POMT2_HUMAN
ID POMT2_HUMAN Reviewed; 750 AA.
AC Q9UKY4; Q9NSG6; Q9P1W0; Q9P1W2;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Protein O-mannosyl-transferase 2;
DE EC=2.4.1.109 {ECO:0000269|PubMed:14699049, ECO:0000269|PubMed:28512129};
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
GN Name=POMT2;
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] (ISOFORM 1), GLYCOSYLATION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Cerebellum;
RX PubMed=12460945; DOI=10.1093/glycob/cwf086;
RA Willer T., Amselgruber W., Deutzmann R., Strahl S.;
RT "Characterization of POMT2, a novel member of the PMT protein O-
RT mannosyltransferase family specifically localized to the acrosome of
RT mammalian spermatids.";
RL Glycobiology 12:771-783(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 612-750.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
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 [7]
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 [8]
RP INVOLVEMENT IN MDDGA2.
RX PubMed=15894594; DOI=10.1136/jmg.2005.031963;
RA van Reeuwijk J., Janssen M., van den Elzen C.,
RA Beltran-Valero de Bernabe D., Sabatelli P., Merlini L., Boon M.,
RA Scheffer H., Brockington M., Muntoni F., Huynen M.A., Verrips A.,
RA Walsh C.A., Barth P.G., Brunner H.G., van Bokhoven H.;
RT "POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-
RT Warburg syndrome.";
RL J. Med. Genet. 42:907-912(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP VARIANTS MDDGA2 SER-353 AND GLU-726.
RX PubMed=16701995; DOI=10.1016/j.nmd.2006.03.016;
RA Mercuri E., D'Amico A., Tessa A., Berardinelli A., Pane M., Messina S.,
RA van Reeuwijk J., Bertini E., Muntoni F., Santorelli F.M.;
RT "POMT2 mutation in a patient with 'MEB-like' phenotype.";
RL Neuromuscul. Disord. 16:446-448(2006).
RN [11]
RP VARIANT MDDGC2 MET-184.
RX PubMed=17923109; DOI=10.1016/j.bbrc.2007.09.066;
RA Biancheri R., Falace A., Tessa A., Pedemonte M., Scapolan S.,
RA Cassandrini D., Aiello C., Rossi A., Broda P., Zara F., Santorelli F.M.,
RA Minetti C., Bruno C.;
RT "POMT2 gene mutation in limb-girdle muscular dystrophy with inflammatory
RT changes.";
RL Biochem. Biophys. Res. Commun. 363:1033-1037(2007).
RN [12]
RP VARIANTS MDDGA2 ASN-198; PHE-373; PRO-413 AND CYS-666, AND VARIANTS MDDGC2
RP MET-184 AND SER-748.
RX PubMed=17878207; DOI=10.1093/brain/awm212;
RA Godfrey C., Clement E., Mein R., Brockington M., Smith J., Talim B.,
RA Straub V., Robb S., Quinlivan R., Feng L., Jimenez-Mallebrera C.,
RA Mercuri E., Manzur A.Y., Kinali M., Torelli S., Brown S.C., Sewry C.A.,
RA Bushby K., Topaloglu H., North K., Abbs S., Muntoni F.;
RT "Refining genotype phenotype correlations in muscular dystrophies with
RT defective glycosylation of dystroglycan.";
RL Brain 130:2725-2735(2007).
RN [13]
RP VARIANTS MDDGB2 CYS-666 AND ARG-748.
RX PubMed=17634419; DOI=10.1212/01.wnl.0000268489.60809.c4;
RA Yanagisawa A., Bouchet C., Van den Bergh P.Y., Cuisset J.M., Viollet L.,
RA Leturcq F., Romero N.B., Quijano-Roy S., Fardeau M., Seta N., Guicheney P.;
RT "New POMT2 mutations causing congenital muscular dystrophy: identification
RT of a founder mutation.";
RL Neurology 69:1254-1260(2007).
RN [14]
RP VARIANTS MDDGA2 VAL-482; 444-ILE-ASN-445 DELINS LEU-LEU-TRP-GLN AND
RP CYS-666.
