T150A_HUMAN
ID T150A_HUMAN Reviewed; 271 AA.
AC Q86TG1; A8K764; B7WPQ9; D6W5L2; Q8N2R6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transmembrane protein 150A;
DE AltName: Full=Transmembrane protein 150;
GN Name=TMEM150A; Synonyms=TMEM150;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH PI4KA.
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).
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 (PubMed:25608530). Acts as
CC a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis
CC (PubMed:25608530). May also play a role in fasting-induced catabolism
CC (By similarity). {ECO:0000250|UniProtKB:Q9QZE9,
CC ECO:0000269|PubMed:25608530}.
CC -!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with PI4KA.
CC {ECO:0000269|PubMed:25608530}.
CC -!- INTERACTION:
CC Q86TG1; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2799342, EBI-10173507;
CC Q86TG1; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2799342, EBI-10171774;
CC Q86TG1; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2799342, EBI-945833;
CC Q86TG1; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2799342, EBI-22310682;
CC Q86TG1; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-2799342, EBI-5235829;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25608530};
CC Multi-pass membrane protein {ECO:0000269|PubMed:25608530}.
CC Note=Localizes mainly at the plasma membrane; only a minor fraction
CC localizes on intracellular structures (PubMed:25608530).
CC {ECO:0000269|PubMed:25608530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86TG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TG1-2; Sequence=VSP_022874, VSP_022875;
CC -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR EMBL; AK074505; BAC11029.1; -; mRNA.
DR EMBL; AK291879; BAF84568.1; -; mRNA.
DR EMBL; AC016753; AAY24344.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99503.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99499.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99500.1; -; Genomic_DNA.
DR EMBL; BC050466; AAH50466.1; -; mRNA.
DR CCDS; CCDS33233.1; -. [Q86TG1-1]
DR RefSeq; NP_001026908.1; NM_001031738.2. [Q86TG1-1]
DR RefSeq; XP_006711993.1; XM_006711930.3. [Q86TG1-1]
DR RefSeq; XP_006711994.1; XM_006711931.3. [Q86TG1-1]
DR RefSeq; XP_006711995.1; XM_006711932.2. [Q86TG1-2]
DR RefSeq; XP_011530810.1; XM_011532508.2. [Q86TG1-2]
DR AlphaFoldDB; Q86TG1; -.
DR BioGRID; 126189; 53.
DR IntAct; Q86TG1; 13.
DR STRING; 9606.ENSP00000387292; -.
DR TCDB; 8.A.113.1.2; the tentonin or tmem150 (tmem150) family.
DR GlyGen; Q86TG1; 2 sites.
DR iPTMnet; Q86TG1; -.
DR PhosphoSitePlus; Q86TG1; -.
DR BioMuta; TMEM150A; -.
DR DMDM; 74727425; -.
DR MassIVE; Q86TG1; -.
DR PaxDb; Q86TG1; -.
DR PeptideAtlas; Q86TG1; -.
DR PRIDE; Q86TG1; -.
DR ProteomicsDB; 69691; -. [Q86TG1-1]
DR Antibodypedia; 16968; 72 antibodies from 20 providers.
DR DNASU; 129303; -.
DR Ensembl; ENST00000306353.7; ENSP00000302715.3; ENSG00000168890.14. [Q86TG1-2]
DR Ensembl; ENST00000334462.10; ENSP00000334708.5; ENSG00000168890.14. [Q86TG1-1]
DR Ensembl; ENST00000409668.1; ENSP00000387292.1; ENSG00000168890.14. [Q86TG1-1]
DR GeneID; 129303; -.
DR KEGG; hsa:129303; -.
DR MANE-Select; ENST00000334462.10; ENSP00000334708.5; NM_001031738.3; NP_001026908.1.
DR UCSC; uc002spy.3; human. [Q86TG1-1]
DR CTD; 129303; -.
DR DisGeNET; 129303; -.
DR GeneCards; TMEM150A; -.
DR HGNC; HGNC:24677; TMEM150A.
DR HPA; ENSG00000168890; Low tissue specificity.
DR MIM; 616757; gene.
DR neXtProt; NX_Q86TG1; -.
DR OpenTargets; ENSG00000168890; -.
DR PharmGKB; PA165697532; -.
DR VEuPathDB; HostDB:ENSG00000168890; -.
DR eggNOG; KOG4320; Eukaryota.
DR GeneTree; ENSGT01030000234578; -.
DR HOGENOM; CLU_1457738_0_0_1; -.
DR InParanoid; Q86TG1; -.
DR OMA; WINTSAL; -.
DR OrthoDB; 955528at2759; -.
DR PhylomeDB; Q86TG1; -.
DR TreeFam; TF314508; -.
DR PathwayCommons; Q86TG1; -.
DR SignaLink; Q86TG1; -.
DR BioGRID-ORCS; 129303; 22 hits in 1082 CRISPR screens.
DR ChiTaRS; TMEM150A; human.
DR GeneWiki; TMEM150; -.
DR GenomeRNAi; 129303; -.
DR Pharos; Q86TG1; Tbio.
DR PRO; PR:Q86TG1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q86TG1; protein.
DR Bgee; ENSG00000168890; Expressed in body of pancreas and 164 other tissues.
DR ExpressionAtlas; Q86TG1; baseline and differential.
DR Genevisible; Q86TG1; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0009056; P:catabolic process; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR027315; TMEM150A.
DR PANTHER; PTHR21324:SF6; PTHR21324:SF6; 1.
DR Pfam; PF10277; Frag1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..271
FT /note="Transmembrane protein 150A"
FT /id="PRO_0000274775"
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:0000305|PubMed:25608530"
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"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022874"
FT VAR_SEQ 61..89
FT /note="DDVPLISKCGSYPPESCLFSLIGNMGAFM -> MYALWRTGPTTSPALLTLL
FT SKGVPRPAAPWTMSPSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022875"
FT CONFLICT 219
FT /note="L -> P (in Ref. 1; BAC11029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 28835 MW; 2995A8A8C53C35B0 CRC64;
MTAWILLPVS LSAFSITGIW TVYAMAVMNH HVCPVENWSY NESCPPDPAE QGGPKTCCTL
DDVPLISKCG SYPPESCLFS LIGNMGAFMV ALICLLRYGQ LLEQSRHSWV NTTALITGCT
NAAGLLVVGN FQVDHARSLH YVGAGVAFPA GLLFVCLHCA LSYQGATAPL DLAVAYLRSV
LAVIAFITLV LSGVFFVHES SQLQHGAALC EWVCVIDILI FYGTFSYEFG AVSSDTLVAA
LQPTPGRACK SSGSSSTSTH LNCAPESIAM I
