ID   CASP2_BRADI             Reviewed;         227 AA.
AC   P0DI37; A0A0Q3I2J9;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Casparian strip membrane protein 2;
DE            Short=BdCASP2;
GN   OrderedLocusNames=Bradi3g12975; ORFNames=LOC100836776;
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Bd21;
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
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; CM000882; KQJ94755.1; -; Genomic_DNA.
DR   RefSeq; XP_003571287.1; XM_003571239.3.
DR   AlphaFoldDB; P0DI37; -.
DR   STRING; 15368.BRADI3G12975.1; -.
DR   EnsemblPlants; KQJ94755; KQJ94755; BRADI_3g12975v3.
DR   GeneID; 100836776; -.
DR   Gramene; KQJ94755; KQJ94755; BRADI_3g12975v3.
DR   KEGG; bdi:100836776; -.
DR   eggNOG; ENOG502QZV7; Eukaryota.
DR   HOGENOM; CLU_066104_3_1_1; -.
DR   InParanoid; P0DI37; -.
DR   OMA; IGYLAHN; -.
DR   OrthoDB; 1385348at2759; -.
DR   Proteomes; UP000008810; Chromosome 3.
DR   GO; GO:0048226; C:Casparian strip; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0042545; P:cell wall modification; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   InterPro; IPR006459; CASP/CASPL.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
DR   TIGRFAMs; TIGR01569; A_tha_TIGR01569; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..227
FT                   /note="Casparian strip membrane protein 2"
FT                   /id="PRO_0000417763"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..107
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          17..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  24188 MW;  F76EED2884A14A3D CRC64;
     MSSTSEATVI HMDGAAGKTP ATAVPPPPPP APTAPVQQQR KAGGVPFLLR SGAEGFRRCM
     ALLDLLLRVA AMGPTLAAAI STGTSDETLS VFTHYFQFRA RFDDFSAFTF FMVANAVAAG
     YLLMSLPFSA FGVIRPKATS VRLLLLICDT IMVVLVTAAA SAAAAIVYVA HEGNRRANWV
     PICMQFHGFC KRTSGAVVAS FLAVLIFILL VFLGACAIRR RHTTTKH