CSPLC_ARALL
ID CSPLC_ARALL Reviewed; 197 AA.
AC D7MFJ8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=CASP-like protein 1B2;
DE Short=AlCASPL1B2;
GN ORFNames=ARALYDRAFT_492822;
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; GL348719; EFH46192.1; -; Genomic_DNA.
DR RefSeq; XP_002869933.1; XM_002869887.1.
DR AlphaFoldDB; D7MFJ8; -.
DR STRING; 81972.D7MFJ8; -.
DR EnsemblPlants; fgenesh2_kg.7__2255__AT4G20390.1; fgenesh2_kg.7__2255__AT4G20390.1; fgenesh2_kg.7__2255__AT4G20390.1.
DR Gramene; fgenesh2_kg.7__2255__AT4G20390.1; fgenesh2_kg.7__2255__AT4G20390.1; fgenesh2_kg.7__2255__AT4G20390.1.
DR eggNOG; ENOG502RYH6; Eukaryota.
DR HOGENOM; CLU_066104_1_0_1; -.
DR OrthoDB; 1282932at2759; -.
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 Acetylation; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SQU2"
FT CHAIN 2..197
FT /note="CASP-like protein 1B2"
FT /id="PRO_0000412011"
FT TOPO_DOM 2..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9SQU2"
SQ SEQUENCE 197 AA; 21071 MW; C4844C72603425E8 CRC64;
MAREKIVVAG GSTKSWKLLL GLRVFAFMAT LAAAIVMSLN KETKTLVVAT IGTLPIKATL
TAKFQDTPAF VFFVIANVMV SFHNLLMIVL QIFSRKLEYK GVRLLSIAIL DMLNATLVSA
AANAAVFVAE LGKNGNKHAK WNKVCDRFAT YCDHGAGALI AAFAGVILML LVSSVSISRL
LINSKHLSTT ATTTAVV