MPU1_MOUSE
ID MPU1_MOUSE Reviewed; 247 AA.
AC Q9R0Q9; O70203; Q9R0P7;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Mannose-P-dolichol utilization defect 1 protein;
DE AltName: Full=Suppressor of Lec15 and Lec35 glycosylation mutation homolog;
DE Short=SL15;
GN Name=Mpdu1; Synonyms=Supl15h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=10524236; DOI=10.1016/s0378-1119(99)00301-7;
RA Miyashita A., Shimizu N., Endo N., Hanyuu T., Ishii N., Ito K., Itoh Y.,
RA Shirai M., Nakajima T., Odani S., Kuwano R.;
RT "Five different genes, Eif4a1, Cd68, Supl15h, Sox15 and Fxr2h, are
RT clustered in a 40 kb region of mouse chromosome 11.";
RL Gene 237:53-60(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RA Miyashita A., Shimizu N., Odani S., Nakajima T., Kuwano R.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250}.
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; AB024713; BAA78781.1; -; mRNA.
DR EMBL; AB025354; BAA78782.1; -; Genomic_DNA.
DR EMBL; AB014471; BAA28603.1; -; Genomic_DNA.
DR CCDS; CCDS24903.1; -.
DR AlphaFoldDB; Q9R0Q9; -.
DR STRING; 10090.ENSMUSP00000018905; -.
DR PhosphoSitePlus; Q9R0Q9; -.
DR EPD; Q9R0Q9; -.
DR jPOST; Q9R0Q9; -.
DR MaxQB; Q9R0Q9; -.
DR PaxDb; Q9R0Q9; -.
DR PRIDE; Q9R0Q9; -.
DR ProteomicsDB; 290308; -.
DR UCSC; uc007jqw.2; mouse.
DR MGI; MGI:1346040; Mpdu1.
DR eggNOG; KOG3211; Eukaryota.
DR InParanoid; Q9R0Q9; -.
DR PhylomeDB; Q9R0Q9; -.
DR Reactome; R-MMU-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR ChiTaRS; Mpdu1; mouse.
DR PRO; PR:Q9R0Q9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R0Q9; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; 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_0000221035"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
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 148
FT /note="L -> V (in Ref. 2; BAA28603)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="L -> LL (in Ref. 2; BAA28603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26498 MW; D639EAFFFE1CA11C CRC64;
MAGEADGRFK GLLVPILLPE KCYDQLFVQW DLLHVPCLKI LLSKGLGLGI VAGSLLVKLP
QVFKLLGAKS AEGLSLQSVM LELVALTGTV VYSITNNFPF SSWGEALFLT LQTVAICFLV
MHYRGETVKG VAFLACYAMV LLALLSPLTP LAVVTLLQAS NVPAVVVGKL LQAATNYRNG
HTGQLSAITV FMLFGGSLAR IFTSVQETGD PLMAGVFVVS SLCNGLIAAQ VLFYWNAKAP
HKQKKEQ
