CSPL2_ARALL
ID CSPL2_ARALL Reviewed; 193 AA.
AC D7MUY4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=CASP-like protein 2D1;
DE Short=AlCASPL2D1;
GN ORFNames=ARALYDRAFT_495581;
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; GL348720; EFH40626.1; -; Genomic_DNA.
DR RefSeq; XP_002864367.1; XM_002864321.1.
DR AlphaFoldDB; D7MUY4; -.
DR PRIDE; D7MUY4; -.
DR EnsemblPlants; fgenesh2_kg.8__1397__AT5G54980.1; fgenesh2_kg.8__1397__AT5G54980.1; fgenesh2_kg.8__1397__AT5G54980.1.
DR GeneID; 9300443; -.
DR Gramene; fgenesh2_kg.8__1397__AT5G54980.1; fgenesh2_kg.8__1397__AT5G54980.1; fgenesh2_kg.8__1397__AT5G54980.1.
DR KEGG; aly:9300443; -.
DR eggNOG; ENOG502RY7Y; Eukaryota.
DR HOGENOM; CLU_066104_2_2_1; -.
DR OrthoDB; 1252134at2759; -.
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..193
FT /note="CASP-like protein 2D1"
FT /id="PRO_0000412001"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..73
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..151
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 193 AA; 21528 MW; 055607AD6F6EAEAE CRC64;
MRANNNNTRE EERSSSSKQQ QPQAHMSLKI IDSCLRLSVV PLSVATIWLT VTNHESNPDY
GNLDYNSIMG LKYMVGVSAI SAIYALLSTI SLWVTCLVSK AWLFFVPDQV LAYVMTTSVA
GATEIVYLLN KGDKIVTWSE MCSSYPHYCS KLTIALGLHV FVLFFFLFLS VISAYRAFSP
FDPPCDSQTN IDA