ID   FAF2_XENTR              Reviewed;         445 AA.
AC   Q28BP9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=FAS-associated factor 2;
DE   AltName: Full=UBX domain-containing protein 8;
GN   Name=faf2; Synonyms=ubxd8; ORFNames=TNeu075m11.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2006) 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. Involved in inhibition of
CC       lipid droplet degradation. {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; CR942713; CAJ82812.1; -; mRNA.
DR   RefSeq; NP_001039235.1; NM_001045770.1.
DR   AlphaFoldDB; Q28BP9; -.
DR   SMR; Q28BP9; -.
DR   STRING; 8364.ENSXETP00000048152; -.
DR   PRIDE; Q28BP9; -.
DR   GeneID; 734096; -.
DR   KEGG; xtr:734096; -.
DR   CTD; 23197; -.
DR   Xenbase; XB-GENE-948050; faf2.
DR   eggNOG; KOG1363; Eukaryota.
DR   InParanoid; Q28BP9; -.
DR   OrthoDB; 1251507at2759; -.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000010945; Expressed in 2-cell stage embryo and 13 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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   Coiled coil; Cytoplasm; Endoplasmic reticulum; Lipid droplet;
KW   Reference proteome.
FT   CHAIN           1..445
FT                   /note="FAS-associated factor 2"
FT                   /id="PRO_0000244069"
FT   DOMAIN          12..53
FT                   /note="UBA"
FT   DOMAIN          357..439
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          303..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          275..353
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        303..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  52395 MW;  DA23F4B799D91041 CRC64;
     MAAPEERELS QEQTEKLLQF QDLTGIESMD QCRQTLQQHN WNIEAAVQDR LNEQEGVPSV
     FNTTPNRPLQ VNTADHRVYS YVVSRPQPRG LLGWGYYLIM LPFRITYYTL LDIFRFAVRF
     IRPDPRSRVT DPVGDVVSFI QLFEEKYGRI HPVFYQGTYS QALNDAKQEL RFLLVYLHGE
     DHQDSDDFCR NTLCIPEVTN FLNSRMLFWA CSTNKPEGFR VSQALRENTY PFLAMIMLKD
     RRMTVVGRLE GLIQPQDLIN QLTFIVEANQ TYLVSERLER EERNQTQVLR QQQDEAYLAS
     LRADQEKERK KKEKQEQKRR EEEEAQLKQM LEERKKRNLE EEKERKSECL PAEPVPDHPD
     NVKIIFKMPN GTRVERRFLF TQSLSVIHDF LFSLKETPEK FQIVTNFPRR VLPCLPSEEI
     PVPPTLQEAG LSQSQLLFVQ DLTDD