ID   CASP1_STRHE             Reviewed;         202 AA.
AC   P0DI63;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Casparian strip membrane protein 1;
DE            Short=ShCASP1;
OS   Striga hermonthica (Purple witchweed) (Buchnera hermonthica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX   NCBI_TaxID=68872;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=20353604; DOI=10.1186/1471-2229-10-55;
RA   Yoshida S., Ishida J.K., Kamal N.M., Ali A.M., Namba S., Shirasu K.;
RT   "A full-length enriched cDNA library and expressed sequence tag analysis of
RT   the parasitic weed, Striga hermonthica.";
RL   BMC Plant Biol. 10:55-55(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; FS447700; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DI63; -.
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..202
FT                   /note="Casparian strip membrane protein 1"
FT                   /id="PRO_0000417807"
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..90
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   202 AA;  21561 MW;  D9C68A2FFF1E5B7E CRC64;
     MEKNKSTAIE IAESSKESKG KAPLLAAAVG HDRAAGYKRG VSIFDLFLRI SAATAALAAT
     IVMGTTEQTL PFFTQFFQFR AQYDDLPTFT FFVVGMAIVT GYLILSVPFS IVCIARPVAI
     GPRFLLIVGD TLKAVLATSA AGSSAAIVYL AHNGNSDANW LDICQQFNDF CQRVSGAVVA
     AFVAVVLLIF LIVLSAMALR KN