CASP1_ARALL
ID CASP1_ARALL Reviewed; 203 AA.
AC D7LIN7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=AlCASP1;
GN ORFNames=ARALYDRAFT_482586;
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 -!- FUNCTION: Regulates membrane-cell wall junctions and localized cell
CC wall deposition. Required for establishment of the Casparian strip
CC membrane domain (CSD) and the subsequent formation of Casparian strips,
CC a cell wall modification of the root endodermis that determines an
CC apoplastic barrier between the intraorganismal apoplasm and the
CC extraorganismal apoplasm and prevents lateral diffusion (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Very restricted localization following a
CC belt shape within the plasma membrane which coincides with the position
CC of the Casparian strip membrane domain in the root endodermis.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
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DR EMBL; GL348716; EFH57686.1; -; Genomic_DNA.
DR RefSeq; XP_002881427.1; XM_002881381.1.
DR AlphaFoldDB; D7LIN7; -.
DR SMR; D7LIN7; -.
DR STRING; 81972.D7LIN7; -.
DR EnsemblPlants; fgenesh2_kg.4__1646__AT2G36100.1; fgenesh2_kg.4__1646__AT2G36100.1; fgenesh2_kg.4__1646__AT2G36100.1.
DR GeneID; 9315659; -.
DR Gramene; fgenesh2_kg.4__1646__AT2G36100.1; fgenesh2_kg.4__1646__AT2G36100.1; fgenesh2_kg.4__1646__AT2G36100.1.
DR KEGG; aly:9315659; -.
DR eggNOG; ENOG502R7BC; Eukaryota.
DR HOGENOM; CLU_066104_3_1_1; -.
DR OrthoDB; 1230007at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0048226; C:Casparian strip; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0042545; P:cell wall modification; IEA:EnsemblPlants.
DR GO; GO:0007043; P:cell-cell junction assembly; IEA:EnsemblPlants.
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; Cell wall biogenesis/degradation; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SQU2"
FT CHAIN 2..203
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000411995"
FT TOPO_DOM 2..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9SQU2"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 203 AA; 21499 MW; 87F7467510249B67 CRC64;
MAKESTTIDV GEPSTVTKSS SHVVKKKGFV AAAAGGGAKR GLAIFDFLLR LAAIGVTIGA
ASVMYTAQET LPFFTQFLQF QAGYDDLPAF QYFVIAVAIV ASYLVLSLPF SIVTIVRPLA
VAPRLILLIF DTLVVTLNTS AAAAAASIVY LAHNGNQSTN WLPICQQFGD FCQNVSTAVV
AASIAILFFI VLIIISAIAL KRH
