ID   CSPL3_PICSI             Reviewed;         180 AA.
AC   D5A972;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=CASP-like protein 2A3;
DE            Short=PsCASPL2A3;
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. FB3-425; TISSUE=Axillary bud;
RA   Reid K.E., Liao N., Chan S., Docking R., Taylor G., Moore R., Mayo M.,
RA   Munro S., King J., Yanchuk A., Holt R., Jones S., Marra M., Ritland C.E.,
RA   Ritland K., Bohlmann J.;
RT   "Full length sequence-verified cDNA sequences from Sitka spruce buds (Picea
RT   sitchensis).";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; BT122730; ADE76091.1; -; mRNA.
DR   AlphaFoldDB; D5A972; -.
DR   SMR; D5A972; -.
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   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..180
FT                   /note="CASP-like protein 2A3"
FT                   /id="PRO_0000412031"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..55
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..135
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   180 AA;  20233 MW;  CA657DE1A898342C CRC64;
     MELIYGSTMR KKWIEPALRF LPVGLCISAL ALMLKSKEGN ENGILEYKHV GAFRYLAYAN
     GICAAYSVLS TFNSVVPRSC SLSRAWFVFV FDQAFTYLML GAGAVVTEVL YLAYKGDEKI
     TWFEICPYYG RFCNRVAASL VISFLALLCF IPLSLISAYR VFSKYDPPSL CKKDQITSQS