T150A_RAT
ID T150A_RAT Reviewed; 271 AA.
AC Q9QZE9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transmembrane protein 150A;
DE AltName: Full=Fasting-inducible integral membrane protein TM6P1;
DE AltName: Full=Transmembrane protein 150;
GN Name=Tmem150a; Synonyms=Tm6p1, Tmem150;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY FASTING.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10858565; DOI=10.1016/s0167-4781(00)00104-4;
RA Zhang J., D'Ercole A.J., Underwood L.E.;
RT "Identification of a new gene (rat TM6P1) encoding a fasting-inducible,
RT integral membrane protein with six transmembrane domains.";
RL Biochim. Biophys. Acta 1492:280-284(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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: Possible role in fasting-induced catabolism.
CC {ECO:0000269|PubMed:10858565}.
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
CC (PubMed:10858565). {ECO:0000250|UniProtKB:Q86TG1,
CC ECO:0000269|PubMed:10858565}.
CC -!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with PI4KA.
CC {ECO:0000250|UniProtKB:Q86TG1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10858565};
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 -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC placenta, liver and kidney. {ECO:0000269|PubMed:10858565}.
CC -!- INDUCTION: Up-regulated in the liver by fasting.
CC {ECO:0000269|PubMed:10858565}.
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR EMBL; AF186469; AAF01324.1; -; mRNA.
DR EMBL; BC072517; AAH72517.1; -; mRNA.
DR RefSeq; NP_620807.1; NM_139107.1.
DR RefSeq; XP_006236720.1; XM_006236658.3.
DR AlphaFoldDB; Q9QZE9; -.
DR STRING; 10116.ENSRNOP00000016002; -.
DR GlyGen; Q9QZE9; 2 sites.
DR PhosphoSitePlus; Q9QZE9; -.
DR PaxDb; Q9QZE9; -.
DR PRIDE; Q9QZE9; -.
DR Ensembl; ENSRNOT00000079415; ENSRNOP00000073089; ENSRNOG00000061100.
DR GeneID; 245966; -.
DR KEGG; rno:245966; -.
DR UCSC; RGD:619998; rat.
DR CTD; 129303; -.
DR RGD; 619998; Tmem150a.
DR eggNOG; KOG4320; Eukaryota.
DR GeneTree; ENSGT01030000234578; -.
DR HOGENOM; CLU_059992_1_0_1; -.
DR InParanoid; Q9QZE9; -.
DR OMA; WINTSAL; -.
DR OrthoDB; 955528at2759; -.
DR PhylomeDB; Q9QZE9; -.
DR TreeFam; TF314508; -.
DR PRO; PR:Q9QZE9; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000061100; Expressed in liver and 19 other tissues.
DR Genevisible; Q9QZE9; RN.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009056; P:catabolic process; IEP:RGD.
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_0000274777"
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..141
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..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; 29050 MW; 7E6CCB68D2849E5C CRC64;
MTAWILLPVS LSAFSITGIW TVYAMAVMNR HVCPVENWSY NDSCSPDPAE QGGPKTCCTL
DDVPLISKCG TYPPESCLFS LIGNMGAFMV ALICLLRYGQ LLEQNRHSWI NTTALITGCT
NAAGLVVVGN FQVDHAKSLH YIGAGVAFPA GLLFVCLHCV LFYHGATTPL DMAMAYLRSV
LAVIAFVTLV LSGVFFLHES SELQHGAALC EWVFVLDILI FYGTFSYEFG AVSSDTLVAA
LQPAPGRACK SSGSSSTSTH LNCAPESIAM I
