TM165_MOUSE
ID TM165_MOUSE Reviewed; 323 AA.
AC P52875; Q9R292;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Transmembrane protein 165;
DE AltName: Full=TPA-regulated locus protein;
DE AltName: Full=Transmembrane protein PFT27;
DE AltName: Full=Transmembrane protein TPARL;
DE Flags: Precursor;
GN Name=Tmem165; Synonyms=Tparl;
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 [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=3202867; DOI=10.1016/s0006-291x(88)80284-5;
RA Akagi J., Nomiyama H., Setoyama C., Shimada K., Akagi M.;
RT "Messenger RNA expressed in mouse teratocarcinoma stem cells and down-
RT regulated by a tumor-promoting phorbol ester codes for a novel
RT transmembrane protein.";
RL Biochem. Biophys. Res. Commun. 157:548-557(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11116088; DOI=10.1101/gr.10.12.1928;
RA Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.;
RT "The mouse Clock locus: sequence and comparative analysis of 204 kb from
RT mouse chromosome 5.";
RL Genome Res. 10:1928-1940(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a calcium/proton transporter involved in
CC calcium and in lysosomal pH homeostasis. Therefore, it may play an
CC indirect role in protein glycosylation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250}. Lysosome membrane {ECO:0000250}. Early
CC endosome membrane {ECO:0000250}. Late endosome membrane {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in undifferentiated mouse F9
CC teratocarcinoma stem cells but disappearing rapidly after treatment
CC with a tumor-promoting phorbol ester.
CC -!- SIMILARITY: Belongs to the GDT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40456.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M23568; AAA40456.1; ALT_FRAME; mRNA.
DR EMBL; AF146793; AAD30566.2; -; Genomic_DNA.
DR CCDS; CCDS19359.1; -.
DR PIR; A31351; A31351.
DR RefSeq; NP_035756.2; NM_011626.2.
DR AlphaFoldDB; P52875; -.
DR BioGRID; 204284; 12.
DR STRING; 10090.ENSMUSP00000031144; -.
DR TCDB; 2.A.106.2.1; the ca(2+):h(+) antiporter-2 (caca2) family.
DR iPTMnet; P52875; -.
DR PhosphoSitePlus; P52875; -.
DR EPD; P52875; -.
DR MaxQB; P52875; -.
DR PaxDb; P52875; -.
DR PeptideAtlas; P52875; -.
DR PRIDE; P52875; -.
DR ProteomicsDB; 259464; -.
DR Antibodypedia; 44090; 128 antibodies from 21 providers.
DR DNASU; 21982; -.
DR Ensembl; ENSMUST00000031144; ENSMUSP00000031144; ENSMUSG00000029234.
DR GeneID; 21982; -.
DR KEGG; mmu:21982; -.
DR UCSC; uc008xup.1; mouse.
DR CTD; 55858; -.
DR MGI; MGI:894407; Tmem165.
DR VEuPathDB; HostDB:ENSMUSG00000029234; -.
DR eggNOG; KOG2881; Eukaryota.
DR GeneTree; ENSGT00390000005261; -.
DR HOGENOM; CLU_040186_0_1_1; -.
DR InParanoid; P52875; -.
DR OMA; QGKWHSF; -.
DR OrthoDB; 919566at2759; -.
DR PhylomeDB; P52875; -.
DR TreeFam; TF105960; -.
DR BioGRID-ORCS; 21982; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem165; mouse.
DR PRO; PR:P52875; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P52875; protein.
DR Bgee; ENSMUSG00000029234; Expressed in molar tooth and 256 other tissues.
DR ExpressionAtlas; P52875; baseline and differential.
DR Genevisible; P52875; MM.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0032468; P:Golgi calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0032472; P:Golgi calcium ion transport; ISS:UniProtKB.
DR GO; GO:0071421; P:manganese ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0035751; P:regulation of lysosomal lumen pH; ISS:UniProtKB.
DR InterPro; IPR001727; Gdt1.
DR PANTHER; PTHR12608; PTHR12608; 1.
DR Pfam; PF01169; UPF0016; 2.
DR PROSITE; PS01214; UPF0016; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Golgi apparatus; Lysosome; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..323
FT /note="Transmembrane protein 165"
FT /id="PRO_0000212469"
FT TOPO_DOM 34..89
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..151
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..266
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..323
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 35..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..211
FT /evidence="ECO:0000255"
SQ SEQUENCE 323 AA; 34791 MW; 3CBE4348A5B70563 CRC64;
MAAAARGSGR APTRRLLVLL LLQLLWAPAG VRAGPEEDLS HRNQEPPAPA QQLQPQPAAV
QGLEPARAEK GLTPVAPVHT NKEDAAAQTN LGFIHAFVAA ISVIIVSELG DKTFFIAAIM
AMRYNRLTVL AGAMLALALM TCLSVLFGYA TTVIPRVYTY YVSTALFAIF GIRMLREGLK
MSPDEGQEEL EEVQAELKKK DEEFQRTKLL NGPDVETGTS TAIPQKKWLH FISPIFVQAL
TLTFLAEWGD RSQLTTIVLA AREDPYGVAV GGTVGHCLCT GLAVIGGRMI AQKISVRTVT
IIGGIVFLAF AFSALFISPE SGF
