CASP1_PICGL
ID CASP1_PICGL Reviewed; 189 AA.
AC P0DH81;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=PgCASP1;
OS Picea glauca (White spruce) (Pinus glauca).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3330;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Root;
RA Morency M.-J., Cooke J., Pavy N., Parsons L., Paule C., Seguin A.,
RA Retzel E., Butterfield Y., Barber S., Yang G., Stott J., Siddiqui A.,
RA Holt R., Marra M., MacKay J.;
RT "Arborea EST sequencing in Picea glauca (white spruce).";
RL Submitted (JUL-2004) 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; CO480275; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DH81; -.
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; Glycoprotein; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..189
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000412209"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..73
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 189 AA; 20517 MW; 275F521BF2BB7900 CRC64;
MMQAESGSAE AKGPLPPPVG RKRRGLGILD FLLRLLAIGA TLSAAITMGT TNETLQFFTQ
FFQFKARFYD LSAFIYFVIA NAIVGGYLLL SLPISILNIV RPRAASSRVF LIFFDTVMVA
VCTSGAAAAV AILYVARKGN SRTNWFAICQ RFNSFCNQAI GAVSASFAGV VFLILLVLLS
ASTLYRRRP