ID   CAS_MAIZE               Reviewed;         395 AA.
AC   B6TVL4;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Calcium sensing receptor, chloroplastic;
DE   AltName: Full=Sulfurtransferase 3;
DE   Flags: Precursor;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 375-383, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP   THR-377.
RC   STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX   PubMed=22833285; DOI=10.1002/pmic.201200196;
RA   Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT   "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT   sheath chloroplasts from maize plants grown under low or high light.";
RL   Proteomics 12:2852-2861(2012).
CC   -!- FUNCTION: Modulates cytoplasmic Ca(2+) concentration and is crucial for
CC       proper stomatal regulation in response to elevated levels of external
CC       Ca(2+). May function by regulating concentrations of inositol 1,4,5-
CC       trisphosphate (IP3), which in turn triggers release of Ca(2+) from
CC       internal stores. May play a role in de-etiolation.
CC       {ECO:0000250|UniProtKB:Q9FN48}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:22833285}; Single-pass membrane protein
CC       {ECO:0000255}; Stromal side {ECO:0000269|PubMed:22833285}.
CC   -!- PTM: Phosphorylated in both bundle sheath and mesophyll cells, under
CC       both low and high light regimes (70 vs 900 umol photons/m-2/s).
CC       {ECO:0000269|PubMed:22833285}.
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DR   EMBL; EU969029; ACG41147.1; -; mRNA.
DR   RefSeq; NP_001150975.1; NM_001157503.2.
DR   STRING; 4577.GRMZM2G122715_P02; -.
DR   iPTMnet; B6TVL4; -.
DR   PaxDb; B6TVL4; -.
DR   PRIDE; B6TVL4; -.
DR   GeneID; 100284608; -.
DR   KEGG; zma:100284608; -.
DR   eggNOG; ENOG502QSV6; Eukaryota.
DR   OrthoDB; 1224370at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; B6TVL4; baseline and differential.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:EnsemblPlants.
DR   GO; GO:0009704; P:de-etiolation; IEA:EnsemblPlants.
DR   GO; GO:0090333; P:regulation of stomatal closure; IEA:EnsemblPlants.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR044690; CAS_plant.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR34209; PTHR34209; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Membrane; Phosphoprotein; Plastid;
KW   Receptor; Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..395
FT                   /note="Calcium sensing receptor, chloroplastic"
FT                   /id="PRO_0000431068"
FT   TOPO_DOM        40..182
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000269|PubMed:22833285"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..395
FT                   /note="Stromal"
FT                   /evidence="ECO:0000269|PubMed:22833285"
FT   DOMAIN          224..345
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         377
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:22833285"
SQ   SEQUENCE   395 AA;  40094 MW;  D410232AEB9BF01D CRC64;
     MAPVPVSVSA TLAPPPAAPP KTTSRSWERR APADAAFAAA SSVAGSAALL TLTPAAPAAA
     LSKEDVAGSL TKAVDTVSQA IDVGGKAAEQ VAAVLKALGE AVKPALPVLK SASDEALKLA
     APVVSAASKQ ATEALQGAGV DPAPVLSVAK TAAEQSTKVI DAAKPVASAA VETITSLGPE
     DYVVAAGXAF LAYLLVPPVW SLVSSSLRGY KGDLTPAQAL DKVTTQGYVL IDVRSEKDKA
     KAGLPQLPSN AKNKLVSVPL EDLPSKLKGM VRNAKKAEAE IAALKISYLK KIGKGSNVII
     MDSYSDVAKT VAKTLDSVGF KNCWVMAGGF SGRKGWAQSR LGTDSYNLSV VEVVTPSRVI
     PAVAGRRTGT TAARIGTASS ASRATTRKLL PGGVD