ID   CASP2_ARALL             Reviewed;         204 AA.
AC   D7LAP2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Casparian strip membrane protein 2;
DE            Short=AlCASP2;
GN   ORFNames=ARALYDRAFT_478496;
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47;
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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; GL348715; EFH58995.1; -; Genomic_DNA.
DR   RefSeq; XP_002882736.1; XM_002882690.1.
DR   AlphaFoldDB; D7LAP2; -.
DR   SMR; D7LAP2; -.
DR   STRING; 81972.D7LAP2; -.
DR   EnsemblPlants; fgenesh2_kg.3__1197__AT3G11550.1; fgenesh2_kg.3__1197__AT3G11550.1; fgenesh2_kg.3__1197__AT3G11550.1.
DR   Gramene; fgenesh2_kg.3__1197__AT3G11550.1; fgenesh2_kg.3__1197__AT3G11550.1; fgenesh2_kg.3__1197__AT3G11550.1.
DR   eggNOG; ENOG502QZV7; Eukaryota.
DR   HOGENOM; CLU_066104_3_1_1; -.
DR   OrthoDB; 1230007at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0048226; C:Casparian strip; IEA:EnsemblPlants.
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:0042545; P:cell wall modification; IEA:EnsemblPlants.
DR   GO; GO:0007043; P:cell-cell junction assembly; IEA:EnsemblPlants.
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..204
FT                   /note="Casparian strip membrane protein 2"
FT                   /id="PRO_0000411996"
FT   TOPO_DOM        1..42
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..92
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..204
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   204 AA;  21480 MW;  B064B6BE4D3A96B2 CRC64;
     MKNESTTIDV PAESSSAMKG KAPLIGVARD HTTSGSGGYN RGLSIFDFLL RLAAIVAALA
     AAATMGTSDE TLPFFTQFLQ FEASYDDLPT FQFFVIAMAL VGGYLVLSLP ISVVTILRPL
     ATAPRLLLLV LDTAVLALNT AAASSAAAIS YLAHSGNQNT NWLPICQQFG DFCQKSSGAV
     VSAFISVVFF TILVVISGVA LKRH