ID   CASP3_LOTJA             Reviewed;         219 AA.
AC   P0DI56; I3SGF9; I3T6S5;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Casparian strip membrane protein 3;
DE            Short=LjCASP3;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Gifu; TISSUE=Cotyledon, Root, and Shoot;
RA   Chan A.P., Cheung F., Xiao Y., Town C.D.;
RT   "Construction and analysis of normalized cDNA library from stressed or
RT   untreated aerial and underground tissues of Lotus japonicus.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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; GO006025; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BT139556; AFK39351.1; -; mRNA.
DR   EMBL; BT148423; AFK48217.1; -; mRNA.
DR   AlphaFoldDB; P0DI56; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR006459; CASP/CASPL.
DR   InterPro; IPR006702; CASP_dom.
DR   Pfam; PF04535; DUF588; 1.
DR   TIGRFAMs; TIGR01569; A_tha_TIGR01569; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..219
FT                   /note="Casparian strip membrane protein 3"
FT                   /id="PRO_0000417775"
FT   TOPO_DOM        1..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        130
FT                   /note="C -> F (in Ref. 2; AFK48217)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   219 AA;  23140 MW;  C54DA73F38592906 CRC64;
     MDPGREDEVP LAATSPESRR TRSNGRGKAT VGDAPPPAET VVSTKAAPLP TGGWKKGIAI
     LDFILRLGAI GAAMGASILM GTNEQILPFF TQFLQFHAQW DDFPVFKLFV VLNALAGGFL
     ILSLPLSIVC IVRPLAVGPR FLLLITDLVN MATVIAAASA AAAIVYVAHN GSQDANWIAI
     CQQFTDFCQG TSEAVVVSFV AAVFLVCLIV VSTLALKRT