ID   T15BA_XENLA             Reviewed;         230 AA.
AC   Q4V7T7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Modulator of macroautophagy TMEM150B-A {ECO:0000305};
DE   AltName: Full=Transmembrane protein 150B-A {ECO:0000250|UniProtKB:A6NC51};
GN   Name=tmem150b-a {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; BC097726; AAH97726.1; -; mRNA.
DR   RefSeq; NP_001089493.1; NM_001096024.2.
DR   AlphaFoldDB; Q4V7T7; -.
DR   DNASU; 734545; -.
DR   GeneID; 734545; -.
DR   KEGG; xla:734545; -.
DR   CTD; 734545; -.
DR   Xenbase; XB-GENE-5873625; tmem150b.S.
DR   OMA; ICLTIWA; -.
DR   OrthoDB; 1199230at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 734545; Expressed in gastrula and 3 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..230
FT                   /note="Modulator of macroautophagy TMEM150B-A"
FT                   /id="PRO_0000349287"
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..230
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   230 AA;  25410 MW;  A8A4C8C6D5CFF86B CRC64;
     MWAWALLPIC LTIWATAGIW IVYGMSVSNG SVNLSDGFPY ISLCGTDPPQ SCVFGQVLNV
     GAMLGVWISA IRFQQIRDYN CHSVLNSVSL AMGILCALGT SIVGNFQQSN QLETHLAGAF
     LAFVIGNIYF WMQTALTYMV KPTHGGCYIG PIRFCLSVAC TALIVLMAVF LKMNMKSISA
     ICEWIVAMIL FLLYGLFAVD FWHLDGHYFH VKKRTVIPNE MQVSTVTLSI