ID   CASP1_THECC             Reviewed;         200 AA.
AC   P0DI43;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Casparian strip membrane protein 1;
DE            Short=TcCASP1;
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hypocotyl;
RX   PubMed=18973681; DOI=10.1186/1471-2164-9-512;
RA   Argout X., Fouet O., Wincker P., Gramacho K., Legavre T., Sabau X.,
RA   Risterucci A.M., Da Silva C., Cascardo J., Allegre M., Kuhn D., Verica J.,
RA   Courtois B., Loor G., Babin R., Sounigo O., Ducamp M., Guiltinan M.J.,
RA   Ruiz M., Alemanno L., Machado R., Phillips W., Schnell R., Gilmour M.,
RA   Rosenquist E., Butler D., Maximova S., Lanaud C.;
RT   "Towards the understanding of the cocoa transcriptome: Production and
RT   analysis of an exhaustive dataset of ESTs of Theobroma cacao L. generated
RT   from various tissues and under various conditions.";
RL   BMC Genomics 9:512-512(2008).
RN   [2]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=24920445; DOI=10.1104/pp.114.239137;
RA   Roppolo D., Boeckmann B., Pfister A., Boutet E., Rubio M.C.,
RA   Denervaud-Tendon V., Vermeer J.E., Gheyselinck J., Xenarios I., Geldner N.;
RT   "Functional and evolutionary analysis of the CASPARIAN STRIP MEMBRANE
RT   DOMAIN PROTEIN family.";
RL   Plant Physiol. 165:1709-1722(2014).
CC   -!- FUNCTION: Regulates membrane-cell wall junctions and localized cell
CC       wall deposition. Required for establishment of the Casparian strip
CC       membrane domain (CSD) and the subsequent formation of Casparian strips,
CC       a cell wall modification of the root endodermis that determines an
CC       apoplastic barrier between the intraorganismal apoplasm and the
CC       extraorganismal apoplasm and prevents lateral diffusion (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Very restricted localization following a
CC       belt shape within the plasma membrane which coincides with the position
CC       of the Casparian strip membrane domain in the root endodermis.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC       family. {ECO:0000305}.
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DR   EMBL; CU571771; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_007027844.2; XM_007027782.2.
DR   AlphaFoldDB; P0DI43; -.
DR   STRING; 3641.EOY08346; -.
DR   EnsemblPlants; EOY08346; EOY08346; TCM_022705.
DR   EnsemblPlants; Tc05v2_t008240.1; Tc05v2_p008240.1; Tc05v2_g008240.
DR   GeneID; 18598306; -.
DR   Gramene; EOY08346; EOY08346; TCM_022705.
DR   Gramene; Tc05v2_t008240.1; Tc05v2_p008240.1; Tc05v2_g008240.
DR   KEGG; tcc:18598306; -.
DR   eggNOG; ENOG502QZV7; Eukaryota.
DR   OrthoDB; 1230007at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR006459; CASP/CASPL.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
DR   TIGRFAMs; TIGR01569; A_tha_TIGR01569; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..200
FT                   /note="Casparian strip membrane protein 1"
FT                   /id="PRO_0000417809"
FT   TOPO_DOM        1..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..86
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   200 AA;  21120 MW;  FE91F0CA8A8DB0EA CRC64;
     MKSGDHAAID VPESSAVAKG KAPLIATPRE QKSGFKKGLG IFDFLLRLGA IIAALAAAAT
     MGTSDETLPF FTQFFQFEAS YDDLPTFMFF VIAMALIGGY LVLSLPFSIV TIVRPHAVAP
     RLLLFILDIV ALTLTTAAGA AAAAIVYLAH NGNPNTNWLA ICQQFGDFCQ EVSGAVVASF
     VTVVVLMSLV LLSGVALKKH