ID   AUP1_XENLA              Reviewed;         399 AA.
AC   B1H1N7; A1L2U0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Lipid droplet-regulating VLDL assembly factor AUP1 {ECO:0000250|UniProtKB:Q9Y679};
DE   AltName: Full=Ancient ubiquitous protein 1 {ECO:0000250|UniProtKB:Q9Y679};
GN   Name=aup1 {ECO:0000250|UniProtKB:Q9Y679};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Thymocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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). {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   -!- SIMILARITY: Belongs to the AUP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI29706.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC129705; AAI29706.1; ALT_INIT; mRNA.
DR   EMBL; BC160678; AAI60678.1; -; mRNA.
DR   RefSeq; NP_001116255.1; NM_001122783.1.
DR   AlphaFoldDB; B1H1N7; -.
DR   SMR; B1H1N7; -.
DR   GeneID; 100036951; -.
DR   KEGG; xla:100036951; -.
DR   CTD; 100036951; -.
DR   Xenbase; XB-GENE-6255853; aup1.S.
DR   OrthoDB; 1319689at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 100036951; Expressed in pancreas and 19 other tissues.
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:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
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:1990044; P:protein localization to lipid droplet; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF02845; CUE; 1.
DR   SMART; SM00546; CUE; 1.
DR   SMART; SM00563; PlsC; 1.
DR   PROSITE; PS51140; CUE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid droplet; Membrane; Reference proteome.
FT   CHAIN           1..399
FT                   /note="Lipid droplet-regulating VLDL assembly factor AUP1"
FT                   /id="PRO_0000359872"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y679"
FT   INTRAMEM        22..42
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y679"
FT   TOPO_DOM        43..399
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y679"
FT   DOMAIN          284..326
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   REGION          332..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        20
FT                   /note="F -> C (in Ref. 1; AAI29706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="R -> M (in Ref. 1; AAI29706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="Missing (in Ref. 1; AAI29706)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  44817 MW;  580A7112FA51950B CRC64;
     MEQPSLESML ELQRFPRNPF SLVLLLLYFP FGLCLFLIRL FIGAHVFLVS CVLPDSVFRR
     ILLRVMSSVL GVYVSHSELR PWDQRGKILI CNHRTAFDHS VISRIAPCCS PSVSCAPGFL
     CWARGFLELG ALGSRTQLME SLKHYLSQPG GAPLLLFPEE DTTNGRTGLL HFSSWPFSLS
     DSVQPLSLTV QRPLIAVAVS GCSWVTELFW LLFIPFTVYQ VRWLPSVCRL PRESDEDFAC
     RVQQIVSLSL GVVATRHTAA DRAEYVKRRR CELPAPKSQP LSPTHIQMAQ HVKEVLPQVP
     LSAIHRDLGH TGCVDTTITN FLEGRVTFVA EEEETTGAAE GTSKSRVSRP LPQGFAKKPE
     DRHLSLQDRK QILYECARRK YLEKFGSVPG EEEEEGARG