ID   CSPL9_PICSI             Reviewed;         238 AA.
AC   B8LQF9;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=CASP-like protein 2BC2;
DE            Short=PsCASPL2BC2;
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=Bark;
RA   Ralph S.G., Chun H.E., Liao N., Ali J., Reid K., Kolosova N., Cooper N.,
RA   Cullis C., Jancsik S., Moore R., Mayo M., Wagner S., Holt R.A.,
RA   Jones S.J.M., Marra M.A., Ritland C.E., Ritland K., Bohlmann J.;
RT   "Full length cDNA sequences from Sitka Spruce (Picea sitchensis).";
RL   Submitted (JUN-2007) 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; EF678110; ABR17889.1; -; mRNA.
DR   AlphaFoldDB; B8LQF9; -.
DR   OMA; VMAYITV; -.
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..238
FT                   /note="CASP-like protein 2BC2"
FT                   /id="PRO_0000391521"
FT   TOPO_DOM        1..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   238 AA;  26637 MW;  F323C3003637E959 CRC64;
     MPSSTYPRRR FDEVFLVEIS SRILVTQEKH QQEEEEKKVR MAGKANVSVL MSEDASFHQK
     VAVEKRLKIG EVILRFAMIA LALVAAVRVG TDTQTRTIFT IEKKAKYSDM KALVFLVVMN
     GIVASYSLLQ GLRCVLSIYT QSPLTSKPLA WLIFALDQTM AYFSLAAAAA AAESAYLAER
     GQTEFQWMKV CIFYEKFCHQ IGEGLVSTFL VSLSMATVSG MSAYHLFRLY GSKGKSIQ