CASP1_LOTJA
ID CASP1_LOTJA Reviewed; 186 AA.
AC P0DKC2;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=LjCASP1;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyakojima MG-20;
RX PubMed=18511435; DOI=10.1093/dnares/dsn008;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Kato T., Nakao M.,
RA Sasamoto S., Watanabe A., Ono A., Kawashima K., Fujishiro T., Katoh M.,
RA Kohara M., Kishida Y., Minami C., Nakayama S., Nakazaki N., Shimizu Y.,
RA Shinpo S., Takahashi C., Wada T., Yamada M., Ohmido N., Hayashi M.,
RA Fukui K., Baba T., Nakamichi T., Mori H., Tabata S.;
RT "Genome structure of the legume, Lotus japonicus.";
RL DNA Res. 15:227-239(2008).
RN [2]
RP SUBCELLULAR LOCATION, 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:0000269|PubMed:24920445};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24920445}. Note=Very
CC restricted localization following a belt shape within the plasma
CC membrane which coincides with the position of the Casparian strip
CC membrane domain in the root endodermis.
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
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DR EMBL; AP004962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DKC2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..186
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000422082"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 186 AA; 20350 MW; D5A1526171907F0A CRC64;
MKSSPAELIS EAKSSTQNSK MKRAVSVLDF ILRLIAVVAT LASAIAMGTT DESLPFFTQF
IRFRAEYDDL PTLRLFVVAS AFASGYLILS LPLSILHITR SSARRTRVIL IILDMVMLTS
LTAASSAAAA IVYLAHKGNA KANWFAFCQQ YDSFCERISG SLIGSFIAIP LFIMLILFSA
LVLSKR