ID AUP1_MOUSE Reviewed; 410 AA. AC P70295; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 10-JUN-2026, entry version 154. DE RecName: Full=Lipid droplet-regulating VLDL assembly factor AUP1 {ECO:0000250|UniProtKB:Q9Y679}; DE AltName: Full=Ancient ubiquitous protein 1 {ECO:0000303|PubMed:8812468}; GN Name=Aup1 {ECO:0000312|MGI:MGI:107789}; 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 [MRNA]. RC STRAIN=C57BL/6J; RX PubMed=8812468; DOI=10.1006/geno.1996.0477; RA Jang W., Weber J.S., Bashir R., Bushby K., Meisler M.H.; RT "Aup1, a novel gene on mouse chromosome 6 and human chromosome 2p13."; RL Genomics 36:366-368(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Pancreas, Spleen, and 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: Plays a role in the translocation of terminally misfolded CC proteins from the endoplasmic reticulum lumen to the cytoplasm and CC their degradation by the proteasome (By similarity). Plays a role in CC lipid droplet formation (By similarity). Induces lipid droplet CC clustering (By similarity). Recruits ubiquitin-conjugating enzyme CC UBE2G2 to lipid droplets which facilitates its interaction with CC ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading to sterol-induced CC ubiquitination of HMGCR and its subsequent proteasomal degradation (By CC similarity). Also required for the degradation of INSIG1, SREBF1 and CC SREBF2 (By similarity). Plays a role in regulating assembly and CC secretion of very low density lipoprotein particles and stability of CC apolipoprotein APOB (By similarity). {ECO:0000250|UniProtKB:Q9Y679}. CC -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8, CC UBE2J1/UBC6E and AUP1 (By similarity). Interacts with the cytoplasmic CC tail of ITGA2B, ITGA1, ITGA2, ITGA5, ITGAV and ITGAM (By similarity). CC Interacts (via C-terminus) with UBE2G2; the interaction recruits UBE2G2 CC to lipid droplets (By similarity). Interacts with ubiquitin ligases CC AMFR/gp78 and RNF139/TRC8; this promotes interaction of UBE2G2 with CC AMFR and RNF139 (By similarity). Interacts with apolipoprotein APOB (By CC similarity). {ECO:0000250|UniProtKB:Q9Y679}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9Y679}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9Y679}. Lipid droplet CC {ECO:0000250|UniProtKB:Q9Y679}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: The CUE domain is required for interaction with the ER quality CC control machinery and misfolded substrates, ubiquitination, lipid CC clustering and interaction with AMFR but is not required for CC localization to lipid droplets. {ECO:0000250|UniProtKB:Q9Y679}. CC -!- PTM: Monoubiquitinated and diubiquitinated. CC {ECO:0000250|UniProtKB:Q9Y679}. CC -!- SIMILARITY: Belongs to the AUP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U41736; AAC52839.1; -; mRNA. DR EMBL; BC016485; AAH16485.1; -; mRNA. DR CCDS; CCDS39526.1; -. DR RefSeq; NP_031543.3; NM_007517.5. DR AlphaFoldDB; P70295; -. DR SMR; P70295; -. DR FunCoup; P70295; 2149. DR STRING; 10090.ENSMUSP00000090281; -. DR iPTMnet; P70295; -. DR PhosphoSitePlus; P70295; -. DR SwissPalm; P70295; -. DR jPOST; P70295; -. DR PaxDb; 10090-ENSMUSP00000090281; -. DR ProteomicsDB; 277209; -. DR Pumba; P70295; -. DR Ensembl; ENSMUST00000092618.10; ENSMUSP00000090281.8; ENSMUSG00000068328.11. DR GeneID; 11993; -. DR KEGG; mmu:11993; -. DR UCSC; uc009clz.2; mouse. DR AGR; MGI:107789; -. DR CTD; 550; -. DR MGI; MGI:107789; Aup1. DR eggNOG; KOG2898; Eukaryota. DR GeneTree; ENSGT00390000016110; -. DR InParanoid; P70295; -. DR OrthoDB; 1854593at2759; -. DR PRO; PR:P70295; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P70295; protein. DR ExpressionAtlas; P70295; baseline and differential. DR GO; GO:0005776; C:autophagosome; ISO:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB. DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB. DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB. DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB. DR GO; GO:0034389; P:lipid droplet organization; ISS:UniProtKB. DR GO; GO:0061724; P:lipophagy; ISO:GO_Central. DR GO; GO:1990044; P:protein localization to lipid droplet; ISS:UniProtKB. DR GO; GO:0009615; P:response to virus; ISO:GO_Central. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:GO_Central. DR CDD; cd14420; CUE_AUP1; 1. DR FunFam; 1.10.8.10:FF:000049; ancient ubiquitous protein 1 isoform X2; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR048056; AUP1_CUE. DR InterPro; IPR003892; CUE. DR PANTHER; PTHR15486; ANCIENT UBIQUITOUS PROTEIN; 1. DR PANTHER; PTHR15486:SF96; LIPID DROPLET-REGULATING VLDL ASSEMBLY FACTOR AUP1; 1. DR Pfam; PF02845; CUE; 1. DR SMART; SM00546; CUE; 1. DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1. DR PROSITE; PS51140; CUE; 1. PE 1: Evidence at protein level; KW Acetylation; Endoplasmic reticulum; Lipid droplet; Membrane; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..410 FT /note="Lipid droplet-regulating VLDL assembly factor AUP1" FT /id="PRO_0000020766" FT TOPO_DOM 1..20 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9Y679" FT INTRAMEM 21..41 FT /evidence="ECO:0000250|UniProtKB:Q9Y679" FT TOPO_DOM 42..410 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9Y679" FT DOMAIN 296..338 FT /note="CUE" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468" FT REGION 258..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 344..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9Y679" FT MOD_RES 292 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y679" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y679" FT MOD_RES 367 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y679" SQ SEQUENCE 410 AA; 46121 MW; E7D070CEB296BD5B CRC64; MEPPPAPGPE RLFDSHRLPS DGFLLLALLL YAPVGLCLLV LRLFLGLHVF LVSCALPDSV LRRFVVRTMC AVLGLVARQE DSGLRDHRVR VLISNHVTPF DHNIVNLLTT CSTPLLNSPP SFVCWSRGFM EMDRRVELVE SLKKFCASTR LPPTPLLLFP EEEATNGREG LLRFSSWPFS IQDVVQPLTL QVQRPLVSVT VSDASWVSEL LWSLFVPFTV YQVRWLHPIR RQLGEESEEF ALRVQQLVAK ELGQIGTRLT PADKAEHMKR QRHPRLRPQS VQSSFPSPPS PSSDVQLTTL AHRVKEVLPH VPLNVIQRDL ARTGCVDLTI TNLLEGAVAF MPEDVTEGSQ SPPAPSAPKF PSSGLATPQP TALTFAKSSW ARQESLQERK QALYEYARRR FRERQAQEAE //