CSCL1_MOUSE
ID CSCL1_MOUSE Reviewed; 804 AA.
AC Q91YT8; Q3TCS5; Q69ZZ1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=CSC1-like protein 1;
DE AltName: Full=Transmembrane protein 63A;
GN Name=Tmem63a; Synonyms=Kiaa0792;
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=NOD; TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, 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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel
CC (PubMed:27045885). Mechanosensitive ion channel that converts
CC mechanical stimuli into a flow of ion (PubMed:30382938).
CC {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:30382938}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O94886};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:27045885, ECO:0000269|PubMed:30382938}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE41880.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173027; BAD32305.1; ALT_INIT; mRNA.
DR EMBL; AK144899; BAE26121.1; -; mRNA.
DR EMBL; AK170559; BAE41880.1; ALT_SEQ; mRNA.
DR EMBL; BC014795; AAH14795.1; -; mRNA.
DR EMBL; BC019442; AAH19442.1; -; mRNA.
DR CCDS; CCDS15578.1; -.
DR RefSeq; NP_659043.1; NM_144794.2.
DR RefSeq; XP_006496784.1; XM_006496721.3.
DR RefSeq; XP_006496785.1; XM_006496722.2.
DR RefSeq; XP_006496786.1; XM_006496723.3.
DR AlphaFoldDB; Q91YT8; -.
DR SMR; Q91YT8; -.
DR BioGRID; 229015; 1.
DR STRING; 10090.ENSMUSP00000027800; -.
DR iPTMnet; Q91YT8; -.
DR PhosphoSitePlus; Q91YT8; -.
DR SwissPalm; Q91YT8; -.
DR EPD; Q91YT8; -.
DR MaxQB; Q91YT8; -.
DR PaxDb; Q91YT8; -.
DR PeptideAtlas; Q91YT8; -.
DR PRIDE; Q91YT8; -.
DR ProteomicsDB; 279069; -.
DR Antibodypedia; 34647; 76 antibodies from 16 providers.
DR DNASU; 208795; -.
DR Ensembl; ENSMUST00000027800; ENSMUSP00000027800; ENSMUSG00000026519.
DR Ensembl; ENSMUST00000161523; ENSMUSP00000124021; ENSMUSG00000026519.
DR GeneID; 208795; -.
DR KEGG; mmu:208795; -.
DR UCSC; uc007dwx.1; mouse.
DR CTD; 9725; -.
DR MGI; MGI:2384789; Tmem63a.
DR VEuPathDB; HostDB:ENSMUSG00000026519; -.
DR eggNOG; KOG1134; Eukaryota.
DR GeneTree; ENSGT00940000159576; -.
DR HOGENOM; CLU_015647_2_0_1; -.
DR InParanoid; Q91YT8; -.
DR OMA; TQVIWSN; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; Q91YT8; -.
DR TreeFam; TF324300; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 208795; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tmem63a; mouse.
DR PRO; PR:Q91YT8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91YT8; protein.
DR Bgee; ENSMUSG00000026519; Expressed in ascending aorta and 206 other tissues.
DR ExpressionAtlas; Q91YT8; baseline and differential.
DR Genevisible; Q91YT8; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IBA:GO_Central.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:1990760; F:osmolarity-sensing cation channel activity; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR032880; Csc1_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027815; PHM7_cyt.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR003864; RSN1_7TM.
DR InterPro; IPR026957; TMEM63A.
DR PANTHER; PTHR13018; PTHR13018; 1.
DR PANTHER; PTHR13018:SF24; PTHR13018:SF24; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Ion channel; Ion transport; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..804
FT /note="CSC1-like protein 1"
FT /id="PRO_0000280726"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 804 AA; 91860 MW; A8F024BA82F2AA33 CRC64;
MTSSPFLDPW PSKAVFVRER LGLGERPNDS YCYNSAKNST VLQGVTFGGI PTVLLLDVSC
FLFLILVFSI IRRRFWDYGR IALVSEAGSE ARFQRLSSSS SGQQDFENEL GCCPWLTAIF
RLHDDQILEW CGEDAIHYLS FQRHIIFLLV VISFLSLCVI LPVNLSGDLL GKDPYSFGRT
TIANLQTDND LLWLHTVFSV IYLFLTVGFM WHHTRSIRYK EESLVRQTLF ITGLPREARK
ETVESHFRDA YPTCEVVDVQ LCYSVAKLIY LCKERKKTEK SLTYYTNLQA KTGRRTLINP
KPCGQFCCCE VQGCEREDAI SYYTRMNDSL LERITAEESR VQDQPLGMAF VTFREKSMAT
YILKDFNACK CQGLRCKGEP QPSSYSRELC VSKWTVTFAS YPEDICWKNL SIQGVRWWLQ
WLGINFSLFV VLFFLTTPSI IMSTMDKFNV TKPIHALNNP VISQFFPTLL LWSFSALLPS
IVYYSTLLES HWTRSGENRI MVSKVYIFLI FMVLILPSLG LTSLDFFFRW LFDKTSSETS
IRLECVFLPD QGAFFVNYVI ASAFIGSGME LLRLPGLILY TFRMIMAKTA ADRRNVKQNQ
AFEYEFGAMY AWMLCVFTVI MAYSITCPII VPFGLIYILL KHMVDRHNLY FAYLPAKLEK
RIHFAAVNQA LAAPILCLFW LFFFSFLRLG LTAPATLFTF LVVLLTILAC LLYTCFGCFK
HLSPWNYKTE ESASDKGSEA EAHVPPPFTP YVPRILNGLA SERTALSPQQ QQTYGAIRNI
SGTLPGQPVA QDPSGTAAYA YQES
