T178A_MOUSE
ID T178A_MOUSE Reviewed; 297 AA.
AC Q9CZ16; F8VPV2; Q8CEU4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Transmembrane protein 178A;
DE Flags: Precursor;
GN Name=Tmem178a; Synonyms=Tmem178;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH STIM1.
RX PubMed=26644563; DOI=10.1073/pnas.1511285112;
RA Decker C.E., Yang Z., Rimer R., Park-Min K.H., Macaubas C., Mellins E.D.,
RA Novack D.V., Faccio R.;
RT "Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
RT regulate bone mass.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:15654-15659(2015).
CC -!- FUNCTION: Acts as a negative regulator of osteoclast differentiation in
CC basal and inflammatory conditions by regulating TNFSF11-induced Ca (2+)
CC fluxes, thereby controlling the induction of NFATC1 (PubMed:26644563).
CC {ECO:0000269|PubMed:26644563}.
CC -!- SUBUNIT: Interacts with STIM1. {ECO:0000269|PubMed:26644563}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26644563}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the bone and its expression
CC increases during osteoclastogenesis. {ECO:0000269|PubMed:26644563}.
CC -!- DISRUPTION PHENOTYPE: Mice are osteopenic and are more susceptible to
CC inflammatory bone loss, owing to enhanced osteoclast formation.
CC {ECO:0000269|PubMed:26644563}.
CC -!- SIMILARITY: Belongs to the TMEM178 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28655.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC25428.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK013110; BAB28655.1; ALT_FRAME; mRNA.
DR EMBL; AK014196; BAC25428.1; ALT_FRAME; mRNA.
DR EMBL; AC163903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37705.1; -.
DR RefSeq; NP_080792.2; NM_026516.2.
DR AlphaFoldDB; Q9CZ16; -.
DR STRING; 10090.ENSMUSP00000025092; -.
DR GlyGen; Q9CZ16; 1 site.
DR PhosphoSitePlus; Q9CZ16; -.
DR PaxDb; Q9CZ16; -.
DR PRIDE; Q9CZ16; -.
DR ProteomicsDB; 254525; -.
DR Antibodypedia; 14741; 83 antibodies from 16 providers.
DR DNASU; 68027; -.
DR Ensembl; ENSMUST00000025092; ENSMUSP00000025092; ENSMUSG00000024245.
DR GeneID; 68027; -.
DR KEGG; mmu:68027; -.
DR UCSC; uc008drn.1; mouse.
DR CTD; 68027; -.
DR MGI; MGI:1915277; Tmem178.
DR VEuPathDB; HostDB:ENSMUSG00000024245; -.
DR eggNOG; ENOG502R2WV; Eukaryota.
DR GeneTree; ENSGT00390000015299; -.
DR HOGENOM; CLU_961492_0_0_1; -.
DR InParanoid; Q9CZ16; -.
DR OMA; ATYAGLW; -.
DR OrthoDB; 1336222at2759; -.
DR PhylomeDB; Q9CZ16; -.
DR TreeFam; TF331307; -.
DR BioGRID-ORCS; 68027; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9CZ16; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CZ16; protein.
DR Bgee; ENSMUSG00000024245; Expressed in cerebellum lobe and 161 other tissues.
DR Genevisible; Q9CZ16; MM.
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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR039625; T178A/B.
DR PANTHER; PTHR32005; PTHR32005; 1.
DR Pfam; PF13903; Claudin_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..297
FT /note="Transmembrane protein 178A"
FT /id="PRO_0000287281"
FT TOPO_DOM 26..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 41..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 47..48
FT /note="RA -> AR (in Ref. 1; BAB28655)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="G -> S (in Ref. 1; BAC25428)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="V -> A (in Ref. 1; BAC25428)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="K -> E (in Ref. 1; BAB28655)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="W -> C (in Ref. 1; BAB28655)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="G -> S (in Ref. 1; BAB28655)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="F -> L (in Ref. 1; BAC25428/BAB28655)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="IV -> SL (in Ref. 1; BAC25428)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="F -> C (in Ref. 1; BAB28655)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="R -> Q (in Ref. 1; BAB28655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33082 MW; E455E4544E48AE80 CRC64;
MEPRALVTAL SLGLSLCSLG LLVTAIFTDH WYETDPRRHK ESCERSRAGA DPPDQKNRLM
PLSHLPLRDS PPLGRRLLPG GPGRSDPESW RSLLGLGGLD AECGRPLFAT YSGLWRKCYF
LGIDRDIDTL ILKGIAQRCT AIKYHFSQPI RLRNIPFNLT KTIQQDEWHL LHLRRITAGF
LGMAVAVLLC GCIVATVSFF WEESLTQHVA GLLFLMTGIF CTISLCTYAA SVSYDLNRVP
KLIYSLPHDV EHGYSWSIFC AWCSLGFIVA AGGLCIAYPF ISRTKIAHLK SGRDSTV
