ID   FAF2_RAT                Reviewed;         346 AA.
AC   Q5BK32;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=FAS-associated factor 2;
DE   AltName: Full=UBX domain-containing protein 8;
GN   Name=Faf2; Synonyms=Ubxd8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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).
CC   -!- FUNCTION: Plays an important role in endoplasmic reticulum-associated
CC       degradation (ERAD) that mediates ubiquitin-dependent degradation of
CC       misfolded endoplasmic reticulum proteins. By controlling the steady-
CC       state expression of the IGF1R receptor, indirectly regulates the
CC       insulin-like growth factor receptor signaling pathway. Involved in
CC       inhibition of lipid droplet degradation by binding to phospholipase
CC       PNPL2 and inhibiting its activity by promoting dissociation of PNPL2
CC       from its endogenous activator, ABHD5 which inhibits the rate of
CC       triacylglycerol hydrolysis. {ECO:0000250|UniProtKB:Q96CS3}.
CC   -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8,
CC       UBE2J1/UBC6E and AUP1 (By similarity). Interacts with YOD1 (By
CC       similarity). Interacts (via N-terminus) with UBQLN2 (via C-terminus)
CC       (By similarity). Interacts with PNPLA2 and UBAC2 (By similarity).
CC       Interacts with ZFAND2B; probably through VCP (By similarity). Interacts
CC       with LMBR1L (By similarity). {ECO:0000250|UniProtKB:Q3TDN2,
CC       ECO:0000250|UniProtKB:Q96CS3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96CS3}. Lipid
CC       droplet {ECO:0000250|UniProtKB:Q96CS3}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q96CS3}.
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DR   EMBL; BC091224; AAH91224.1; -; mRNA.
DR   RefSeq; NP_001017445.1; NM_001017445.1.
DR   AlphaFoldDB; Q5BK32; -.
DR   SMR; Q5BK32; -.
DR   STRING; 10116.ENSRNOP00000063246; -.
DR   iPTMnet; Q5BK32; -.
DR   PhosphoSitePlus; Q5BK32; -.
DR   jPOST; Q5BK32; -.
DR   PaxDb; Q5BK32; -.
DR   PRIDE; Q5BK32; -.
DR   Ensembl; ENSRNOT00000064477; ENSRNOP00000063246; ENSRNOG00000017607.
DR   GeneID; 291000; -.
DR   KEGG; rno:291000; -.
DR   UCSC; RGD:1306577; rat.
DR   CTD; 23197; -.
DR   RGD; 1306577; Faf2.
DR   eggNOG; KOG1363; Eukaryota.
DR   GeneTree; ENSGT00940000157197; -.
DR   HOGENOM; CLU_047924_0_1_1; -.
DR   InParanoid; Q5BK32; -.
DR   PhylomeDB; Q5BK32; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR   PRO; PR:Q5BK32; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000017607; Expressed in liver and 19 other tissues.
DR   ExpressionAtlas; Q5BK32; baseline and differential.
DR   Genevisible; Q5BK32; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:RGD.
DR   GO; GO:0035473; F:lipase binding; ISO:RGD.
DR   GO; GO:0055102; F:lipase inhibitor activity; ISO:RGD.
DR   GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0034389; P:lipid droplet organization; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR006577; UAS.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001012; UBX_dom.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00594; UAS; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Endoplasmic reticulum; Lipid droplet;
KW   Reference proteome; Unfolded protein response.
FT   CHAIN           1..346
FT                   /note="FAS-associated factor 2"
FT                   /id="PRO_0000244066"
FT   DOMAIN          258..340
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          200..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          176..251
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        201..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96CS3"
SQ   SEQUENCE   346 AA;  41080 MW;  3852DEB92B939F44 CRC64;
     MLPFRFTYYT ILDIFRFALR FIRPDPRSRV TDPVGDIVSF MHSFEEKYGR AHPVFYQGTY
     SQALSDAKRE LRFLLVYLHG DDHQDSDEFC RNALCAPEVI SLINSRMLFW ACSTNKPEGY
     RVSQALRENT YPFLAMIMLK DRRMTVVGRL EGLIQPDDLI NQLTFIMDAN QTYLVSERLE
     REERNQTQVL RQQQDEAYLA SLRADQEKER KKREERERKR RKEEEVQQQK LAEERRRQNL
     QEEKERKLEC LPPEPSPDDP DSVKIIFKLP NDSRVERRFH FSQSLTVIHD FLFSLKESPE
     KFQIEANFPR RVLPCVPSEE WPNPPTLQEA GLSHTEVLFV QDLTDE