LOCUS       NM_003863                912 bp    mRNA    linear   PRI 12-OCT-2024
DEFINITION  Homo sapiens dolichyl-phosphate mannosyltransferase subunit 2,
            regulatory (DPM2), transcript variant 1, mRNA.
ACCESSION   NM_003863
VERSION     NM_003863.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 912)
  AUTHORS   Radenkovic,S., Fitzpatrick-Schmidt,T., Byeon,S.K., Madugundu,A.K.,
            Saraswat,M., Lichty,A., Wong,S.Y.W., McGee,S., Kubiak,K.,
            Ligezka,A., Ranatunga,W., Zhang,Y., Wood,T., Friez,M.J.,
            Clarkson,K., Pandey,A., Jones,J.R. and Morava,E.
  TITLE     Expanding the clinical and metabolic phenotype of DPM2 deficient
            congenital disorders of glycosylation
  JOURNAL   Mol Genet Metab 132 (1), 27-37 (2021)
   PUBMED   33129689
  REMARK    GeneRIF: Expanding the clinical and metabolic phenotype of DPM2
            deficient congenital disorders of glycosylation.
REFERENCE   2  (bases 1 to 912)
  AUTHORS   Pilsyk,S., Perlinska-Lenart,U., Janik,A., Gryz,E.,
            Ajchler-Adamska,M. and Kruszewska,J.S.
  TITLE     Yil102c-A is a Functional Homologue of the DPMII Subunit of
            Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae
  JOURNAL   Int J Mol Sci 21 (23), 8938 (2020)
   PUBMED   33255655
  REMARK    GeneRIF: Yil102c-A is a Functional Homologue of the DPMII Subunit
            of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae.
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 912)
  AUTHORS   Nongpiur,M.E., Cheng,C.Y., Duvesh,R., Vijayan,S., Baskaran,M.,
            Khor,C.C., Allen,J., Kavitha,S., Venkatesh,R., Goh,D., Husain,R.,
            Boey,P.Y., Quek,D., Ho,C.L., Wong,T.T., Perera,S., Wong,T.Y.,
            Krishnadas,S.R., Sundaresan,P., Aung,T. and Vithana,E.N.
  TITLE     Evaluation of Primary Angle-Closure Glaucoma Susceptibility Loci in
            Patients with Early Stages of Angle-Closure Disease
  JOURNAL   Ophthalmology 125 (5), 664-670 (2018)
   PUBMED   29310965
  REMARK    GeneRIF: In this study, 2 of 8 (primary angle-closure glaucoma)
            PACG-associated loci were associated significantly with PACS
            status, the earliest stage in the angle-closure glaucoma disease
            course. The association of these PACG loci with PACS status
            suggests that these loci may confer susceptibility to a narrow
            angle configuration.
REFERENCE   4  (bases 1 to 912)
  AUTHORS   Barone,R., Aiello,C., Race,V., Morava,E., Foulquier,F.,
            Riemersma,M., Passarelli,C., Concolino,D., Carella,M.,
            Santorelli,F., Vleugels,W., Mercuri,E., Garozzo,D., Sturiale,L.,
            Messina,S., Jaeken,J., Fiumara,A., Wevers,R.A., Bertini,E.,
            Matthijs,G. and Lefeber,D.J.
  TITLE     DPM2-CDG: a muscular dystrophy-dystroglycanopathy syndrome with
            severe epilepsy
  JOURNAL   Ann Neurol 72 (4), 550-558 (2012)
   PUBMED   23109149
  REMARK    GeneRIF: We describe a new congenital disorders of glycosylation,
            due to a deficiency of DPM2
REFERENCE   5  (bases 1 to 912)
  AUTHORS   Ashida,H., Maeda,Y. and Kinoshita,T.
  TITLE     DPM1, the catalytic subunit of dolichol-phosphate mannose synthase,
            is tethered to and stabilized on the endoplasmic reticulum membrane
            by DPM3
  JOURNAL   J Biol Chem 281 (2), 896-904 (2006)
   PUBMED   16280320
REFERENCE   6  (bases 1 to 912)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   7  (bases 1 to 912)
  AUTHORS   Watanabe,R., Murakami,Y., Marmor,M.D., Inoue,N., Maeda,Y., Hino,J.,
            Kangawa,K., Julius,M. and Kinoshita,T.
  TITLE     Initial enzyme for glycosylphosphatidylinositol biosynthesis
            requires PIG-P and is regulated by DPM2
  JOURNAL   EMBO J 19 (16), 4402-4411 (2000)
   PUBMED   10944123
REFERENCE   8  (bases 1 to 912)
  AUTHORS   Maeda,Y., Tanaka,S., Hino,J., Kangawa,K. and Kinoshita,T.
  TITLE     Human dolichol-phosphate-mannose synthase consists of three
            subunits, DPM1, DPM2 and DPM3
  JOURNAL   EMBO J 19 (11), 2475-2482 (2000)
   PUBMED   10835346
REFERENCE   9  (bases 1 to 912)
  AUTHORS   Maeda,Y., Tomita,S., Watanabe,R., Ohishi,K. and Kinoshita,T.
