CASP1_STRAF
ID CASP1_STRAF Reviewed; 189 AA.
AC Q1W3A5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=SaCASP1;
DE Flags: Fragment;
OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX NCBI_TaxID=4170;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liang L., Lynn D.G.;
RT "Cloning of genes for Striga asiatica haustorium formation by suppressive
RT subtractive hybridization (SSH).";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ442388; ABD98039.1; -; mRNA.
DR AlphaFoldDB; Q1W3A5; -.
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..>189
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000370730"
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..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT NON_TER 189
SQ SEQUENCE 189 AA; 19990 MW; F0205A44CD3A53E2 CRC64;
MEKNESSAIE IAESSKERKG KAPLLAAAVG HDRAAGYKRG VSIFDLILRI SAATAALAAT
IVMGTTEQTL PFFTQFFQFR AQYDDLPTFT FFVVGMAIVT GYLILSVPLS IVCIARPVAI
GPRFLLIVCD TVTAVLATSA AGSSAAIVYL AHNGNSDANW LAICQQFNDF CQRVSGAVVA
AFVAVVCSS