CSC1_RAT
ID CSC1_RAT Reviewed; 802 AA.
AC D3ZNF5;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Calcium permeable stress-gated cation channel 1;
DE AltName: Full=Transmembrane protein 63C;
GN Name=Tmem63c; Synonyms=Csc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30900988; DOI=10.7554/elife.42068;
RA Schulz A., Mueller N.V., van de Lest N.A., Eisenreich A., Schmidbauer M.,
RA Barysenka A., Purfuerst B., Sporbert A., Lorenzen T., Meyer A.M.,
RA Herlan L., Witten A., Ruehle F., Zhou W., de Heer E., Scharpfenecker M.,
RA Panakova D., Stoll M., Kreutz R.;
RT "Analysis of the genomic architecture of a complex trait locus in
RT hypertensive rat models links Tmem63c to kidney damage.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel (By
CC similarity). Required for the functional integrity of the kidney
CC glomerular filtration barrier (PubMed:30900988).
CC {ECO:0000250|UniProtKB:Q9P1W3, ECO:0000269|PubMed:30900988}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8CBX0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in podocytes of kidney glomeruli.
CC {ECO:0000269|PubMed:30900988}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
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DR EMBL; AABR07065129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07065130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473982; EDL81621.1; -; Genomic_DNA.
DR EMBL; CH473982; EDL81622.1; -; Genomic_DNA.
DR RefSeq; NP_001101515.1; NM_001108045.1.
DR RefSeq; XP_006240444.1; XM_006240382.3.
DR RefSeq; XP_006240445.1; XM_006240383.3.
DR RefSeq; XP_006240446.1; XM_006240384.2.
DR RefSeq; XP_006240447.1; XM_006240385.3.
DR RefSeq; XP_006240448.1; XM_006240386.3.
DR RefSeq; XP_006240449.1; XM_006240387.3.
DR RefSeq; XP_006240451.1; XM_006240389.3.
DR RefSeq; XP_017449647.1; XM_017594158.1.
DR RefSeq; XP_017449648.1; XM_017594159.1.
DR RefSeq; XP_017449649.1; XM_017594160.1.
DR RefSeq; XP_017449650.1; XM_017594161.1.
DR AlphaFoldDB; D3ZNF5; -.
DR SMR; D3ZNF5; -.
DR STRING; 10116.ENSRNOP00000015571; -.
DR PaxDb; D3ZNF5; -.
DR Ensembl; ENSRNOT00000015571; ENSRNOP00000015571; ENSRNOG00000011334.
DR GeneID; 314332; -.
DR KEGG; rno:314332; -.
DR UCSC; RGD:1310207; rat.
DR CTD; 57156; -.
DR RGD; 1310207; Tmem63c.
DR eggNOG; KOG1134; Eukaryota.
DR GeneTree; ENSGT00940000159072; -.
DR HOGENOM; CLU_015647_0_0_1; -.
DR InParanoid; D3ZNF5; -.
DR OMA; QGIGMFP; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; D3ZNF5; -.
DR TreeFam; TF324300; -.
DR PRO; PR:D3ZNF5; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000011334; Expressed in cerebellum and 16 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; ISO:RGD.
DR GO; GO:1990760; F:osmolarity-sensing cation channel activity; ISS:UniProtKB.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0003094; P:glomerular filtration; IMP: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..802
FT /note="Calcium permeable stress-gated cation channel 1"
FT /id="PRO_0000448961"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 753..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBX0"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBX0"
SQ SEQUENCE 802 AA; 92962 MW; 2FDBCFF91A4CE111 CRC64;
MTASPESMGQ KFRNMTANEC FQSRSTVLQG QPFGGIPTVL LLNIILWVCV VLVYSFLRKA
AWDYGRLALL IHNDSLTSLI YGEQSEKSSP SEVYLEAERR DKGFSTWFFN SLTMRDRDLI
NKCGEDARIY IMFQYHLIIF VLILCIPSLG IILPVNYIGS ALDWSSHFGR TTIVNVSTES
QFLWLHSIFA FMYFLTNFAF MGHHCLGFVP KKNLHFTRTL MITYVPTEIQ DPETISKHFH
EAYPGCVVTR VHFCYDVRNL IDLDDQRRHA MRGRLYYTAK AKKTGKVMIK VHPCSHLCFC
KCWTCFKEVD AEQYYSELEE QLTDEFNAEL NRVQLKRLDL IFVTFQDART VKRIHNDYKY
INCGRHPMQS SVTTIVKNNH WRVARAPHPK DIIWKHLSIR RFSWWARFIA INTSLFFLFF
FLTTPAIIIN TIDMYNVTRP IEKLQSPVVT QFFPSVLLWA FTVIMPLLVY FSAFLEAHWT
RSNQNLIIMY KCYIFLVFMV VILPSMGLTS LDVFLRWLFD IYYLEHATIR FQCVFLPDNG
AFFINYVITS ALFGTGMELM RLGSLCTYCT RLFLSRSEPE RVHIRKNLAM DFQFGREYAW
MLNVFSVVMA YSITCPIIVP FGLLYLCMKH ITDRYNMYYS YAPTKLNAQI HMAAVYQAIF
APLLGLFWML FFSILRVGSL HSITLFSLSS IIISVIIAFS GVFLGKFRIA QQYEQPEEET
ETVFDVEPSS TTSTPTSLLY VATVLQEPEL NLTPASSPAR HTYGTMNSQP EEGEEESGLR
GFARELDPAQ FQEGLELEGQ SH
