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 27-MAR-2024, entry version 198. 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}; 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; 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; 56. DR ComplexPortal; CPX-2659; POMT1-POMT2 O-mannosyltransferase complex. DR IntAct; Q9UKY4; 17. DR STRING; 9606.ENSP00000261534; -. DR CAZy; GT39; Glycosyltransferase Family 39. DR GlyConnect; 1665; 2 N-Linked glycans (2 sites). DR GlyCosmos; Q9UKY4; 5 sites, 2 glycans. 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; 9606-ENSP00000261534; -. DR PeptideAtlas; Q9UKY4; -. DR ProteomicsDB; 84912; -. [Q9UKY4-1] DR ProteomicsDB; 84913; -. [Q9UKY4-2] DR Pumba; Q9UKY4; -. DR Antibodypedia; 67; 146 antibodies from 23 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 AGR; HGNC:19743; -. 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; MCGWDDN; -. DR OrthoDB; 5489060at2759; -. DR PhylomeDB; Q9UKY4; -. DR TreeFam; TF300552; -. DR BioCyc; MetaCyc:HS00268-MONOMER; -. 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; 13 hits in 1158 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 145 other cell types or tissues. DR ExpressionAtlas; Q9UKY4; baseline and differential. 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: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:0071711; P:basement membrane organization; IEA:Ensembl. DR GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl. 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 GO; GO:0150103; P:reactive gliosis; IEA:Ensembl. DR Gene3D; 2.80.10.50; -; 1. 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; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1. DR PANTHER; PTHR10050:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 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; MIR domain; 1. DR PROSITE; PS50919; MIR; 3. DR Genevisible; Q9UKY4; HS. 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 //