ID   CSPL5_PICSI             Reviewed;         201 AA.
AC   A9P0A6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=CASP-like protein 1U1;
DE            Short=PsCASPL1U1;
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].
RA   Ralph S.G., Kirkpatrick R., Chun H.J.E., Palmquist D., Wynhoven B.,
RA   Kolosova N., Cooper N., Oddy C., Jancsik S., Ritland C.E., Douglas C.J.,
RA   Butterfield Y.S.N., Liu J., Stott J., Yang G., Barber S., Holt R.A.,
RA   Siddiqui A., Jones S.J.M., Marra M.A., Ritland K., Bohlmann J.;
RT   "The spruce transcriptome: analysis of ca. 6,500 sequence-verified full-
RT   length cDNAs.";
RL   Submitted (OCT-2006) 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; EF087061; ABK26317.1; -; mRNA.
DR   AlphaFoldDB; A9P0A6; -.
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..201
FT                   /note="CASP-like protein 1U1"
FT                   /id="PRO_0000370318"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   201 AA;  21638 MW;  B708BF18FF4CDBA7 CRC64;
     MESRTKLDYS ETARSYTENK SGGNDAQRIN GVYSSSFFVV DFSLRLLVIG STFTAAIVMG
     TNKQTAILPI VGPLSAKYQY SPAFVFFVIA NAVACGYTLL SLIFSITGKF TSTPLSVFLL
     SVTDLVMVAL VSAGVSAAAA IAYVGYKGNS HTQWGKVCGI YDRFCHHGAG AIVASFVSLI
     IFMVLTVMST YSFYRRTSSA R