CASP1_TRIPD
ID CASP1_TRIPD Reviewed; 202 AA.
AC P0DI31;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 07-OCT-2020, entry version 15.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=TpCASP1;
OS Triphysaria pusilla (Dwarf owl's-clover) (Orthocarpus pusillus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Pedicularideae; Castillejinae;
OC Triphysaria.
OX NCBI_TaxID=188295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. TA-136; TISSUE=Root tip;
RA Tomilov A.A., Tomilova N.B., Matvienko M., Yoder J.I.;
RT "Early haustorium development in hemiparasitic Orobanchaceae.";
RL Submitted (NOV-2007) 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}.
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DR EMBL; EY144887; -; NOT_ANNOTATED_CDS; mRNA.
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_0000417812"
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..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 202 AA; 21660 MW; A5F55A1350BDF0A6 CRC64;
MEKSESSTIQ IAESSKDRKG KAPLLPPPVH HERAAGYKRG VAIFDLILRI SAATAALAAT
IVMGTTEQTL PFFTQFFQFR ASYDDLPTFT FFVIAMAIVT GYLILSVPFS IVCIARPVVA
APRILLILCD TLTVTLATSA AGASAAIVYL AHNGXSDANW LAICQQFNDF CQRVSGAVVA
AFVSAVLLIF LVVLSAIVLK KH