CSPLI_ARALL
ID CSPLI_ARALL Reviewed; 276 AA.
AC D7LIR2;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=CASP-like protein 4A3;
DE Short=AlCASPL4A3;
GN ORFNames=ARALYDRAFT_482607;
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; GL348716; EFH55863.1; -; Genomic_DNA.
DR RefSeq; XP_002879604.1; XM_002879558.1.
DR AlphaFoldDB; D7LIR2; -.
DR STRING; 81972.D7LIR2; -.
DR EnsemblPlants; fgenesh2_kg.4__1667__AT2G36330.1; fgenesh2_kg.4__1667__AT2G36330.1; fgenesh2_kg.4__1667__AT2G36330.1.
DR Gramene; fgenesh2_kg.4__1667__AT2G36330.1; fgenesh2_kg.4__1667__AT2G36330.1; fgenesh2_kg.4__1667__AT2G36330.1.
DR eggNOG; ENOG502QW75; Eukaryota.
DR HOGENOM; CLU_048961_2_0_1; -.
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; IPR006702; CASP_dom.
DR Pfam; PF04535; DUF588; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..276
FT /note="CASP-like protein 4A3"
FT /id="PRO_0000417758"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 30743 MW; E682AEE0597B77DC CRC64;
MPSMSPSSIS TEKSPPPSDT SMAIVAFDNS TTHLSSSPSP PHSLDHSSDS EKEDEKRRPE
SRRNKNPVKI EETPSPIVVV HNHNRSVKEV VPTRKTARVG SGRSSGQRSG AVLAILRRSR
REEIVKFVAL GFRLSEVVLA LISFSIMAAD KTKGWSGDSF DRYKEYRFCL SVNVVAFIYA
SFQACDLAYH LVKEKHLISH HLRPLFEFII DQVLAYLLMC ASTAAVTRVD DWVSNWGKDD
FTEMASASIA MSFLTFLAFA FSSLISGYNL FNQDSL