CSPLD_ARALL
ID CSPLD_ARALL Reviewed; 200 AA.
AC D7L5G6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=CASP-like protein 1D2;
DE Short=AlCASPL1D2;
GN ORFNames=ARALYDRAFT_477942;
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47;
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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 -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
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DR EMBL; GL348715; EFH60835.1; -; Genomic_DNA.
DR RefSeq; XP_002884576.1; XM_002884530.1.
DR AlphaFoldDB; D7L5G6; -.
DR STRING; 59689.fgenesh2_kg.3__643__AT3G06390.1; -.
DR EnsemblPlants; fgenesh2_kg.3__643__AT3G06390.1; fgenesh2_kg.3__643__AT3G06390.1; fgenesh2_kg.3__643__AT3G06390.1.
DR Gramene; fgenesh2_kg.3__643__AT3G06390.1; fgenesh2_kg.3__643__AT3G06390.1; fgenesh2_kg.3__643__AT3G06390.1.
DR eggNOG; ENOG502S2UF; Eukaryota.
DR HOGENOM; CLU_066104_1_2_1; -.
DR OrthoDB; 1495110at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..200
FT /note="CASP-like protein 1D2"
FT /id="PRO_0000412012"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 21191 MW; 042D001D1682F49F CRC64;
MASTENPDPE TGKSEPIPAS ATTPPPSAAS FLDCRKIDVI IRVLLFSATL TALIVMVTSD
QTEKTQLPGV SSPAPVSAEF NDSPAFIFFV VALVVTSFYA LMSTLVSISL LLKPEFTARV
SVYLASLDMV MLGILASATG TAGGVAYIAL KGNKEVGWNK ICNVYDKFCR YIATSLALSL
FATLLLLVLS ICSALSKRTP