ID   FAF2A_XENLA             Reviewed;         445 AA.
AC   Q6AZH6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=FAS-associated factor 2-A;
DE   AltName: Full=UBX domain-containing protein 8-A;
GN   Name=faf2-a; Synonyms=ubxd8-a;
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;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC078001; AAH78001.1; -; mRNA.
DR   RefSeq; NP_001087113.1; NM_001093644.1.
DR   AlphaFoldDB; Q6AZH6; -.
DR   SMR; Q6AZH6; -.
DR   DNASU; 447002; -.
DR   GeneID; 447002; -.
DR   KEGG; xla:447002; -.
DR   CTD; 447002; -.
DR   Xenbase; XB-GENE-6254585; faf2.S.
DR   OrthoDB; 1251507at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 447002; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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-A"
FT                   /id="PRO_0000244067"
FT   DOMAIN          12..53
FT                   /note="UBA"
FT   DOMAIN          357..439
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          302..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          275..353
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        302..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  52616 MW;  B2E175781E86CB37 CRC64;
     MAALEERELS QEQTEKLLQF QDLTGIESMD QCRQTLQQHN WNIEAAVQDR LNEQEGVPRV
     FNNPPNRPLQ VNTADHRVYS YVVSRPQPRG LLGWGYYLIM LPFRITYYTL LDIFRFTLRF
     IRPDPRSRVT DPVGDVVSFI HLFEEKYGRI HPVFYQGTYS QALNDAKQEL RFLLVYLHGE
     DHQDSDDFCR NTLCTPEVTH FINSRMLFWA CSTNKPEGFR VSQALRENTY PFLGMIMLKD
     RRMTVVGRLE GLMQPQDLIN QLTFIIEANQ TYLVSERLER EERNETQVLR QQQDEAYLVS
     LRADQEKERK KKEKQEQKRR EEEEAQRKQM LEERKKRNLE EEKERKSECL PAEPVPDHPD
     NVKIIFKMPN GTRVERRFLF TQSLSVIHDF LFSLKETPEK FQIVTSFPRR VLPCLPSEEI
     PVPPTLQEAG LSQSQLLFVQ DLTDD