ID   T150B_BOVIN             Reviewed;         235 AA.
AC   A7MBB3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Modulator of macroautophagy TMEM150B {ECO:0000305};
DE   AltName: Full=Transmembrane protein 150B {ECO:0000250|UniProtKB:A6NC51};
GN   Name=TMEM150B {ECO:0000250|UniProtKB:A6NC51};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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}. Note=Localizes mainly at the plasma membrane where it
CC       concentrates at actin-rich focal adhesions (By similarity).
CC       {ECO:0000250|UniProtKB:A6NC51}.
CC   -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR   EMBL; BC151463; AAI51464.1; -; mRNA.
DR   RefSeq; NP_001095495.1; NM_001102025.2.
DR   RefSeq; XP_015313866.1; XM_015458380.1.
DR   RefSeq; XP_015313867.1; XM_015458381.1.
DR   AlphaFoldDB; A7MBB3; -.
DR   STRING; 9913.ENSBTAP00000049701; -.
DR   PaxDb; A7MBB3; -.
DR   Ensembl; ENSBTAT00000055412; ENSBTAP00000049701; ENSBTAG00000022813.
DR   Ensembl; ENSBTAT00000070615; ENSBTAP00000071501; ENSBTAG00000022813.
DR   GeneID; 515527; -.
DR   KEGG; bta:515527; -.
DR   CTD; 284417; -.
DR   VEuPathDB; HostDB:ENSBTAG00000022813; -.
DR   VGNC; VGNC:35981; TMEM150B.
DR   eggNOG; KOG4320; Eukaryota.
DR   GeneTree; ENSGT01030000234578; -.
DR   HOGENOM; CLU_059992_0_0_1; -.
DR   InParanoid; A7MBB3; -.
DR   OrthoDB; 1199230at2759; -.
DR   TreeFam; TF314508; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000022813; Expressed in monocyte and 100 other tissues.
DR   ExpressionAtlas; A7MBB3; baseline.
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..235
FT                   /note="Modulator of macroautophagy TMEM150B"
FT                   /id="PRO_0000349283"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..51
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..156
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TG1"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   235 AA;  26159 MW;  32E2204E4F9864BD CRC64;
     MWGYLSLLPM CLAFWAIAGI WTVFSLAVVN KAVNLTDGFP YISVCGNVPP QSCIFSQVLN
     IGAASAAWIC ILRYYQLRDW GVRKWHNQVI LWTGLLCALG TSIVGNFQEK NQRATHLTGA
     FLAFFVGIVY FWLQLFLSWR MKNLPQPGAP WIGPLRLVLC SACFILEVAM VVLHSWSMRS
     VSAICEWVAA MLLFILFGLL AVDFSRLDSC TLCLQPGSGS LRPPPDSPTS LHVQL