T150B_HUMAN
ID T150B_HUMAN Reviewed; 233 AA.
AC A6NC51; B7ZW71;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Modulator of macroautophagy TMEM150B {ECO:0000305};
DE AltName: Full=Protein DRAM-3 {ECO:0000303|PubMed:25929859};
DE AltName: Full=Transmembrane protein 150B {ECO:0000312|HGNC:HGNC:34415};
DE AltName: Full=Transmembrane protein 224 {ECO:0000312|HGNC:HGNC:34415};
GN Name=TMEM150B {ECO:0000312|HGNC:HGNC:34415};
GN Synonyms=TMEM224 {ECO:0000312|HGNC:HGNC:34415};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-199.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-199.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=25608530; DOI=10.15252/embr.201439151;
RA Chung J., Nakatsu F., Baskin J.M., De Camilli P.;
RT "Plasticity of PI4KIIIalpha interactions at the plasma membrane.";
RL EMBO Rep. 16:312-320(2015).
RN [5]
RP TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25929859; DOI=10.1038/cdd.2015.26;
RA Mrschtik M., O'Prey J., Lao L.Y., Long J.S., Beaumatin F., Strachan D.,
RA O'Prey M., Skommer J., Ryan K.M.;
RT "DRAM-3 modulates autophagy and promotes cell survival in the absence of
RT glucose.";
RL Cell Death Differ. 22:1714-1726(2015).
CC -!- FUNCTION: Modulator of macroautophagy that causes accumulation of
CC autophagosomes under basal conditions and enhances autophagic flux
CC (PubMed:25929859). Represses cell death and promotes long-term
CC clonogenic survival of cells grown in the absence of glucose in a
CC macroautophagy-independent manner (PubMed:25929859). May have some role
CC in extracellular matrix engulfment or growth factor receptor recycling,
CC both of which can modulate cell survival (PubMed:25929859).
CC {ECO:0000269|PubMed:25929859}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25608530,
CC ECO:0000269|PubMed:25929859}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:25608530}. Endosome membrane
CC {ECO:0000269|PubMed:25929859}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:25929859}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes mainly at the plasma membrane where it
CC concentrates at actin-rich focal adhesions (PubMed:25608530,
CC PubMed:25929859). {ECO:0000269|PubMed:25608530,
CC ECO:0000269|PubMed:25929859}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the colon and lung with
CC comparatively high levels also detectable in the lymph nodes, placenta,
CC duodenum, peripheral blood mononuclear cells and spleen
CC (PubMed:25929859). {ECO:0000269|PubMed:25929859}.
CC -!- INDUCTION: Is not markedly up- or down-regulated by DNA damage,
CC nutrient deprivation or by exposure to TNF-alpha and IFN-gamma
CC (PubMed:25929859). {ECO:0000269|PubMed:25929859}.
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72362.1; -; Genomic_DNA.
DR EMBL; BC171904; AAI71904.1; -; mRNA.
DR CCDS; CCDS42629.1; -.
DR RefSeq; NP_001078957.1; NM_001085488.2.
DR RefSeq; NP_001268940.1; NM_001282011.1.
DR RefSeq; XP_005258869.1; XM_005258812.3.
DR RefSeq; XP_011525154.1; XM_011526852.2.
DR RefSeq; XP_011525155.1; XM_011526853.2.
DR RefSeq; XP_011525156.1; XM_011526854.2.
DR RefSeq; XP_011525157.1; XM_011526855.2.
DR RefSeq; XP_011525158.1; XM_011526856.2.
DR RefSeq; XP_016882156.1; XM_017026667.1.
DR AlphaFoldDB; A6NC51; -.
DR STRING; 9606.ENSP00000320757; -.
DR TCDB; 8.A.113.1.3; the tentonin or tmem150 (tmem150) family.
DR GlyGen; A6NC51; 1 site.
DR BioMuta; TMEM150B; -.
DR PaxDb; A6NC51; -.
DR PeptideAtlas; A6NC51; -.
DR PRIDE; A6NC51; -.
DR Antibodypedia; 66997; 54 antibodies from 11 providers.
DR DNASU; 284417; -.
DR Ensembl; ENST00000326652.9; ENSP00000320757.4; ENSG00000180061.10.
DR GeneID; 284417; -.
DR KEGG; hsa:284417; -.
DR MANE-Select; ENST00000326652.9; ENSP00000320757.4; NM_001282011.2; NP_001268940.1.
DR UCSC; uc010yfu.3; human.
DR CTD; 284417; -.
DR DisGeNET; 284417; -.
DR GeneCards; TMEM150B; -.
DR HGNC; HGNC:34415; TMEM150B.
DR HPA; ENSG00000180061; Tissue enriched (intestine).
DR neXtProt; NX_A6NC51; -.
DR OpenTargets; ENSG00000180061; -.
DR PharmGKB; PA165394503; -.
DR VEuPathDB; HostDB:ENSG00000180061; -.
DR eggNOG; KOG4320; Eukaryota.
DR GeneTree; ENSGT01030000234578; -.
DR InParanoid; A6NC51; -.
DR OMA; WICIIRY; -.
DR OrthoDB; 1199230at2759; -.
DR PhylomeDB; A6NC51; -.
DR TreeFam; TF314508; -.
DR PathwayCommons; A6NC51; -.
DR BioGRID-ORCS; 284417; 12 hits in 1068 CRISPR screens.
DR GenomeRNAi; 284417; -.
DR Pharos; A6NC51; Tbio.
DR PRO; PR:A6NC51; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; A6NC51; protein.
DR Bgee; ENSG00000180061; Expressed in monocyte and 93 other tissues.
DR ExpressionAtlas; A6NC51; baseline and differential.
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; IDA: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..233
FT /note="Modulator of macroautophagy TMEM150B"
FT /id="PRO_0000349284"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..51
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..116
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TG1"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 199
FT /note="L -> F (in dbSNP:rs7246479)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_046343"
SQ SEQUENCE 233 AA; 25701 MW; F818C4617E8AA9F8 CRC64;
MWGYLSLMPV FLAVWAISGV WIVFAIAVTN RTVDLSKGFP YISICGSFPP QSCIFSQVLN
MGAALAAWIC IVRYHQLRDW GVRRWPNQLI LWTGLLCALG TSVVGNFQEK NQRPTHLAGA
FLAFILGNVY FWLQLLLWRL KRLPQPGAAW IGPLRLGLCS VCTILIVAMI VLHACSLRSV
SAACEWVVAM LLFALFGLLA VDFSALESCT LCVQPWPSLS PPPASPISLP VQL
