TM147_HUMAN
ID TM147_HUMAN Reviewed; 224 AA.
AC Q9BVK8; A8MWW0; O75790;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transmembrane protein 147;
DE AltName: Full=Protein NIFIE 14;
GN Name=TMEM147;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Tongue epithelium;
RA Daniell S.J., Perry B.N., Connerton I.F.;
RT "Cloning of a novel putative seven transmembrane domain protein from human
RT lingual tissue.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary, and Skin;
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 INTERACTION WITH NCLN AND NOMO, AND SUBCELLULAR LOCATION.
RX PubMed=20538592; DOI=10.1074/jbc.m110.132548;
RA Dettmer U., Kuhn P.H., Abou-Ajram C., Lichtenthaler S.F., Kruger M.,
RA Kremmer E., Haass C., Haffner C.;
RT "Transmembrane protein 147 (TMEM147) is a novel component of the Nicalin-
RT NOMO protein complex.";
RL J. Biol. Chem. 285:26174-26181(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHRM3; CHRM1 AND
RP AVPR2.
RX PubMed=21056967; DOI=10.1124/mol.110.067363;
RA Rosemond E., Rossi M., McMillin S.M., Scarselli M., Donaldson J.G.,
RA Wess J.;
RT "Regulation of M(3) muscarinic receptor expression and function by
RT transmembrane protein 147.";
RL Mol. Pharmacol. 79:251-261(2011).
RN [6]
RP FUNCTION, AND INTERACTION WITH TMCO1; CCDC47; NCLN; NOMO; SEC61A1; SEC61B
RP AND SEC61G.
RX PubMed=32820719; DOI=10.7554/elife.56889;
RA McGilvray P.T., Anghel S.A., Sundaram A., Zhong F., Trnka M.J.,
RA Fuller J.R., Hu H., Burlingame A.L., Keenan R.J.;
RT "An ER translocon for multi-pass membrane protein biogenesis.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Component of a ribosome-associated endoplasmic reticulum (ER)
CC translocon complex involved in multi-pass membrane protein transport
CC into the ER membrane and biogenesis (PubMed:32820719). Together with
CC SEC61 and TMCO1, forms the lipid-filled cavity at the center of the
CC translocon where TMEM147 may insert hydrophobic segments of mutli-pass
CC membrane proteins from the lumen into de central membrane cavity in a
CC process gated by SEC61, and TMCO1 may insert hydrophobic segments of
CC nascent chains from the cytosol into the cavity (PubMed:32820719). Acts
CC as a negative regulator of CHRM3 function, most likely by interfering
CC with its trafficking to the cell membrane. Negatively regulates CHRM3-
CC mediated calcium mobilization and activation of RPS6KA1/p90RSK activity
CC (PubMed:21056967). {ECO:0000269|PubMed:21056967,
CC ECO:0000269|PubMed:32820719}.
CC -!- SUBUNIT: Forms a complex with NCLN/Nicalin and NOMO, resulting in a
CC stabilization of the 3 proteins, which are otherwise quickly degraded
CC by the proteasome (PubMed:20538592). Interacts with CHRM3, CHRM1 and
CC AVPR2 (PubMed:21056967). The ribosome-associated ER translocon complex
CC includes SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and
CC TMEM147; in the absence of ribosomes, only the complex forms with
CC NCLN/Nicalin, NOMO and TMEM147 remains intact (PubMed:32820719).
CC {ECO:0000269|PubMed:20538592, ECO:0000269|PubMed:21056967,
CC ECO:0000269|PubMed:32820719}.
