CSCL2_MOUSE
ID CSCL2_MOUSE Reviewed; 832 AA.
AC Q3TWI9; Q6PCL2; Q6PGA4; Q8C1V5; Q8R0W7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=CSC1-like protein 2;
DE AltName: Full=Transmembrane protein 63B;
GN Name=Tmem63b;
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=Lung;
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] OF 179-832.
RC STRAIN=FVB/N; TISSUE=Liver, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-114 AND SER-115, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-113; SER-114 AND
RP SER-115, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, 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).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27045885; DOI=10.1002/cbf.3185;
RA Zhao X., Yan X., Liu Y., Zhang P., Ni X.;
RT "Co-expression of mouse TMEM63A, TMEM63B and TMEM63C confers
RT hyperosmolarity activated ion currents in HEK293 cells.";
RL Cell Biochem. Funct. 34:238-241(2016).
RN [7]
RP FUNCTION.
RX PubMed=30382938; DOI=10.7554/elife.41844;
RA Murthy S.E., Dubin A.E., Whitwam T., Jojoa-Cruz S., Cahalan S.M.,
RA Mousavi S.A.R., Ward A.B., Patapoutian A.;
RT "OSCA/TMEM63 are an Evolutionarily Conserved Family of Mechanically
RT Activated Ion Channels.";
RL Elife 7:0-0(2018).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31243992; DOI=10.1021/acs.biochem.9b00224;
RA Marques M.C., Albuquerque I.S., Vaz S.H., Bernardes G.J.L.;
RT "Overexpression of Osmosensitive Ca2+-Permeable Channel TMEM63B Promotes
RT Migration in HEK293T Cells.";
RL Biochemistry 58:2861-2866(2019).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel
CC (PubMed:27045885, PubMed:31243992). Mechanosensitive ion channel that
CC converts mechanical stimuli into a flow of ion (PubMed:30382938).
CC {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:30382938,
CC ECO:0000269|PubMed:31243992}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27045885,
CC ECO:0000269|PubMed:31243992}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57136.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH59283.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK090200; BAC41131.1; -; mRNA.
DR EMBL; AK159673; BAE35277.1; -; mRNA.
DR EMBL; BC026370; AAH26370.1; -; mRNA.
DR EMBL; BC057136; AAH57136.1; ALT_INIT; mRNA.
DR EMBL; BC059283; AAH59283.1; ALT_INIT; mRNA.
DR CCDS; CCDS28814.1; -.
DR RefSeq; NP_937810.2; NM_198167.3.
DR RefSeq; XP_006524199.1; XM_006524136.1.
DR RefSeq; XP_006524200.1; XM_006524137.2.
DR AlphaFoldDB; Q3TWI9; -.
DR SMR; Q3TWI9; -.
DR BioGRID; 230322; 3.
DR IntAct; Q3TWI9; 1.
DR STRING; 10090.ENSMUSP00000109151; -.
DR iPTMnet; Q3TWI9; -.
DR PhosphoSitePlus; Q3TWI9; -.
DR SwissPalm; Q3TWI9; -.
DR jPOST; Q3TWI9; -.
DR MaxQB; Q3TWI9; -.
DR PaxDb; Q3TWI9; -.
DR PeptideAtlas; Q3TWI9; -.
DR PRIDE; Q3TWI9; -.
DR ProteomicsDB; 285341; -.
DR Antibodypedia; 30591; 35 antibodies from 13 providers.
DR DNASU; 224807; -.
DR Ensembl; ENSMUST00000113523; ENSMUSP00000109151; ENSMUSG00000036026.
DR GeneID; 224807; -.
DR KEGG; mmu:224807; -.
DR UCSC; uc012auh.1; mouse.
DR CTD; 55362; -.
DR MGI; MGI:2387609; Tmem63b.
DR VEuPathDB; HostDB:ENSMUSG00000036026; -.
DR eggNOG; KOG1134; Eukaryota.
DR GeneTree; ENSGT00940000157084; -.
DR HOGENOM; CLU_015647_0_0_1; -.
DR InParanoid; Q3TWI9; -.
DR OMA; NLGLVWP; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; Q3TWI9; -.
DR TreeFam; TF324300; -.
DR BioGRID-ORCS; 224807; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tmem63b; mouse.
DR PRO; PR:Q3TWI9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3TWI9; protein.
DR Bgee; ENSMUSG00000036026; Expressed in retinal neural layer and 245 other tissues.
DR ExpressionAtlas; Q3TWI9; baseline and differential.
DR Genevisible; Q3TWI9; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:UniProtKB.
DR GO; GO:1990760; F:osmolarity-sensing cation channel activity; IDA:UniProtKB.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR003864; RSN1_7TM.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..832
FT /note="CSC1-like protein 2"
FT /id="PRO_0000280729"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 748..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 619
FT /note="Q -> R (in Ref. 1; BAC41131)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="L -> P (in Ref. 2; AAH26370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 94775 MW; E162259652DAE89C CRC64;
MLPFLLATLG TAALNSSNPK DYCYSARIRS TVLQGLPFGG VPTVLALDFM CFLALLFLFS
ILRKVAWDYG RLALVTDADR LRRQERERVE QEYVASAMHG DSHDRYERLT SVSSSVDFDQ
RDNGFCSWLT AIFRIKDDEI RDKCGGDAVH YLSFQRHIIG LLVVVGVLSV GIVLPVNFSG
DLLENNAYSF GRTTIANLKS GNNLLWLHTS FAFLYLLLTV YSMRRHTSKM RYKEDDLVKR
TLFINGISKY AESEKIKKHF EEAYPNCTVL EARPCYNVAR LMFLDAERKK AERGKLYFTN
LQSKENVPAM INPKPCGHLC CCVVRGCEQV EAIEYYTKLE QRLKEDYRRE KEKVNEKPLG
MAFVTFHNET ITAIILKDFN VCKCQGCTCR GEPRASSCSE ALHISNWTVT YAPDPQNIYW
EHLSIRGFIW WLRCLVINVV LFILLFFLTT PAIIITTMDK FNVTKPVEYL NNPIITQFFP
TLLLWCFSAL LPTIVYYSAF FEAHWTRSGE NRTTMHKCYT FLIFMVLLLP SLGLSSLDLF
FRWLFDKKFL AEAAIRFECV FLPDNGAFFV NYVIASAFIG NAMDLLRIPG LLMYMIRLCL
ARSAAERRNV KRHQAYEFQF GAAYAWMMCV FTVVMTYSIT CPIIVPFGLM YMLLKHLVDR
YNLYYAYLPA KLDKKIHSGA VNQVVAAPIL CLFWLLFFST MRTGFLAPTS MFTFVVLVIT
IVICLCHVCF GHFKYLSAHN YKIEHTETDA VSSRSNGRPP TAGAVPKSAK YIAQVLQDSE
GDGDGDGAPG SSGDEPPSSS SQDEELLMPP DGLTDTDFQS CEDSLIENEI HQ
