ID   FAF2B_XENLA             Reviewed;         445 AA.
AC   Q6GQ69;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=FAS-associated factor 2-B;
DE   AltName: Full=UBX domain-containing protein 8-B;
GN   Name=faf2-b; Synonyms=ubxd8-b;
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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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; BC072879; AAH72879.1; -; mRNA.
DR   RefSeq; NP_001085517.1; NM_001092048.1.
DR   AlphaFoldDB; Q6GQ69; -.
DR   SMR; Q6GQ69; -.
DR   PRIDE; Q6GQ69; -.
DR   DNASU; 443943; -.
DR   GeneID; 443943; -.
DR   KEGG; xla:443943; -.
DR   CTD; 443943; -.
DR   Xenbase; XB-GENE-948055; faf2.L.
DR   OMA; RTLCNED; -.
DR   OrthoDB; 1251507at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 443943; 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-B"
FT                   /id="PRO_0000244068"
FT   DOMAIN          12..48
FT                   /note="UBA"
FT   DOMAIN          357..439
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          302..355
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;  52290 MW;  E798CCB4566618D6 CRC64;
     MAALEERGLS QDQTEKLLQF QDLTGIESID QCRQTLQQHN WNIETAVQDR LNEQEGVPRV
     FNTTPNRPLQ VNTADHRVYS YVVSRPQPRG LLGWGYYLIM LPFRITYYTV LDIFRFALRF
     IRPDPRSRVT DPVGDVVSFI HLFEEKYGST HPVFYQGTYS QALNDAKQEL RFLLVYLHGE
     DHQDSDDFCR NTLCTSEVTH FINSRMLFWA CSSNKPEGFR VSQALHESTY PFLAMIMLKD
     RRMTVVGRLE GLIQPQDLIN QLTFIIEANQ TYLVSERLER EERNQTQVLR QQQDEAYLVS
     LRADQEKERK KKEKQDQKRR EEEEAQRKQM LEERKKRNLE EEKERKSECL PAEPVPDHPD
     NVKIIFKMPN GTRVERRFLF TQSLSVIHDF LFSLKETPEK FQIVTSFPRQ VLPCLPSEEI
     PVPPTLQEAG LSQSQLLFVQ DLTDD