TMM64_MOUSE
ID TMM64_MOUSE Reviewed; 381 AA.
AC Q3U145; Q3TCK1; Q3TE31; Q6YI45; Q8CBJ4; Q8K2Q6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Transmembrane protein 64;
GN Name=Tmem64;
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=Kidney;
RA Ding P., Jin C., Han W., Wang L., Song Q., Zhang Y., Ma D.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Dendritic cell, and Spleen;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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, TISSUE SPECIFICITY, INTERACTION WITH ATP2A2, DISRUPTION
RP PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=23395171; DOI=10.1016/j.cmet.2013.01.002;
RA Kim H., Kim T., Jeong B.C., Cho I.T., Han D., Takegahara N.,
RA Negishi-Koga T., Takayanagi H., Lee J.H., Sul J.Y., Prasad V., Lee S.H.,
RA Choi Y.;
RT "Tmem64 modulates calcium signaling during RANKL-mediated osteoclast
RT differentiation.";
RL Cell Metab. 17:249-260(2013).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25979161; DOI=10.1016/j.bone.2015.05.009;
RA Jeong B.C., Kim T.S., Kim H.S., Lee S.H., Choi Y.;
RT "Transmembrane protein 64 reciprocally regulates osteoblast and adipocyte
RT differentiation by modulating Wnt/beta-catenin signaling.";
RL Bone 78:165-173(2015).
CC -!- FUNCTION: Positively regulates TNFSF11-induced osteoclast
CC differentiation. Acts as a regulator of TNFSF11-mediated Ca(2+)
CC signaling pathways via its interaction with SERCA2 which is critical
CC for the TNFSF11-induced CREB1 activation and mitochondrial ROS
CC generation necessary for proper osteoclast generation. Association
CC between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking
CC for activation of NFATC1 and production of mitochondrial ROS, thereby
CC triggering Ca (2+) signaling cascades that promote osteoclast
CC differentiation and activation (PubMed:23395171). Negatively regulates
CC osteoblast differentiation and positively regulates adipocyte
CC differentiation via modulation of the canonical Wnt signaling pathway.
CC Mediates the switch in lineage commitment to osteogenesis rather than
CC to adipogenesis in mesenchymal stem cells by negatively regulating the
CC expression, activity and nuclear localization of CTNNB1
CC (PubMed:25979161). {ECO:0000269|PubMed:23395171,
CC ECO:0000269|PubMed:25979161}.
CC -!- SUBUNIT: Interacts with ATP2A2 (PubMed:23395171).
CC {ECO:0000269|PubMed:23395171}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:23395171}.
CC -!- TISSUE SPECIFICITY: Liver, testis, kidney and muscle.
CC {ECO:0000269|PubMed:23395171}.
CC -!- DOMAIN: The VTT domain was previously called the SNARE-assoc domain. As
CC there is no evidence that this domain associates with SNARE proteins,
CC it was renamed as VMP1, TMEM41, and TVP38 (VTT) domain.
CC {ECO:0000250|UniProtKB:P36164}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit increased bone mass due in part to
CC impaired osteoclast formation. Bones show reduced osteoclast numbers
CC (PubMed:23395171). Increased osteogenesis and impaired adipogenesis
CC observed in bone marrow-derived stromal cells (PubMed:25979161).
CC {ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:25979161}.
CC -!- SIMILARITY: Belongs to the TVP38/TMEM64 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN05738.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY147882; AAN05738.1; ALT_FRAME; mRNA.
DR EMBL; AK035894; BAC29231.1; -; mRNA.
DR EMBL; AK156282; BAE33655.1; -; mRNA.
DR EMBL; AK169861; BAE41417.1; -; mRNA.
DR EMBL; AK170682; BAE41955.1; -; mRNA.
DR EMBL; AL732571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030341; AAH30341.1; -; mRNA.
DR CCDS; CCDS17983.1; -.
DR RefSeq; NP_852066.2; NM_181401.3.
DR AlphaFoldDB; Q3U145; -.
DR BioGRID; 221400; 1.
DR STRING; 10090.ENSMUSP00000055892; -.
DR PhosphoSitePlus; Q3U145; -.
DR PaxDb; Q3U145; -.
DR PRIDE; Q3U145; -.
DR ProteomicsDB; 259038; -.
DR Antibodypedia; 77108; 32 antibodies from 8 providers.
DR Ensembl; ENSMUST00000062684; ENSMUSP00000055892; ENSMUSG00000043252.
DR GeneID; 100201; -.
DR KEGG; mmu:100201; -.
DR UCSC; uc008sbk.2; mouse.
DR CTD; 169200; -.
DR MGI; MGI:2140359; Tmem64.
DR VEuPathDB; HostDB:ENSMUSG00000043252; -.
DR eggNOG; KOG3140; Eukaryota.
DR GeneTree; ENSGT00390000007813; -.
DR HOGENOM; CLU_069147_0_0_1; -.
DR InParanoid; Q3U145; -.
DR OMA; LMVYIVQ; -.
DR OrthoDB; 1327131at2759; -.
DR PhylomeDB; Q3U145; -.
DR TreeFam; TF323931; -.
DR BioGRID-ORCS; 100201; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem64; mouse.
DR PRO; PR:Q3U145; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3U145; protein.
DR Bgee; ENSMUSG00000043252; Expressed in urinary bladder urothelium and 226 other tissues.
DR Genevisible; Q3U145; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IMP:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:MGI.
DR InterPro; IPR032816; SNARE_assoc.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..381
FT /note="Transmembrane protein 64"
FT /id="PRO_0000287343"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..297
FT /note="VTT domain"
FT /evidence="ECO:0000250|UniProtKB:P36164"
FT CONFLICT 3
FT /note="N -> S (in Ref. 1; AAN05738 and 4; AAH30341)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Y -> D (in Ref. 2; BAE41417)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> R (in Ref. 2; BAE41417)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="S -> L (in Ref. 4; AAH30341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 39815 MW; 7C6AB3E0259E5DE4 CRC64;
MRNPGGSLPH TLPRALQHAG RTGVVEQPGR WAPERTAGGD RSEDRLPRGG GASAAAAAAA
AAASGALLGA YLERHGLPAA SDLPAPAGAL AGGPGSGGGV VVGVAEVRNW RCCCLGSTCW
CRSLVLVCVL AALCFASLAL VRRYLQHLLL WVESLDSLLG VLLFVVGFIV VSFPCGWGYI
VLNVAAGYLY GFVLGMGLMV VGVLIGTFIA HVVCKRLLTA WVAARIQNSD KLSAVIRVVE
GGSGLKVVAL ARLTPIPFGL QNAVFSITDV PLPSYLMASS AGLLPTQLLN SYLGTTLRTM
EDVIAEQSLS GYFVFCLQIV ISIGLMFYVV HRAQVELNAA IVACEMELKT SLVKGNQSDP
SGSSFYNKRT LTFSGGGINI V