RX PubMed=19138766; DOI=10.1016/j.ejmg.2008.12.004;
RA Yanagisawa A., Bouchet C., Quijano-Roy S., Vuillaumier-Barrot S.,
RA Clarke N., Odent S., Rodriguez D., Romero N.B., Osawa M., Endo T.,
RA Taratuto A.L., Seta N., Guicheney P.;
RT "POMT2 intragenic deletions and splicing abnormalities causing congenital
RT muscular dystrophy with mental retardation.";
RL Eur. J. Med. Genet. 52:201-206(2009).
RN [15]
RP VARIANTS MDDGB2 ASP-246; SER-353; CYS-666 AND GLU-726.
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).
RN [16]
RP VARIANT MDDGA2 ARG-478.
RX PubMed=22958903; DOI=10.1016/j.ajhg.2012.07.009;
RA Manzini M.C., Tambunan D.E., Hill R.S., Yu T.W., Maynard T.M.,
RA Heinzen E.L., Shianna K.V., Stevens C.R., Partlow J.N., Barry B.J.,
RA Rodriguez J., Gupta V.A., Al-Qudah A.K., Eyaid W.M., Friedman J.M.,
RA Salih M.A., Clark R., Moroni I., Mora M., Beggs A.H., Gabriel S.B.,
RA Walsh C.A.;
RT "Exome sequencing and functional validation in zebrafish identify GTDC2
RT mutations as a cause of Walker-Warburg syndrome.";
RL Am. J. Hum. Genet. 91:541-547(2012).
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:14699049, PubMed:28512129). Essentially
CC dedicated to O-mannosylation of alpha-DAG1 and few other proteins but
CC not of cadherins and protocaherins (PubMed:28512129).
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 POMT1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12460945, ECO:0000269|PubMed:14699049}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12460945,
CC ECO:0000269|PubMed:14699049}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKY4-2; Sequence=VSP_041457;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis; detected at low levels
CC in most tissues.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12460945}.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC and eye anomalies A2 (MDDGA2) [MIM:613150]: 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:15894594, ECO:0000269|PubMed:16701995,
CC ECO:0000269|PubMed:17878207, ECO:0000269|PubMed:19138766,
CC ECO:0000269|PubMed:22958903}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with impaired
CC intellectual development B2 (MDDGB2) [MIM:613156]: An autosomal
CC recessive disorder characterized by congenital muscular dystrophy
CC associated with intellectual disability and mild structural brain
CC abnormalities. {ECO:0000269|PubMed:17634419,
CC ECO:0000269|PubMed:19299310}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C2 (MDDGC2)
CC [MIM:613158]: An autosomal recessive muscular dystrophy with onset
CC after ambulation is achieved. MDDGC2 is characterized by increased
CC serum creatine kinase and mild muscle weakness. Muscle biopsy shows
CC dystrophic changes, inflammatory changes, and severely decreased alpha-
CC dystroglycan. Cognition is normal. {ECO:0000269|PubMed:17878207,
CC ECO:0000269|PubMed:17923109}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62348.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AF105020; AAF14118.1; -; mRNA.
DR EMBL; AY090480; AAM12046.1; -; mRNA.
DR EMBL; BX248027; CAD62348.1; ALT_SEQ; mRNA.
DR EMBL; AC007954; AAF62558.1; -; Genomic_DNA.
DR EMBL; AC007375; AAF63184.1; -; Genomic_DNA.
DR EMBL; BC031651; AAH31651.1; -; mRNA.
DR EMBL; AL353956; CAB89256.1; -; mRNA.
DR CCDS; CCDS9857.1; -. [Q9UKY4-1]
DR PIR; T48691; T48691.
DR RefSeq; NP_037514.2; NM_013382.5. [Q9UKY4-1]
DR AlphaFoldDB; Q9UKY4; -.
DR SMR; Q9UKY4; -.
DR BioGRID; 118991; 53.
DR IntAct; Q9UKY4; 16.
DR STRING; 9606.ENSP00000261534; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyConnect; 1665; 2 N-Linked glycans (2 sites).
DR GlyGen; Q9UKY4; 5 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q9UKY4; -.
DR PhosphoSitePlus; Q9UKY4; -.
DR BioMuta; POMT2; -.
DR DMDM; 32171723; -.
DR EPD; Q9UKY4; -.
DR jPOST; Q9UKY4; -.
