CSPLJ_ARALL
ID CSPLJ_ARALL Reviewed; 297 AA.
AC D7MMW4;
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 4A2;
DE Short=AlCASPL4A2;
GN ORFNames=ARALYDRAFT_919556;
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; EFH42770.1; -; Genomic_DNA.
DR RefSeq; XP_002866511.1; XM_002866465.1.
DR AlphaFoldDB; D7MMW4; -.
DR STRING; 59689.scaffold_802956.1; -.
DR EnsemblPlants; scaffold_802956.1; scaffold_802956.1; scaffold_802956.1.
DR GeneID; 9300896; -.
DR Gramene; scaffold_802956.1; scaffold_802956.1; scaffold_802956.1.
DR KEGG; aly:9300896; -.
DR eggNOG; ENOG502QW75; Eukaryota.
DR HOGENOM; CLU_048961_2_0_1; -.
DR OrthoDB; 1502083at2759; -.
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..297
FT /note="CASP-like protein 4A2"
FT /id="PRO_0000417759"
FT TOPO_DOM 1..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 32766 MW; 4E0ACF247AF8E249 CRC64;
MKMKRTVSSN SEAYSYNESP HSPLRFHSPL SDAGDLPESR YVSPEGSPFK IENPKSIVAG
NKLTQFSPLP SPIPPPPPQI PPPRRQRNAR VPMNSSLDKS PSSMVVQNSW VREDGQQNTT
RKAGAPMNGE ESATTAVNRA RRDDLVSVTA LGFRITEVIL CVISFSIMAA DKTQGWSGDS
YDRYKEYRYC LAVNVIAFVY SAFEACDAAC YMAKESYMMN CGFHDLFVFS MDQLLAYLLM
SASSCAATRV DDWVSNWGKD EFTQMATASI AVSFLAFGAF AVSALISSYR LFTHASS