T150A_MOUSE
ID T150A_MOUSE Reviewed; 271 AA.
AC Q91WN2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transmembrane protein 150A;
DE AltName: Full=Transmembrane protein 150;
GN Name=Tmem150a; Synonyms=Tmem150;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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).
CC -!- FUNCTION: Regulates localization of phosphatidylinositol 4-kinase
CC (PI4K) to the plasma membrane, possibly by reducing the association of
CC TTC7 (TTC7A or TTC7B) with the PI4K complex. Acts as a regulator of
CC phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (By
CC similarity). May also play a role in fasting-induced catabolism (By
CC similarity). {ECO:0000250|UniProtKB:Q86TG1,
CC ECO:0000250|UniProtKB:Q9QZE9}.
CC -!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with PI4KA.
CC {ECO:0000250|UniProtKB:Q86TG1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86TG1};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86TG1}.
CC Note=Localizes mainly at the plasma membrane; only a minor fraction
CC localizes on intracellular structures. {ECO:0000250|UniProtKB:Q86TG1}.
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR EMBL; BC014685; AAH14685.1; -; mRNA.
DR EMBL; BC028825; AAH28825.1; -; mRNA.
DR CCDS; CCDS20239.1; -.
DR RefSeq; NP_659165.1; NM_144916.3.
DR AlphaFoldDB; Q91WN2; -.
DR STRING; 10090.ENSMUSP00000063977; -.
DR GlyGen; Q91WN2; 2 sites.
DR iPTMnet; Q91WN2; -.
DR PhosphoSitePlus; Q91WN2; -.
DR jPOST; Q91WN2; -.
DR MaxQB; Q91WN2; -.
DR PaxDb; Q91WN2; -.
DR PRIDE; Q91WN2; -.
DR ProteomicsDB; 254625; -.
DR Antibodypedia; 16968; 72 antibodies from 20 providers.
DR Ensembl; ENSMUST00000069695; ENSMUSP00000063977; ENSMUSG00000055912.
DR GeneID; 232086; -.
DR KEGG; mmu:232086; -.
DR UCSC; uc009cih.1; mouse.
DR CTD; 129303; -.
DR MGI; MGI:2385244; Tmem150a.
DR VEuPathDB; HostDB:ENSMUSG00000055912; -.
DR eggNOG; KOG4320; Eukaryota.
DR GeneTree; ENSGT01030000234578; -.
DR HOGENOM; CLU_059992_1_0_1; -.
DR InParanoid; Q91WN2; -.
DR OMA; WINTSAL; -.
DR OrthoDB; 955528at2759; -.
DR PhylomeDB; Q91WN2; -.
DR TreeFam; TF314508; -.
DR BioGRID-ORCS; 232086; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Tmem150a; mouse.
DR PRO; PR:Q91WN2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91WN2; protein.
DR Bgee; ENSMUSG00000055912; Expressed in yolk sac and 62 other tissues.
DR ExpressionAtlas; Q91WN2; baseline and differential.
DR Genevisible; Q91WN2; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009056; P:catabolic process; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR027315; TMEM150A.
DR PANTHER; PTHR21324:SF6; PTHR21324:SF6; 1.
DR Pfam; PF10277; Frag1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..271
FT /note="Transmembrane protein 150A"
FT /id="PRO_0000274776"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..75
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..140
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..211
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q86TG1"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 271 AA; 29066 MW; 9F74F4B8F5136202 CRC64;
MTAWILLPVS LSAFSITGIW TVYAMAVMNR HVCPVENWSY NESCSPDPAE QGGPKSCCTL
DDVPLISKCG TYPPESCLFS LIGNMGAVMV ALICLLRYGQ LLEQSRHSWI NTTALITGCT
NAAGLVVVGN FQVDHAKSLH YIGTGVAFTA GLLFVCLHCV LFYHGATTPL DMAMAYLRSV
LAVIAFITLV LSGVFFLHES SQLQHGAALC EWVFVLDILI FYGTFSYEFG TISSDTLVAA
LQPAPGRACK SSGSSSTSTH LNCAPESIAM I