DR MassIVE; Q9UKY4; -.
DR MaxQB; Q9UKY4; -.
DR PaxDb; Q9UKY4; -.
DR PeptideAtlas; Q9UKY4; -.
DR PRIDE; Q9UKY4; -.
DR ProteomicsDB; 84912; -. [Q9UKY4-1]
DR ProteomicsDB; 84913; -. [Q9UKY4-2]
DR Antibodypedia; 67; 132 antibodies from 22 providers.
DR DNASU; 29954; -.
DR Ensembl; ENST00000261534.9; ENSP00000261534.4; ENSG00000009830.13. [Q9UKY4-1]
DR Ensembl; ENST00000556326.5; ENSP00000450630.1; ENSG00000009830.13. [Q9UKY4-2]
DR GeneID; 29954; -.
DR KEGG; hsa:29954; -.
DR MANE-Select; ENST00000261534.9; ENSP00000261534.4; NM_013382.7; NP_037514.2.
DR UCSC; uc001xti.3; human. [Q9UKY4-1]
DR CTD; 29954; -.
DR DisGeNET; 29954; -.
DR GeneCards; POMT2; -.
DR HGNC; HGNC:19743; POMT2.
DR HPA; ENSG00000009830; Tissue enhanced (testis).
DR MalaCards; POMT2; -.
DR MIM; 607439; gene.
DR MIM; 613150; phenotype.
DR MIM; 613156; phenotype.
DR MIM; 613158; phenotype.
DR neXtProt; NX_Q9UKY4; -.
DR OpenTargets; ENSG00000009830; -.
DR Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement.
DR Orphanet; 370968; Congenital muscular dystrophy with intellectual disability.
DR Orphanet; 588; Muscle-eye-brain disease.
DR Orphanet; 206559; POMT2-related limb-girdle muscular dystrophy R14.
DR Orphanet; 899; Walker-Warburg syndrome.
DR PharmGKB; PA134980627; -.
DR VEuPathDB; HostDB:ENSG00000009830; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000156829; -.
DR HOGENOM; CLU_008438_5_1_1; -.
DR InParanoid; Q9UKY4; -.
DR OMA; DANDVWR; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q9UKY4; -.
DR TreeFam; TF300552; -.
DR BioCyc; MetaCyc:HS00268-MON; -.
DR BRENDA; 2.4.1.109; 2681.
DR PathwayCommons; Q9UKY4; -.
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; Q9UKY4; -.
DR SIGNOR; Q9UKY4; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 29954; 11 hits in 1074 CRISPR screens.
DR ChiTaRS; POMT2; human.
DR GeneWiki; POMT2; -.
DR GenomeRNAi; 29954; -.
DR Pharos; Q9UKY4; Tbio.
DR PRO; PR:Q9UKY4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UKY4; protein.
DR Bgee; ENSG00000009830; Expressed in right testis and 143 other tissues.
DR ExpressionAtlas; Q9UKY4; baseline and differential.
DR Genevisible; Q9UKY4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IEA:Ensembl.