CC -!- INTERACTION:
CC Q9BVK8; O95870: ABHD16A; NbExp=4; IntAct=EBI-348587, EBI-348517;
CC Q9BVK8; P25942: CD40; NbExp=3; IntAct=EBI-348587, EBI-525714;
CC Q9BVK8; P11912: CD79A; NbExp=3; IntAct=EBI-348587, EBI-7797864;
CC Q9BVK8; O95471: CLDN7; NbExp=3; IntAct=EBI-348587, EBI-740744;
CC Q9BVK8; P58418: CLRN1; NbExp=3; IntAct=EBI-348587, EBI-17274839;
CC Q9BVK8; Q96BA8: CREB3L1; NbExp=9; IntAct=EBI-348587, EBI-6942903;
CC Q9BVK8; P25025: CXCR2; NbExp=3; IntAct=EBI-348587, EBI-2835281;
CC Q9BVK8; Q9P2X0-2: DPM3; NbExp=3; IntAct=EBI-348587, EBI-10962476;
CC Q9BVK8; Q15125: EBP; NbExp=3; IntAct=EBI-348587, EBI-3915253;
CC Q9BVK8; P52798: EFNA4; NbExp=3; IntAct=EBI-348587, EBI-5241592;
CC Q9BVK8; Q9Y6X5: ENPP4; NbExp=3; IntAct=EBI-348587, EBI-17442870;
CC Q9BVK8; Q9Y624: F11R; NbExp=3; IntAct=EBI-348587, EBI-742600;
CC Q9BVK8; O15552: FFAR2; NbExp=3; IntAct=EBI-348587, EBI-2833872;
CC Q9BVK8; P48165: GJA8; NbExp=3; IntAct=EBI-348587, EBI-17458373;
CC Q9BVK8; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-348587, EBI-712073;
CC Q9BVK8; Q96P66: GPR101; NbExp=3; IntAct=EBI-348587, EBI-17935713;
CC Q9BVK8; O60883: GPR37L1; NbExp=3; IntAct=EBI-348587, EBI-2927498;
CC Q9BVK8; O15529: GPR42; NbExp=3; IntAct=EBI-348587, EBI-18076404;
CC Q9BVK8; Q9BZJ8: GPR61; NbExp=3; IntAct=EBI-348587, EBI-12808020;
CC Q9BVK8; P28335: HTR2C; NbExp=4; IntAct=EBI-348587, EBI-994141;
CC Q9BVK8; P26951: IL3RA; NbExp=3; IntAct=EBI-348587, EBI-1757512;
CC Q9BVK8; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-348587, EBI-749265;
CC Q9BVK8; Q5T700: LDLRAD1; NbExp=7; IntAct=EBI-348587, EBI-10173166;
CC Q9BVK8; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-348587, EBI-17490413;
CC Q9BVK8; Q6ZUX7: LHFPL2; NbExp=3; IntAct=EBI-348587, EBI-17566767;
CC Q9BVK8; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-348587, EBI-3923617;
CC Q9BVK8; P15941-11: MUC1; NbExp=3; IntAct=EBI-348587, EBI-17263240;
CC Q9BVK8; Q9H813: PACC1; NbExp=4; IntAct=EBI-348587, EBI-4319734;
CC Q9BVK8; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-348587, EBI-16427978;
CC Q9BVK8; P15151: PVR; NbExp=3; IntAct=EBI-348587, EBI-3919694;
CC Q9BVK8; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-348587, EBI-1056589;
CC Q9BVK8; Q96GF1: RNF185; NbExp=3; IntAct=EBI-348587, EBI-2340249;
CC Q9BVK8; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-348587, EBI-4403649;
CC Q9BVK8; A0PJX4: SHISA3; NbExp=3; IntAct=EBI-348587, EBI-10171518;
CC Q9BVK8; Q14973: SLC10A1; NbExp=3; IntAct=EBI-348587, EBI-3923031;
CC Q9BVK8; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-348587, EBI-12854384;
CC Q9BVK8; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-348587, EBI-12808018;
CC Q9BVK8; Q96L08: SUSD3; NbExp=3; IntAct=EBI-348587, EBI-18194029;
CC Q9BVK8; Q8N205: SYNE4; NbExp=3; IntAct=EBI-348587, EBI-7131783;
CC Q9BVK8; P25103: TACR1; NbExp=3; IntAct=EBI-348587, EBI-6655287;
CC Q9BVK8; Q8N6K0: TEX29; NbExp=3; IntAct=EBI-348587, EBI-19027521;
CC Q9BVK8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-348587, EBI-8638294;
CC Q9BVK8; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-348587, EBI-10982110;
CC Q9BVK8; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-348587, EBI-10314986;
CC Q9BVK8; Q8N6L7: TMEM252; NbExp=3; IntAct=EBI-348587, EBI-8787626;
CC Q9BVK8; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-348587, EBI-12038591;
CC Q9BVK8; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-348587, EBI-18178701;
CC Q9BVK8; O95859: TSPAN12; NbExp=3; IntAct=EBI-348587, EBI-2466403;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20538592, ECO:0000269|PubMed:21056967}; Multi-pass
CC membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:I6VSD2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BVK8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVK8-2; Sequence=VSP_047210;
CC -!- SEQUENCE CAUTION:
CC Sequence=BG697070; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y18007; CAA77013.1; -; mRNA.
DR EMBL; AC002389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001118; AAH01118.1; -; mRNA.
DR EMBL; BG697070; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12466.1; -. [Q9BVK8-1]
DR CCDS; CCDS56091.1; -. [Q9BVK8-2]
DR RefSeq; NP_001229526.1; NM_001242597.1. [Q9BVK8-2]
DR RefSeq; NP_116024.1; NM_032635.3. [Q9BVK8-1]
DR PDB; 6W6L; EM; 3.84 A; 4=1-224.
