ID   DPM1_DICDI              Reviewed;         254 AA.
AC   Q54LP3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Dolichol-phosphate mannosyltransferase subunit 1;
DE            EC=2.4.1.83;
DE   AltName: Full=Dolichol-phosphate mannose synthase subunit 1;
DE            Short=DPM synthase subunit 1;
DE   AltName: Full=Dolichyl-phosphate beta-D-mannosyltransferase subunit 1;
DE   AltName: Full=Mannose-P-dolichol synthase subunit 1;
DE            Short=MPD synthase subunit 1;
GN   Name=dpm1; Synonyms=dgtB; ORFNames=DDB_G0286519;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Transfers mannose from GDP-mannose to dolichol monophosphate
CC       to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl
CC       donor in pathways leading to N-glycosylation, glycosyl
CC       phosphatidylinositol membrane anchoring, and O-mannosylation of
CC       proteins; catalytic subunit of the dolichol-phosphate mannose (DPM)
CC       synthase complex. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-
CC         D-mannosyl phosphate + GDP; Xref=Rhea:RHEA:21184, Rhea:RHEA-
CC         COMP:9517, Rhea:RHEA-COMP:9527, ChEBI:CHEBI:57527, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:58211; EC=2.4.1.83;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Component of the dolichol-phosphate mannose (DPM) synthase
CC       complex composed of dpm1, dpm2 and dpm3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AAFI02000087; EAL64186.1; -; Genomic_DNA.
DR   RefSeq; XP_637689.1; XM_632597.1.
DR   AlphaFoldDB; Q54LP3; -.
DR   SMR; Q54LP3; -.
DR   STRING; 44689.DDB0231708; -.
DR   PaxDb; Q54LP3; -.
DR   EnsemblProtists; EAL64186; EAL64186; DDB_G0286519.
DR   GeneID; 8625655; -.
DR   KEGG; ddi:DDB_G0286519; -.
DR   dictyBase; DDB_G0286519; dgtB.
DR   eggNOG; KOG2978; Eukaryota.
DR   HOGENOM; CLU_033536_13_3_1; -.
DR   InParanoid; Q54LP3; -.
DR   OMA; TAYIHGF; -.
DR   PhylomeDB; Q54LP3; -.
DR   Reactome; R-DDI-162699; Synthesis of dolichyl-phosphate mannose.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q54LP3; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:dictyBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0035268; P:protein mannosylation; ISS:UniProtKB.
DR   GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR   CDD; cd06442; DPM1_like; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR039528; DPM1-like.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43398; PTHR43398; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..254
FT                   /note="Dolichol-phosphate mannosyltransferase subunit 1"
FT                   /id="PRO_0000327894"
SQ   SEQUENCE   254 AA;  28698 MW;  3A547C62A8152C0E CRC64;
     MSTKNRSDKS SSSSITKDKY TIILPTYKER ENLPIIIWLI STELEKCFID YEVVIVEDNS
     PDGTLEVAQQ LQKIYGEEKI KILSRPGKMG LGSAYMDGIK KSTGNWVILM DADLSHHPKF
     IPQFIEKQKK LNCEIVTGTR YQSGGGVFGW NLYRKLTSRV ANYIASVLLT PGVSDLTGSF
     RLYRKDVLEK LITQNKSKGY VFQVEMMVRA NQLGYQVGEV PITFVDRIFG VSNLDSGEIV
     GFLKSVLNLF MNIE