UN50B_XENLA
ID UN50B_XENLA Reviewed; 259 AA.
AC Q5U520;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Protein unc-50 homolog B;
GN Name=unc50-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].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the cell surface expression of neuronal nicotinic
CC receptors (By similarity). Binds RNA (By similarity).
CC {ECO:0000250|UniProtKB:O55227}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:O55227}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O55227}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q53HI1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q53HI1}.
CC -!- SIMILARITY: Belongs to the unc-50 family. {ECO:0000305}.
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DR EMBL; BC084865; AAH84865.1; -; mRNA.
DR RefSeq; NP_001088522.1; NM_001095053.2.
DR RefSeq; XP_018103913.1; XM_018248424.1.
DR AlphaFoldDB; Q5U520; -.
DR DNASU; 495394; -.
DR GeneID; 495394; -.
DR KEGG; xla:495394; -.
DR CTD; 495394; -.
DR Xenbase; XB-GENE-6253952; unc50.S.
DR OMA; IWFISNK; -.
DR OrthoDB; 1351297at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 495394; Expressed in oocyte and 19 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR InterPro; IPR007881; UNC-50.
DR PANTHER; PTHR12841; PTHR12841; 1.
DR Pfam; PF05216; UNC-50; 1.
PE 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Nucleus; Reference proteome; RNA-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Protein unc-50 homolog B"
FT /id="PRO_0000308966"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..259
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 259 AA; 30417 MW; 350DC453F4F47768 CRC64;
MLPTTSVSPR SPDNGILSPR DATRHTAGAK RYKYLRRLFH FKQMDFEFAL WQMLYLFTSP
QKVYRNFHYR KQTKDQWARD DPAFLVLLGI WLCVSTVGFG FVLDMSFFET FTLLLWVVFI
DCVGVGLLIA TSMWFVSNKY MVNRQGKDYD VEWGYTFDVH LNAFYPLLVI LHFIQLFFIN
HVILTGWFIG CFVGNTLWLI AIGYYIYITF LGYSALPFLK NTVVLLYPFA ALALLYILSL
ALGWNFTAKL CLFYKYRVR