  TITLE     DPM2 regulates biosynthesis of dolichol phosphate-mannose in
            mammalian cells: correct subcellular localization and stabilization
            of DPM1, and binding of dolichol phosphate
  JOURNAL   EMBO J 17 (17), 4920-4929 (1998)
   PUBMED   9724629
REFERENCE   10 (bases 1 to 912)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157935.28.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 15, 2019 this sequence version replaced NM_003863.3.
            
            Summary: Dolichol-phosphate mannose (Dol-P-Man) serves as a donor
            of mannosyl residues on the lumenal side of the endoplasmic
            reticulum (ER). Lack of Dol-P-Man results in defective surface
            expression of GPI-anchored proteins. Dol-P-Man is synthesized from
            GDP-mannose and dolichol-phosphate on the cytosolic side of the ER
            by the enzyme dolichyl-phosphate mannosyltransferase. The protein
            encoded by this gene is a hydrophobic protein that contains 2
            predicted transmembrane domains and a putative ER localization
            signal near the C terminus. This protein associates with DPM1 in
            vivo and is required for the ER localization and stable expression
            of DPM1 and also enhances the binding of dolichol-phosphate to
            DPM1. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015233.1, BU595073.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314392.13/ ENSP00000322181.8
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-37                AL157935.28        111151-111187       c
            38-127              AL157935.28        110767-110856       c
            128-230             AL157935.28        109886-109988       c
            231-912             AL157935.28        108432-109113       c
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     gene            1..912
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /note="dolichyl-phosphate mannosyltransferase subunit 2,
                     regulatory"
                     /db_xref="GeneID:8818"
                     /db_xref="HGNC:HGNC:3006"
                     /db_xref="MIM:603564"
     exon            1..37
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /inference="alignment:Splign:2.1.0"
     CDS             35..289
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /EC_number="2.4.1.83"
                     /note="isoform 1 is encoded by transcript variant 1; DPM
                     synthase subunit 2; dolichyl-phosphate mannosyltransferase
                     polypeptide 2, regulatory subunit; dolichol-phosphate
                     mannose synthase subunit 2; dolichol phosphate-mannose
                     biosynthesis regulatory protein; DPM synthase complex
                     subunit"
                     /codon_start=1
                     /product="dolichol phosphate-mannose biosynthesis
                     regulatory protein isoform 1"
                     /protein_id="NP_003854.1"
                     /db_xref="CCDS:CCDS6886.1"
                     /db_xref="GeneID:8818"
                     /db_xref="HGNC:HGNC:3006"
                     /db_xref="MIM:603564"
                     /translation="MATGTDQVVGLGLVAVSLIIFTYYTAWVILLPFIDSQHVIHKYF
                     LPRAYAVAIPLAAGLLLLLFVGLFISYVMLKTKRVTKKAQ"
     exon            38..127
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /inference="alignment:Splign:2.1.0"
     exon            128..230
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /inference="alignment:Splign:2.1.0"
     exon            231..912
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /inference="alignment:Splign:2.1.0"
     regulatory      892..897
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /note="hexamer: AATAAA"
     polyA_site      912
                     /gene="DPM2"
                     /gene_synonym="CDG1U"
                     /note="major polyA site"
ORIGIN      
        1 ggcttgcggc tcgggtggct gagcgcgcgg ggaaatggcc acggggacag accaggtggt
       61 gggactcggc ctcgtcgccg ttagcctgat catcttcacc tactacaccg cctgggtgat
      121 tctcttgcca ttcatcgaca gtcagcatgt catccacaag tatttcctgc cccgagccta
      181 tgctgtcgcc atcccactgg ctgcaggcct cctgctgctc ctgtttgtgg gactgttcat
      241 ctcctatgtg atgctgaaga ccaagagagt gaccaagaag gctcagtgaa ggtcccgcag
      301 ggatgaggct gccagcccct tctctgcttc ccctccagca cagggaccaa gtgggggagc
      361 ctgcagaacc tgtccaggca cagtggctcc tcaagcctgc ctgtcctgca gagtccccat
      421 ggcatggagc ttacacctga ctgactggag ccccctcccc gactcccact tccagaagct
      481 aggagggagg gatacctgga agactccggt cacctccttc ttgctcaggg cctaaaagat
      541 gctggtcctc ccaacctcac tctcagactc cctgccacct tttcccctgg gttctgccgt
      601 cttgcctcac ttcccctcct gtcacatgct gacgttggac ttagcaggtt ctaaggccac
      661 atgtgtgacc tctctgactt ctcttcctcc accaaggcag ctttccttac cctgacacag
      721 ccccagaccc cacaaagcct tctggacctg gaaagcctgg ggaaggactg acagacccca
      781 ggaccagccc tggggctcag ggcagccacc ccgggccgct gaccgactga cctctcctca
      841 cggaggccca gccccaaagc cccagggctg gcccgtttgg gacagctgac caataaacac
      901 tgatggtgtg tt
//
