ID   MPU1_CRIGR              Reviewed;         247 AA.
AC   Q60441; Q9R265;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Mannose-P-dolichol utilization defect 1 protein;
DE   AltName: Full=Suppressor of Lec15 and Lec35 glycosylation mutation;
DE            Short=SL15;
GN   Name=MPDU1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8663248; DOI=10.1074/jbc.271.24.13935;
RA   Ware F.E., Lehrman M.A.;
RT   "Expression cloning of a novel suppressor of the Lec15 and Lec35
RT   glycosylation mutations of Chinese hamster ovary cells.";
RL   J. Biol. Chem. 271:13935-13938(1996).
RN   [2]
RP   ERRATUM OF PUBMED:8663248.
RX   PubMed=12755100; DOI=10.1016/s0021-9258(19)57957-1;
RA   Ware F.E., Lehrman M.A.;
RL   J. Biol. Chem. 273:13366-13366(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pu L., Scocca J.R., Walker B.K., Wu J.S., Krag S.S.;
RT   "Mutation in B4-2-1 CHO cells defective in MPD synthase activity.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=11179430; DOI=10.1091/mbc.12.2.487;
RA   Anand M., Rush J.S., Ray S., Doucey M.A., Weik J., Ware F.E.,
RA   Hofsteenge J., Waechter C.J., Lehrman M.A.;
RT   "Requirement of the Lec35 gene for all known classes of monosaccharide-P-
RT   dolichol-dependent glycosyltransferase reactions in mammals.";
RL   Mol. Biol. Cell 12:487-501(2001).
CC   -!- FUNCTION: Required for normal utilization of mannose-dolichol phosphate
CC       (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides
CC       and GPI anchors. {ECO:0000269|PubMed:11179430}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MPDU1 (TC 2.A.43.3) family. {ECO:0000305}.
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DR   EMBL; U55387; AAC52600.2; -; mRNA.
DR   EMBL; AF121896; AAD30976.1; -; mRNA.
DR   RefSeq; NP_001230966.1; NM_001244037.1.
DR   AlphaFoldDB; Q60441; -.
DR   STRING; 10029.NP_001230966.1; -.
DR   TCDB; 2.A.43.3.1; the lysosomal cystine transporter (lct) family.
DR   GeneID; 100689049; -.
DR   KEGG; cge:100689049; -.
DR   CTD; 9526; -.
DR   eggNOG; KOG3211; Eukaryota.
DR   OrthoDB; 1059579at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR016817; MannP-dilichol_defect-1.
DR   InterPro; IPR006603; PQ-loop_rpt.
DR   PANTHER; PTHR12226; PTHR12226; 1.
DR   Pfam; PF04193; PQ-loop; 2.
DR   PIRSF; PIRSF023381; MannP-dilichol_defect-1p; 1.
DR   SMART; SM00679; CTNS; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75352"
FT   CHAIN           2..247
FT                   /note="Mannose-P-dolichol utilization defect 1 protein"
FT                   /id="PRO_0000221033"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          39..105
FT                   /note="PQ-loop 1"
FT   DOMAIN          159..216
FT                   /note="PQ-loop 2"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75352"
FT   CONFLICT        118
FT                   /note="L -> F (in Ref. 3; AAD30976)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   247 AA;  26543 MW;  406476EE66398DB8 CRC64;
     MAGEADGPFK RVLVPVLLPE KCYDQLFVHW DFLHVPCLKI LLSKGLGLGI VAGSLLVKLP
     QIFKILGAKS AEGLSLQSVM LELVALTGTV IYSITNNFPF SSWGEALFLT LQTITICLLV
     LHYRGDTVKG VALLACYATL LLALLSPLTP LAVVTMLQAS NVPAVVVGKL LQAATNYHNG
     HTGQLSAITV FMLFGGSLAR IFTSVQETGD PLMAGVFVVS SLCNGLIAAQ VLFYWNAKPP
     HKHKKEQ