FAF2_BOVIN
ID FAF2_BOVIN Reviewed; 445 AA.
AC Q2HJD0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=FAS-associated factor 2;
DE AltName: Full=UBX domain-containing protein 8;
GN Name=FAF2; Synonyms=UBXD8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BC105572; AAI05573.1; -; mRNA.
DR RefSeq; NP_001070488.1; NM_001077020.1.
DR AlphaFoldDB; Q2HJD0; -.
DR BMRB; Q2HJD0; -.
DR SMR; Q2HJD0; -.
DR STRING; 9913.ENSBTAP00000052507; -.
DR PaxDb; Q2HJD0; -.
DR PRIDE; Q2HJD0; -.
DR Ensembl; ENSBTAT00000057329; ENSBTAP00000052507; ENSBTAG00000017744.
DR GeneID; 767948; -.
DR KEGG; bta:767948; -.
DR CTD; 23197; -.
DR VEuPathDB; HostDB:ENSBTAG00000017744; -.
DR VGNC; VGNC:28706; FAF2.
DR eggNOG; KOG1363; Eukaryota.
DR GeneTree; ENSGT00940000157197; -.
DR HOGENOM; CLU_047924_0_0_1; -.
DR InParanoid; Q2HJD0; -.
DR OMA; HTLFWAC; -.
DR OrthoDB; 1251507at2759; -.
DR TreeFam; TF314172; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000017744; Expressed in spermatocyte and 107 other tissues.
DR ExpressionAtlas; Q2HJD0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IEA:Ensembl.
DR GO; GO:0035473; F:lipase binding; IEA:Ensembl.
DR GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0034389; P:lipid droplet organization; IEA:Ensembl.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SUPFAM; SSF46934; SSF46934; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96CS3"
FT CHAIN 2..445
FT /note="FAS-associated factor 2"
FT /id="PRO_0000244063"
FT DOMAIN 12..48
FT /note="UBA"
FT DOMAIN 357..439
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 299..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 275..350
FT /evidence="ECO:0000255"
FT COMPBIAS 300..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96CS3"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96CS3"
SQ SEQUENCE 445 AA; 52664 MW; 42979FF2F5E38119 CRC64;
MAAPEERDLT QEQTEKLLQF QDLTGIESMD QCRHTLEQHN WNIEAAVQDR LNEQEGVPSV
FNPPPSRPLQ VNTADHRIYS YVVSRPQPRG LLGWGYYLIM LPFRFTYYTI LDIFRFALRF
IRPDPRNRVT DPVGDIVSFM HSFEEKYGRA HPVFYLGTYS QALNDAKREL RFLLVYLHGD
DHQDSDEFCR NTLCAPEVIS LINTRMLFWA CSTNKPEGYR VSQALRENTY PFLAMIMLKD
RRMTVVGRLE GLIQPDDLIN QLTFIMDANQ TYLVSERLER EERNQTQVLR QQQDEAYLAS
LRADQEKERK KREERERKRR KEEEVQQQKL AEERRRRNLQ EEKERKLECL PPEPSPDDPE
SVKIIFKLPN DSRVERRFHF SQSLTVIHDF LFSLKESPEK FQIEANFPRR VLPCLPSEEW
PNPPTLQEAG LSHTEVLFVQ DLTDE
