AUP1_MOUSE
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 03-AUG-2022, entry version 137.
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}.
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DR EMBL; U41736; AAC52839.1; -; mRNA.
DR EMBL; BC016485; AAH16485.1; -; mRNA.
DR CCDS; CCDS39526.1; -.
DR RefSeq; NP_031543.2; NM_007517.4.
DR AlphaFoldDB; P70295; -.
DR SMR; P70295; -.
DR STRING; 10090.ENSMUSP00000090281; -.
DR iPTMnet; P70295; -.
DR PhosphoSitePlus; P70295; -.
DR SwissPalm; P70295; -.
DR EPD; P70295; -.
DR jPOST; P70295; -.
DR PaxDb; P70295; -.
DR PRIDE; P70295; -.
DR ProteomicsDB; 277209; -.
DR Ensembl; ENSMUST00000092618; ENSMUSP00000090281; ENSMUSG00000068328.
DR GeneID; 11993; -.
DR KEGG; mmu:11993; -.
DR UCSC; uc009clz.2; mouse.
DR CTD; 550; -.
DR MGI; MGI:107789; Aup1.
DR eggNOG; KOG2898; Eukaryota.
DR InParanoid; P70295; -.
DR PRO; PR:P70295; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P70295; protein.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
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:0097027; F:ubiquitin-protein transferase activator activity; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; 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:MGI.
DR GO; GO:1990044; P:protein localization to lipid droplet; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR003892; CUE.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 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 COMPBIAS 277..295
FT /note="Polar residues"
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
