LOCUS       NM_003859               1054 bp    mRNA    linear   PRI 12-OCT-2024
DEFINITION  Homo sapiens dolichyl-phosphate mannosyltransferase subunit 1,
            catalytic (DPM1), transcript variant 3, mRNA.
ACCESSION   NM_003859
VERSION     NM_003859.3
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 1054)
  AUTHORS   Rathod,M., Franz,H., Beyersdorfer,V., Wanuske,M.T.,
            Leal-Fischer,K., Hanns,P., Studle,C., Zimmermann,A., Buczak,K.,
            Schinner,C. and Spindler,V.
  TITLE     DPM1 modulates desmosomal adhesion and epidermal differentiation
            through SERPINB5
  JOURNAL   J Cell Biol 223 (4) (2024)
   PUBMED   38477878
  REMARK    GeneRIF: DPM1 modulates desmosomal adhesion and epidermal
            differentiation through SERPINB5.
REFERENCE   2  (bases 1 to 1054)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (bases 1 to 1054)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (bases 1 to 1054)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   5  (bases 1 to 1054)
  AUTHORS   Imbach,T., Schenk,B., Schollen,E., Burda,P., Stutz,A.,
            Grunewald,S., Bailie,N.M., King,M.D., Jaeken,J., Matthijs,G.,
            Berger,E.G., Aebi,M. and Hennet,T.
  TITLE     Deficiency of dolichol-phosphate-mannose synthase-1 causes
            congenital disorder of glycosylation type Ie
  JOURNAL   J Clin Invest 105 (2), 233-239 (2000)
   PUBMED   10642602
REFERENCE   6  (bases 1 to 1054)
  AUTHORS   Kim,S., Westphal,V., Srikrishna,G., Mehta,D.P., Peterson,S.,
            Filiano,J., Karnes,P.S., Patterson,M.C. and Freeze,H.H.
  TITLE     Dolichol phosphate mannose synthase (DPM1) mutations define
            congenital disorder of glycosylation Ie (CDG-Ie)
  JOURNAL   J Clin Invest 105 (2), 191-198 (2000)
   PUBMED   10642597
REFERENCE   7  (bases 1 to 1054)
  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   8  (bases 1 to 1054)
  AUTHORS   Tomita,S., Inoue,N., Maeda,Y., Ohishi,K., Takeda,J. and
            Kinoshita,T.
  TITLE     A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for
            synthesis of dolichol-phosphate-mannose in mammalian cells
  JOURNAL   J Biol Chem 273 (15), 9249-9254 (1998)
   PUBMED   9535917
REFERENCE   9  (bases 1 to 1054)
  AUTHORS   Colussi,P.A., Taron,C.H., Mack,J.C. and Orlean,P.
  TITLE     Human and Saccharomyces cerevisiae dolichol phosphate mannose
            synthases represent two classes of the enzyme, but both function in
            Schizosaccharomyces pombe
  JOURNAL   Proc Natl Acad Sci U S A 94 (15), 7873-7878 (1997)
   PUBMED   9223280
REFERENCE   10 (bases 1 to 1054)
  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 BC016322.1 and D86198.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 25, 2020 this sequence version replaced NM_003859.2.
            
            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. Human DPM1
            lacks a carboxy-terminal transmembrane domain and signal sequence
            and is regulated by DPM2. Mutations in this gene are associated
            with congenital disorder of glycosylation type Ie. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (3) is shorter than isoform 1.
            
            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 :: BC016322.1, AK289569.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371588.10/ ENSP00000360644.5
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1050              BC016322.1         4-1053
            1051-1054           D86198.1           1042-1045
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     gene            1..1054
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /note="dolichyl-phosphate mannosyltransferase subunit 1,
                     catalytic"
                     /db_xref="GeneID:8813"
                     /db_xref="HGNC:HGNC:3005"
                     /db_xref="MIM:603503"
     exon            1..170
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     CDS             10..792
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /EC_number="2.4.1.83"
                     /note="isoform 3 is encoded by transcript variant 3;
                     dolichol monophosphate mannose synthase; DPM synthase
                     complex, catalytic subunit; DPM synthase subunit 1; MPD
                     synthase subunit 1; mannose-P-dolichol synthase subunit 1;
                     dolichol-phosphate mannose synthase subunit 1;
                     dolichyl-phosphate beta-D-mannosyltransferase subunit 1;
                     dolichyl-phosphate mannosyltransferase polypeptide 1
                     catalytic subunit"
                     /codon_start=1
                     /product="dolichol-phosphate mannosyltransferase subunit 1
                     isoform 3"
                     /protein_id="NP_003850.1"
                     /db_xref="CCDS:CCDS13434.1"
                     /db_xref="GeneID:8813"
                     /db_xref="HGNC:HGNC:3005"
                     /db_xref="MIM:603503"
                     /translation="MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIV
                     WLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAY
                     IHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLK
                     RKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRAR
                     QLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT"
     exon            171..270
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            271..304
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            305..381
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            382..407
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            408..503
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            504..572
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            573..687
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     exon            688..1054
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1027..1032
                     /regulatory_class="polyA_signal_sequence"
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /note="hexamer: AATAAA"
     polyA_site      1054
                     /gene="DPM1"
                     /gene_synonym="CDGIE; MPDS"
                     /note="major polyA site"
ORIGIN      
        1 agttccgcca tggcctcctt ggaagtcagt cgtagtcctc gcaggtctcg gcgggagctg
       61 gaagtgcgca gtccacgaca gaacaaatat tcggtgcttt tacctaccta caacgagcgc
      121 gagaacctgc cgctcatcgt gtggctgctg gtgaaaagct tctccgagag tggaatcaac
      181 tatgaaatta taatcataga tgatggaagc ccagatggaa caagggatgt tgctgaacag
      241 ttggagaaga tctatgggtc agacagaatt cttctaagac cacgagagaa aaagttggga
      301 ctaggaactg catatattca tggaatgaaa catgccacag gaaactacat cattattatg
      361 gatgctgatc tctcacacca tccaaaattt attcctgaat ttattaggaa gcaaaaggag
      421 ggtaattttg atattgtctc tggaactcgc tacaaaggaa atggaggtgt atatggctgg
      481 gatttgaaaa gaaaaataat cagccgtggg gccaattttt taactcagat cttgctgaga
      541 ccaggagcat ctgatttaac aggaagtttc agattatacc gaaaagaagt tctagagaaa
      601 ttaatagaaa aatgtgtttc taaaggctac gtcttccaga tggagatgat tgttcgggca
      661 agacagttga attatactat tggcgaggtt ccaatatcat ttgtggatcg tgtttatggt
      721 gaatccaagt tgggaggaaa tgaaatagta tctttcttga aaggattatt gactcttttt
      781 gctactacat aaaagaaaga tactcattta tagttacgtt catttcaggt taaacatgaa
      841 agaagcctgg ttactgattt gtataaaatg tactcttaaa gtataaaata taaggtaagg
      901 taaatttcat gcatcttttt atgaagacca cctattttat atttcaaatt aaataatttt
      961 aaagttgctg gcctaatgag caatgttctc aattttcgtt ttcattttgc tgtattgaga
     1021 cctataaata aatgtatatt tttttttgca taaa
//
