PharmGKB; PA33527; -.
eggNOG; KOG3359; Eukaryota.
eggNOG; COG1928; LUCA.
GeneTree; ENSGT00870000136482; -.
HOVERGEN; HBG053637; -.
InParanoid; Q9Y6A1; -.
KO; K00728; -.
OMA; WWIVKDP; -.
OrthoDB; EOG091G02QX; -.
PhylomeDB; Q9Y6A1; -.
TreeFam; TF300552; -.
BRENDA; 2.4.1.109; 2681.
Reactome; R-HSA-5173105; O-linked glycosylation.
UniPathway; UPA00378; -.
ChiTaRS; POMT1; human.
GeneWiki; POMT1; -.
GenomeRNAi; 10585; -.
PRO; PR:Q9Y6A1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000130714; -.
ExpressionAtlas; Q9Y6A1; baseline and differential.
Genevisible; Q9Y6A1; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
GO; GO:0000030; F:mannosyltransferase activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IEA:Ensembl.
GO; GO:0006493; P:protein O-linked glycosylation; TAS:Reactome.
InterPro; IPR027005; GlyclTrfase_39-like.
InterPro; IPR003342; Glyco_trans_39/83.
InterPro; IPR016093; MIR_motif.
InterPro; IPR032421; PMT_4TMC.
PANTHER; PTHR10050; PTHR10050; 1.
Pfam; PF02815; MIR; 1.
Pfam; PF02366; PMT; 1.
Pfam; PF16192; PMT_4TMC; 1.
SMART; SM00472; MIR; 3.
SUPFAM; SSF82109; SSF82109; 1.
PROSITE; PS50919; MIR; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome;
Congenital muscular dystrophy; Disease mutation; Dystroglycanopathy;
Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
Limb-girdle muscular dystrophy; Lissencephaly; Membrane;
Metal-binding; Polymorphism; Reference proteome; Repeat; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 747 Protein O-mannosyl-transferase 1.
/FTId=PRO_0000121484.
TRANSMEM 8 28 Helical. {ECO:0000255}.
TRANSMEM 40 60 Helical. {ECO:0000255}.
TRANSMEM 68 88 Helical. {ECO:0000255}.
TRANSMEM 99 119 Helical. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TRANSMEM 154 174 Helical. {ECO:0000255}.
TRANSMEM 183 203 Helical. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TRANSMEM 269 289 Helical. {ECO:0000255}.
TRANSMEM 597 617 Helical. {ECO:0000255}.
TRANSMEM 636 656 Helical. {ECO:0000255}.
TRANSMEM 661 681 Helical. {ECO:0000255}.
DOMAIN 318 381 MIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 392 449 MIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 453 513 MIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 539 539 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 117 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041024.
VAR_SEQ 1 54 Missing (in isoform 3).
{ECO:0000303|PubMed:16303743}.
/FTId=VSP_007590.
VAR_SEQ 234 255 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:10366449,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16303743}.
/FTId=VSP_007591.
VARIANT 65 65 G -> R (in MDDGB1; dbSNP:rs119462983).
{ECO:0000269|PubMed:16575835,
ECO:0000269|PubMed:16717220,
ECO:0000269|PubMed:19299310}.
/FTId=VAR_065027.
VARIANT 76 76 G -> R (in MDDGA1; dbSNP:rs28941782).
{ECO:0000269|PubMed:12369018}.
/FTId=VAR_015734.
VARIANT 105 105 R -> C (in MDDGA1; severe Walker-Warburg
syndrome). {ECO:0000269|PubMed:16575835}.
/FTId=VAR_065028.
VARIANT 105 105 R -> H (in MDDGA1; severe Walker-Warburg
syndrome). {ECO:0000269|PubMed:16575835}.
/FTId=VAR_065029.
VARIANT 140 140 Missing (in MDDGB1).
{ECO:0000269|PubMed:16575835}.
/FTId=VAR_065030.
VARIANT 200 200 A -> P (in MDDGC1; a common founder
mutation; dbSNP:rs119462982).
{ECO:0000269|PubMed:15792865}.
/FTId=VAR_022661.
VARIANT 207 207 G -> V (in MDDGA1; severe Walker-Warburg
syndrome). {ECO:0000269|PubMed:16575835}.
/FTId=VAR_065031.
VARIANT 251 251 Q -> R (in dbSNP:rs2296949).
{ECO:0000269|PubMed:10366449,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_034390.
VARIANT 251 251 Q -> W (requires 2 nucleotide
substitutions; dbSNP:rs3887873).
/FTId=VAR_034389.
VARIANT 285 285 L -> F (in dbSNP:rs201073763).
{ECO:0000269|PubMed:16575835}.
/FTId=VAR_065032.
VARIANT 327 327 V -> I (in dbSNP:rs4740164).
/FTId=VAR_034391.
VARIANT 421 421 Missing (in MDDGA1; associated with the
loss of function of alpha dystroglycan as
a matrix receptor).
{ECO:0000269|PubMed:15037715}.
/FTId=VAR_022662.
VARIANT 428 428 V -> D (in MDDGA1).
{ECO:0000269|PubMed:12369018}.
/FTId=VAR_015735.
VARIANT 433 433 D -> E (in dbSNP:rs11243406).
/FTId=VAR_034392.
VARIANT 522 522 R -> K (in dbSNP:rs117985576).
{ECO:0000269|PubMed:16575835}.
/FTId=VAR_065033.
VARIANT 537 537 S -> R (in MDDGA1 and MDDGB1;
dbSNP:rs150367385).
{ECO:0000269|PubMed:15637732,
ECO:0000269|PubMed:19299310}.
/FTId=VAR_026697.
VARIANT 582 582 W -> C (in MDDGB1; dbSNP:rs119462984).
{ECO:0000269|PubMed:16575835}.
/FTId=VAR_065034.
VARIANT 590 590 Q -> H (in MDDGB1; dbSNP:rs119462986).
{ECO:0000269|PubMed:16575835,
ECO:0000269|PubMed:16717220}.
/FTId=VAR_065035.
VARIANT 669 669 A -> T (in MDDGB1; dbSNP:rs119462987).
{ECO:0000269|PubMed:16717220}.
/FTId=VAR_065036.
CONFLICT 37 37 P -> Q (in Ref. 6; AAH22877).
{ECO:0000305}.
CONFLICT 143 143 E -> K (in Ref. 1; AAD41245).
{ECO:0000305}.
CONFLICT 147 147 I -> V (in Ref. 2; BAG58462).
{ECO:0000305}.
CONFLICT 178 178 K -> E (in Ref. 6; AAH22877).
{ECO:0000305}.
CONFLICT 377 377 I -> V (in Ref. 6; AAH22877).
{ECO:0000305}.
CONFLICT 665 665 H -> L (in Ref. 3; BAC11269).
{ECO:0000305}.
CONFLICT 696 697 SI -> NS (in Ref. 1; AAD41245).
{ECO:0000305}.
CONFLICT 739 739 S -> G (in Ref. 2; BAA91135).
{ECO:0000305}.
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


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