CSPL6_PICSI
ID CSPL6_PICSI Reviewed; 196 AA.
AC A9P1V1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=CASP-like protein 2A2;
DE Short=PsCASPL2A2;
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;
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; EF087625; ABK26862.1; -; mRNA.
DR AlphaFoldDB; A9P1V1; -.
DR SMR; A9P1V1; -.
DR OMA; NGVCAGY; -.
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..196
FT /note="CASP-like protein 2A2"
FT /id="PRO_0000370319"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..68
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 196 AA; 21493 MW; DD29ABA3F3932952 CRC64;
MAQGKESVSV VEMEGSGNGP AVEMRHFETL FRLLPVGLCI SALVLMLKSE QSDQYMQLDY
SNVDAFRCLA YANGICAGYS LISAFDSMVP VSHHISRSWI LFLLDQGITY LMLAGGAVAT
QVLYVAYKGD EKATWEQICG SYGRFCNRAG ASVIISFFAL VCFLLLSLLS AYRLFSKYDP
PIHGGAKLED QTTAQI