CSCLD_ARATH
ID CSCLD_ARATH Reviewed; 724 AA.
AC Q9C8G5; A0A097NUQ9; Q56WQ8; Q94B69; Q94II2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=CSC1-like protein ERD4 {ECO:0000305};
DE AltName: Full=Hyperosmolality-gated Ca2+ permeable channel 3.1 {ECO:0000303|PubMed:25162526};
DE Short=AtOSCA3.1 {ECO:0000303|PubMed:25162526};
DE AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION STRESS 4 {ECO:0000303|PubMed:24503647};
GN Name=ERD4 {ECO:0000303|PubMed:24503647};
GN Synonyms=OSCA3.1 {ECO:0000303|PubMed:25162526};
GN OrderedLocusNames=At1g30360 {ECO:0000312|Araport:AT1G30360};
GN ORFNames=T4K22.4 {ECO:0000312|EMBL:AAG51102.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=25162526; DOI=10.1038/nature13593;
RA Yuan F., Yang H., Xue Y., Kong D., Ye R., Li C., Zhang J.,
RA Theprungsirikul L., Shrift T., Krichilsky B., Johnson D.M., Swift G.B.,
RA He Y., Siedow J.N., Pei Z.M.;
RT "OSCA1 mediates osmotic-stress-evoked Ca(2+) increases vital for
RT osmosensing in Arabidopsis.";
RL Nature 514:367-371(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-724.
RC STRAIN=cv. Columbia;
RX PubMed=8075396; DOI=10.1007/bf00028874;
RA Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.;
RT "Cloning of cDNAs for genes that are early-responsive to dehydration stress
RT (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP
RT cognate genes.";
RL Plant Mol. Biol. 25:791-798(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 522-724.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY.
RX PubMed=24503647; DOI=10.1038/cr.2014.14;
RA Hou C., Tian W., Kleist T., He K., Garcia V., Bai F., Hao Y., Luan S.,
RA Li L.;
RT "DUF221 proteins are a family of osmosensitive calcium-permeable cation
RT channels conserved across eukaryotes.";
RL Cell Res. 24:632-635(2014).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS), FUNCTION, AND
RP HOMODIMERIZATION.
RX PubMed=30190597; DOI=10.1038/s41594-018-0117-6;
RA Zhang M., Wang D., Kang Y., Wu J.X., Yao F., Pan C., Yan Z., Song C.,
RA Chen L.;
RT "Structure of the mechanosensitive OSCA channels.";
RL Nat. Struct. Mol. Biol. 25:850-858(2018).
CC -!- FUNCTION: Acts as a hyperosmolarity-gated non-selective cation channel
CC that permeates Ca(2+) ions (PubMed:30190597). Mechanosensitive ion
CC channel that converts mechanical stimuli into a flow of ions
CC (PubMed:30190597). {ECO:0000269|PubMed:30190597}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30190597}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ920369; AIU34626.1; -; mRNA.
DR EMBL; AC025295; AAG51102.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31209.1; -; Genomic_DNA.
DR EMBL; AY035092; AAK59597.1; -; mRNA.
DR EMBL; AY042812; AAK68752.1; -; mRNA.
DR EMBL; AY063056; AAL34230.1; -; mRNA.
DR EMBL; AB039928; BAB63915.1; -; mRNA.
DR EMBL; AK221977; BAD94517.1; -; mRNA.
DR PIR; H86427; H86427.
DR RefSeq; NP_564354.1; NM_102773.3.
DR PDB; 5Z1F; EM; 4.80 A; A/B=1-724.
DR PDBsum; 5Z1F; -.
DR AlphaFoldDB; Q9C8G5; -.
DR SMR; Q9C8G5; -.
DR BioGRID; 25151; 17.
DR IntAct; Q9C8G5; 13.
DR STRING; 3702.AT1G30360.1; -.
DR SwissPalm; Q9C8G5; -.
DR PaxDb; Q9C8G5; -.
DR PRIDE; Q9C8G5; -.
DR ProteomicsDB; 220494; -.
DR EnsemblPlants; AT1G30360.1; AT1G30360.1; AT1G30360.
DR GeneID; 839916; -.
DR Gramene; AT1G30360.1; AT1G30360.1; AT1G30360.
DR KEGG; ath:AT1G30360; -.
DR Araport; AT1G30360; -.
DR TAIR; locus:2204227; AT1G30360.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_7_1_1; -.
DR InParanoid; Q9C8G5; -.
DR OMA; NLGLVWP; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; Q9C8G5; -.
DR PRO; PR:Q9C8G5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8G5; baseline and differential.
DR Genevisible; Q9C8G5; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005227; F:calcium activated cation channel activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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 3D-structure; Calcium; Coiled coil; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..724
FT /note="CSC1-like protein ERD4"
FT /id="PRO_0000429811"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 241..309
FT /evidence="ECO:0000255"
FT CONFLICT 284
FT /note="Y -> C (in Ref. 4; AAK68752)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="P -> T (in Ref. 4; AAK68752)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="D -> V (in Ref. 5; BAB63915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 81935 MW; 7E0D3247BD29C987 CRC64;
MEFGSFLVSL GTSFVIFVIL MLLFTWLSRK SGNAPIYYPN RILKGLEPWE GTSLTRNPFA
WMREALTSSE QDVVNLSGVD TAVHFVFLST VLGIFACSSL LLLPTLLPLA ATDNNIKNTK
NATDTTSKGT FSQLDNLSMA NITKKSSRLW AFLGAVYWIS LVTYFFLWKA YKHVSSLRAQ
ALMSADVKPE QFAILVRDMP APPDGQTQKE FIDSYFREIY PETFYRSLVA TENSKVNKIW
EKLEGYKKKL ARAEAILAAT NNRPTNKTGF CGLVGKQVDS IEYYTELINE SVAKLETEQK
AVLAEKQQTA AVVFFTTRVA AASAAQSLHC QMVDKWTVTE APEPRQLLWQ NLNIKLFSRI
IRQYFIYFFV AVTILFYMIP IAFVSAITTL KNLQRIIPFI KPVVEITAIR TVLESFLPQI
ALIVFLAMLP KLLLFLSKAE GIPSQSHAIR AASGKYFYFS VFNVFIGVTL AGTLFNTVKD
IAKNPKLDMI INLLATSLPK SATFFLTYVA LKFFIGYGLE LSRIIPLIIF HLKKKYLCKT
EAEVKEAWYP GDLSYATRVP GDMLILTITF CYSVIAPLIL IFGITYFGLG WLVLRNQALK
VYVPSYESYG RMWPHIHQRI LAALFLFQVV MFGYLGAKTF FYTALVIPLI ITSLIFGYVC
RQKFYGGFEH TALEVACREL KQSPDLEEIF RAYIPHSLSS HKPEEHEFKG AMSRYQDFNA
IAGV
