CASP1_MALDO
ID CASP1_MALDO Reviewed; 175 AA.
AC P0DI54;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=MdCASP1;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. IM62; TISSUE=Root;
RA Korban S., Vodkin L., Liu L., Gasic K., Gonzales O., Hernandez A.,
RA Aldwinckle H., Malnoy M., Carroll N., Goldsbrough P., Orvis K., Clifton S.,
RA Pape D., Marra M., Hillier L., Martin J., Wylie T., Dante M., Theising B.,
RA Bowers Y., Gibbons M., Ritter E., Ronko I., Tsagareishvili R., Kennedy S.,
RA Waterston R., Wilson R.;
RT "Apple functional genomics grant - NSF 0321702.";
RL Submitted (APR-2009) 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; GO516639; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DI54; -.
DR STRING; 3750.XP_008348077.1; -.
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..175
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000417778"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 175 AA; 19047 MW; 91D84D3B0152CE6D CRC64;
MTSTAARAGV NRGASILDFI LRIVAFLGTL VSAVTMGTTR ERLPFFTQFL QFRAEYDDLP
TFTFFVVANS IVCAYLVFSL ALSVFHIIRS NAKKSRIILI FFDTAMLALL TAGASAAAAI
VYLSHKGNAK ANWFAICQQF NSFCERISGS LIGSFVGVVV FILLILLSAA ALSRR