CSCL1_ARATH
ID CSCL1_ARATH Reviewed; 806 AA.
AC Q9FVQ5; I1VCA2; Q9C6X4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=CSC1-like protein At1g32090;
GN OrderedLocusNames=At1g32090; ORFNames=F3C3.11, T12O21.1;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22430844; DOI=10.1104/pp.111.193151;
RA Parsons H.T., Christiansen K., Knierim B., Carroll A., Ito J., Batth T.S.,
RA Smith-Moritz A.M., Morrison S., McInerney P., Hadi M.Z., Auer M.,
RA Mukhopadhyay A., Petzold C.J., Scheller H.V., Loque D., Heazlewood J.L.;
RT "Isolation and proteomic characterization of the Arabidopsis Golgi defines
RT functional and novel components involved in plant cell wall biosynthesis.";
RL Plant Physiol. 159:12-26(2012).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-735, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
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).
CC -!- FUNCTION: Acts as an osmosensitive calcium-permeable cation channel.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22430844}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22430844}. Cell membrane
CC {ECO:0000269|PubMed:22430844}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22430844}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50793.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JQ937229; AFI41197.1; -; mRNA.
DR EMBL; AC074309; AAG50793.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC084165; AAG23449.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31435.1; -; Genomic_DNA.
DR EMBL; AK229383; BAF01245.1; -; mRNA.
DR PIR; C86445; C86445.
DR RefSeq; NP_174489.1; NM_102943.6.
DR AlphaFoldDB; Q9FVQ5; -.
DR SMR; Q9FVQ5; -.
DR STRING; 3702.AT1G32090.1; -.
DR iPTMnet; Q9FVQ5; -.
DR PaxDb; Q9FVQ5; -.
DR PRIDE; Q9FVQ5; -.
DR ProteomicsDB; 220354; -.
DR EnsemblPlants; AT1G32090.1; AT1G32090.1; AT1G32090.
DR GeneID; 840101; -.
DR Gramene; AT1G32090.1; AT1G32090.1; AT1G32090.
DR KEGG; ath:AT1G32090; -.
DR Araport; AT1G32090; -.
DR TAIR; locus:2031735; AT1G32090.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_7_1_1; -.
DR InParanoid; Q9FVQ5; -.
DR OMA; QGIGMFP; -.
DR OrthoDB; 395194at2759; -.
DR PhylomeDB; Q9FVQ5; -.
DR PRO; PR:Q9FVQ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVQ5; baseline and differential.
DR Genevisible; Q9FVQ5; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA: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:0008381; F:mechanosensitive ion channel activity; 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 Calcium; Cell membrane; Golgi apparatus; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..806
FT /note="CSC1-like protein At1g32090"
FT /id="PRO_0000429799"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 726..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 735
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:14506206"
FT CONFLICT 456
FT /note="L -> I (in Ref. 1; AFI41197)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="I -> V (in Ref. 1; AFI41197)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="S -> P (in Ref. 1; AFI41197)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="T -> I (in Ref. 1; AFI41197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 93133 MW; AA28BE286BEE6B28 CRC64;
MATLQDIGVS ALINLFGAFL FLIAFAVLRI QPINDRVYFP KWYLTGERNS PRRSDRTLVG
KFVNLNYKTY FTFLNWMPQA MKMSESEIIR HAGLDSAIFL RIYTLGLKIF APVMVLALVV
LVPVNVSSGT LFFLKKELVV SNIDKLSISN VQPKSSKFFF HIAVEYIFTF WACFMLYREY
NNVAIMRLQY LASQRRRPEQ FTVVVRNVPD MPGHSVPDTV DQFFKTNHPE HYLCHQAVYN
ANTYAKLVKQ RAKLQRWFDY YVLKHQRNPH KQPTCRTGFL GLWGKRVDSI EYYKQQIKEF
DHNMSLERQK VLKDSKLMLP VAFVSFDSRW GAAVCAQTQQ SKNPTLWLTS SAPEPRDIYW
QNLAIPFISL TIRKLVIGVS VFALVFFYMI PIAFVQSLAN LEGLDRVAPF LRPVTRLDFI
KSFLQGFLPG LALKIFLWIL PTVLLIMSKI EGYIALSTLE RRAAAKYYYF MLVNVFLGSI
IAGTAFEQLH SFLHQSPSQI PRTIGVSIPM KATFFITYIM VDGWAGIAGE ILRLKPLVIF
HLKNMFIVKT EEDRVRAMDP GFVDFKETIP SLQLYFLLGI VYTAVTPILL PFILIFFAFA
YLVYRHQIIN VYNQQYESCG AFWPHVHGRI IASLLISQLL LMGLLASKKA ADSTPLLIIL
PILTLSFHKY CKHRFEPAFR QYPLEEAMAK DKLEKETEPE LNMKADLADA YLHPIFHSFE
KEVELSSSSS SEKETHQEET PEVRVDKHET QSSSPVTELG TSSHHHHVYN STSPSSHYAS
AYEQSSSQYE YHYNTHQYEE HEYRYN