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; Dystroglycanopathy;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Limb-girdle muscular dystrophy; Lissencephaly; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..750
FT /note="Protein O-mannosyl-transferase 2"
FT /id="PRO_0000121488"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 334..390
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 403..459
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 464..521
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 83..750
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041457"
FT VARIANT 54
FT /note="A -> E (in dbSNP:rs8177536)"
FT /id="VAR_022083"
FT VARIANT 184
FT /note="T -> M (in MDDGC2; dbSNP:rs267606971)"
FT /evidence="ECO:0000269|PubMed:17878207,
FT ECO:0000269|PubMed:17923109"
FT /id="VAR_065037"
FT VARIANT 198
FT /note="I -> N (in MDDGA2; dbSNP:rs267606972)"
FT /evidence="ECO:0000269|PubMed:17878207"
FT /id="VAR_065038"
FT VARIANT 246
FT /note="G -> D (in MDDGB2; dbSNP:rs267606966)"
FT /evidence="ECO:0000269|PubMed:19299310"
FT /id="VAR_065039"
FT VARIANT 353
FT /note="G -> S (in MDDGA2; dbSNP:rs267606970)"
FT /evidence="ECO:0000269|PubMed:16701995,
FT ECO:0000269|PubMed:19299310"
FT /id="VAR_065040"
FT VARIANT 373
FT /note="V -> F (in MDDGA2; dbSNP:rs267606965)"
FT /evidence="ECO:0000269|PubMed:17878207"
FT /id="VAR_065041"
FT VARIANT 413
FT /note="R -> P (in MDDGA2; dbSNP:rs190285831)"
FT /evidence="ECO:0000269|PubMed:17878207"
FT /id="VAR_065042"
FT VARIANT 444..445
FT /note="IN -> LLWQ (in MDDGA2)"
FT /evidence="ECO:0000269|PubMed:19138766"
FT /id="VAR_065043"
FT VARIANT 478
FT /note="H -> R (in MDDGA2; dbSNP:rs765346043)"
FT /evidence="ECO:0000269|PubMed:22958903"
FT /id="VAR_068968"
FT VARIANT 482
FT /note="G -> V (in MDDGA2; dbSNP:rs267606968)"
FT /evidence="ECO:0000269|PubMed:19138766"
FT /id="VAR_065044"
FT VARIANT 666
FT /note="Y -> C (in MDDGB2 and MDDGA2; dbSNP:rs200198778)"
FT /evidence="ECO:0000269|PubMed:17634419,
FT ECO:0000269|PubMed:17878207, ECO:0000269|PubMed:19138766,
FT ECO:0000269|PubMed:19299310"
FT /id="VAR_065045"
FT VARIANT 717
FT /note="F -> S (in MDDGB2)"
FT /id="VAR_065046"
FT VARIANT 726
FT /note="G -> E (in MDDGA2 and MDDGB2; dbSNP:rs267606969)"
FT /evidence="ECO:0000269|PubMed:16701995,
FT ECO:0000269|PubMed:19299310"
FT /id="VAR_065047"
FT VARIANT 748
FT /note="W -> R (in MDDGB2; dbSNP:rs267606964)"
FT /evidence="ECO:0000269|PubMed:17634419"
FT /id="VAR_065048"
FT VARIANT 748
FT /note="W -> S (in MDDGC2; dbSNP:rs267606967)"
FT /evidence="ECO:0000269|PubMed:17878207"
FT /id="VAR_065049"
FT CONFLICT 53
FT /note="E -> Q (in Ref. 1; AAF14118/AAM12046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 750 AA; 84214 MW; 79732D6C4978CFB9 CRC64;
MPPATGGGLA ESELRPRRGR CGPQAARAAG RDVAAEAVAR SPKRPAWGSR RFEAVGWWAL
LALVTLLSFA TRFHRLDEPP HICWDETHFG KMGSYYINRT FFFDVHPPLG KMLIGLAGYL
SGYDGTFLFQ KPGDKYEHHS YMGMRGFCAF LGSWLVPFAY LTVLDLSKSL SAALLTAALL
TFDTGCLTLS QYILLDPILM FFIMAAMLSM VKYNSCADRP FSAPWWFWLS LTGVSLAGAL
GVKFVGLFII LQVGLNTIAD LWYLFGDLSL SLVTVGKHLT ARVLCLIVLP LALYTATFAV
HFMVLSKSGP GDGFFSSAFQ ARLSGNNLHN ASIPEHLAYG SVITVKNLRM AIGYLHSHRH
LYPEGIGARQ QQVTTYLHKD YNNLWIIKKH NTNSDPLDPS FPVEFVRHGD IIRLEHKETS
RNLHSHYHEA PMTRKHYQVT GYGINGTGDS NDFWRIEVVN RKFGNRIKVL RSRIRFIHLV
TGCVLGSSGK VLPKWGWEQL EVTCTPYLKE TLNSIWNVED HINPKLPNIS LDVLQPSFPE
ILLESHMVMI RGNSGLKPKD NEFTSKPWHW PINYQGLRFS GVNDTDFRVY LLGNPVVWWL
NLLSIALYLL SGSIIAVAMQ RGARLPAEVA GLSQVLLRGG GQVLLGWTLH YFPFFLMGRV
LYFHHYFPAM LFSSMLTGIL WDTLLRLCAW GLASWPLARG IHVAGILSLL LGTAYSFYLF
HPLAYGMVGP LAQDPQSPMA GLRWLDSWDF
