TM147_MOUSE
ID TM147_MOUSE Reviewed; 224 AA.
AC Q9CQG6; Q8CI89; Q9D8F0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Transmembrane protein 147;
GN Name=Tmem147;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Pancreas, Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
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).
RN [4]
RP TISSUE SPECIFICITY.
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).
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. Together with SEC61 and TMCO1,
CC forms the lipid-filled cavity at the center of the translocon where
CC TMEM147 may insert hydrophobic segments of mutli-pass membrane proteins
CC from the lumen into de central membrane cavity in a process gated by
CC SEC61, and TMCO1 may insert hydrophobic segments of nascent chains from
CC the cytosol into the cavity. Acts as a negative regulator of CHRM3
CC function, most likely by interfering with its trafficking to the cell
CC membrane. Negatively regulates CHRM3-mediated calcium mobilization and
CC activation of RPS6KA1/p90RSK activity. {ECO:0000250|UniProtKB:Q9BVK8}.
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. Interacts with CHRM3, CHRM1 and AVPR2. The ribosome-
CC associated ER translocon complex includes SEC61A1, SEC61B, SEC61G,
CC TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence of
CC ribosomes, only the complex forms with NCLN/Nicalin, NOMO and TMEM147
CC remains intact. {ECO:0000250|UniProtKB:Q9BVK8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9BVK8}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:I6VSD2}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQG6-2; Sequence=VSP_022328, VSP_022329;
CC -!- TISSUE SPECIFICITY: Expressed in cerebral cortex, submandibular gland,
CC hypothalamus, pancreas, liver, and ileum.
CC {ECO:0000269|PubMed:21056967}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25453.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK007753; BAB25234.1; -; mRNA.
DR EMBL; AK008089; BAB25453.1; ALT_FRAME; mRNA.
DR EMBL; AK010168; BAB26744.1; -; mRNA.
DR EMBL; BC035323; AAH35323.1; -; mRNA.
DR CCDS; CCDS39890.1; -. [Q9CQG6-1]
DR RefSeq; NP_081491.2; NM_027215.2. [Q9CQG6-1]
DR AlphaFoldDB; Q9CQG6; -.
DR SMR; Q9CQG6; -.
DR BioGRID; 213689; 2.
DR STRING; 10090.ENSMUSP00000006478; -.
DR PhosphoSitePlus; Q9CQG6; -.
DR EPD; Q9CQG6; -.
DR jPOST; Q9CQG6; -.
DR MaxQB; Q9CQG6; -.
DR PaxDb; Q9CQG6; -.
DR PRIDE; Q9CQG6; -.
DR ProteomicsDB; 259534; -. [Q9CQG6-1]
DR ProteomicsDB; 259535; -. [Q9CQG6-2]
DR Antibodypedia; 54092; 89 antibodies from 23 providers.
DR DNASU; 69804; -.
DR Ensembl; ENSMUST00000006478; ENSMUSP00000006478; ENSMUSG00000006315. [Q9CQG6-1]
DR Ensembl; ENSMUST00000207779; ENSMUSP00000146550; ENSMUSG00000006315. [Q9CQG6-2]
DR GeneID; 69804; -.
DR KEGG; mmu:69804; -.
DR UCSC; uc009gga.1; mouse. [Q9CQG6-1]
DR CTD; 10430; -.
DR MGI; MGI:1915011; Tmem147.
DR VEuPathDB; HostDB:ENSMUSG00000006315; -.
DR eggNOG; KOG3236; Eukaryota.
DR GeneTree; ENSGT00390000013276; -.
DR HOGENOM; CLU_086813_0_0_1; -.
DR InParanoid; Q9CQG6; -.
DR OMA; MKSTVDL; -.
DR PhylomeDB; Q9CQG6; -.
DR TreeFam; TF314086; -.
DR BioGRID-ORCS; 69804; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Tmem147; mouse.
DR PRO; PR:Q9CQG6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CQG6; protein.
DR Bgee; ENSMUSG00000006315; Expressed in right kidney and 254 other tissues.
DR ExpressionAtlas; Q9CQG6; baseline and differential.
DR Genevisible; Q9CQG6; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS: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; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR InterPro; IPR019164; TMEM147.
DR PANTHER; PTHR12869; PTHR12869; 1.
DR Pfam; PF09767; DUF2053; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..224
FT /note="Transmembrane protein 147"
FT /id="PRO_0000271702"
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 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 93..112
FT /note="GKGEYKIMVAALGWATAELI -> DASPSGWEPEALNLTGNISR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022328"
FT VAR_SEQ 113..224
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022329"
FT CONFLICT 223
FT /note="H -> Q (in Ref. 1; BAB25453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25335 MW; 90122835A76E53AE CRC64;
MTLFHFGNCF ALAYFPYFIT YKCSGLSEYN AFWKCVQAGV TYLFVQLCKM LFLATFFPTW
EGGIYDFIGE FMKASVDVAD LIGLNLVMSR NAGKGEYKIM VAALGWATAE LIMSRCIPLW
VGARGIEFDW KYIQMSIDSN ISLVHYIVAS AQVWMITRYD LYHTFRPAVL LLMFLSVYKA
FVMETFVHLF SLGSWTALLA RAVVTGLLAL STLALYVAVV NVHS
