T15BB_XENLA
ID T15BB_XENLA Reviewed; 231 AA.
AC Q4V7T3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Modulator of macroautophagy TMEM150B-B {ECO:0000305};
DE AltName: Full=Transmembrane protein 150B-B {ECO:0000250|UniProtKB:A6NC51};
GN Name=tmem150b-b {ECO:0000250|UniProtKB:A6NC51};
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 (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Modulator of macroautophagy that causes accumulation of
CC autophagosomes under basal conditions and enhances autophagic flux (By
CC similarity). Represses cell death and promotes long-term clonogenic
CC survival of cells grown in the absence of glucose in a macroautophagy-
CC independent manner (By similarity). May have some role in extracellular
CC matrix engulfment or growth factor receptor recycling, both of which
CC can modulate cell survival (By similarity).
CC {ECO:0000250|UniProtKB:A6NC51}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NC51};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:A6NC51}. Endosome
CC membrane {ECO:0000250|UniProtKB:A6NC51}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:A6NC51}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR EMBL; BC097732; AAH97732.1; -; mRNA.
DR RefSeq; NP_001090042.1; NM_001096573.1.
DR AlphaFoldDB; Q4V7T3; -.
DR DNASU; 735115; -.
DR GeneID; 735115; -.
DR KEGG; xla:735115; -.
DR CTD; 735115; -.
DR Xenbase; XB-GENE-6254290; tmem150b.L.
DR OrthoDB; 1199230at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 735115; Expressed in intestine and 5 other tissues.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR Pfam; PF10277; Frag1; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cell membrane; Cytoplasmic vesicle; Endosome; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..231
FT /note="Modulator of macroautophagy TMEM150B-B"
FT /id="PRO_0000349288"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..50
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..115
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..183
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TG1"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 231 AA; 25551 MW; 0F4BE98B343E0F8A CRC64;
MWAWALLPIC LTVWATGGIW IVYAMSVSNG SVNLSDGFPY ISVSGTYPPQ SCVFGQVLNV
GAMLAVWISV IRFQQIRDYN CHSVLNSVSL ATGILCALGT SIVGNFQQSN QLQTHLAGAF
LAFIIGNVYF WMQTALTYMV KPKHGGCYIG PIRFCLSIAC TALIVAMAVF LKMNMKSVSA
ICEWIVAMIL FLLYGLFAVD FWHLDGHFFH VKKRRTVIPN EMEVSTVTLS I