DR PDBsum; 6W6L; -.
DR AlphaFoldDB; Q9BVK8; -.
DR SMR; Q9BVK8; -.
DR BioGRID; 115698; 70.
DR IntAct; Q9BVK8; 49.
DR STRING; 9606.ENSP00000222284; -.
DR TCDB; 8.A.145.1.1; the tmem147 (tmem147) family.
DR iPTMnet; Q9BVK8; -.
DR PhosphoSitePlus; Q9BVK8; -.
DR SwissPalm; Q9BVK8; -.
DR BioMuta; TMEM147; -.
DR DMDM; 74733336; -.
DR EPD; Q9BVK8; -.
DR jPOST; Q9BVK8; -.
DR MassIVE; Q9BVK8; -.
DR MaxQB; Q9BVK8; -.
DR PaxDb; Q9BVK8; -.
DR PeptideAtlas; Q9BVK8; -.
DR PRIDE; Q9BVK8; -.
DR ProteomicsDB; 2272; -.
DR ProteomicsDB; 79215; -. [Q9BVK8-1]
DR Antibodypedia; 54092; 89 antibodies from 23 providers.
DR DNASU; 10430; -.
DR Ensembl; ENST00000222284.10; ENSP00000222284.4; ENSG00000105677.12. [Q9BVK8-1]
DR Ensembl; ENST00000392204.6; ENSP00000376040.1; ENSG00000105677.12. [Q9BVK8-2]
DR GeneID; 10430; -.
DR KEGG; hsa:10430; -.
DR MANE-Select; ENST00000222284.10; ENSP00000222284.4; NM_032635.4; NP_116024.1.
DR UCSC; uc002oai.3; human. [Q9BVK8-1]
DR CTD; 10430; -.
DR DisGeNET; 10430; -.
DR GeneCards; TMEM147; -.
DR HGNC; HGNC:30414; TMEM147.
DR HPA; ENSG00000105677; Low tissue specificity.
DR MIM; 613585; gene.
DR neXtProt; NX_Q9BVK8; -.
DR OpenTargets; ENSG00000105677; -.
DR PharmGKB; PA144596255; -.
DR VEuPathDB; HostDB:ENSG00000105677; -.
DR eggNOG; KOG3236; Eukaryota.
DR GeneTree; ENSGT00390000013276; -.
DR InParanoid; Q9BVK8; -.
DR OMA; MKSTVDL; -.
DR OrthoDB; 1388283at2759; -.
DR PhylomeDB; Q9BVK8; -.
DR TreeFam; TF314086; -.
DR PathwayCommons; Q9BVK8; -.
DR SignaLink; Q9BVK8; -.
DR BioGRID-ORCS; 10430; 31 hits in 1081 CRISPR screens.
DR ChiTaRS; TMEM147; human.
DR GenomeRNAi; 10430; -.
DR Pharos; Q9BVK8; Tbio.
DR PRO; PR:Q9BVK8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BVK8; protein.
DR Bgee; ENSG00000105677; Expressed in right adrenal gland and 206 other tissues.
DR ExpressionAtlas; Q9BVK8; baseline and differential.
DR Genevisible; Q9BVK8; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR InterPro; IPR019164; TMEM147.
DR PANTHER; PTHR12869; PTHR12869; 1.
DR Pfam; PF09767; DUF2053; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..224
FT /note="Transmembrane protein 147"
FT /id="PRO_0000271701"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047210"
FT VARIANT 132
FT /note="Y -> H (in dbSNP:rs1269215)"
FT /id="VAR_051429"
FT CONFLICT 24..25
FT /note="SG -> TD (in Ref. 1; CAA77013)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="VH -> GP (in Ref. 1; CAA77013)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="S -> R (in Ref. 1; CAA77013)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..205
FT /note="ALLARAVVT -> VLMAGVVVK (in Ref. 1; CAA77013)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..215
FT /note="ALSTLAL -> VIRNLAM (in Ref. 1; CAA77013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25261 MW; 90122F32C34F16AE CRC64;
MTLFHFGNCF ALAYFPYFIT YKCSGLSEYN AFWKCVQAGV TYLFVQLCKM LFLATFFPTW
EGGIYDFIGE FMKASVDVAD LIGLNLVMSR NAGKGEYKIM VAALGWATAE LIMSRCIPLW
VGARGIEFDW KYIQMSIDSN ISLVHYIVAS AQVWMITRYD LYHTFRPAVL LLMFLSVYKA
FVMETFVHLC SLGSWAALLA RAVVTGLLAL STLALYVAVV NVHS
