CSPL8_PICSI
ID CSPL8_PICSI Reviewed; 185 AA.
AC A9NMM6;
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 2A1;
DE Short=PsCASPL2A1;
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; EF082530; ABK21887.1; -; mRNA.
DR AlphaFoldDB; A9NMM6; -.
DR OMA; HHKTSHG; -.
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..185
FT /note="CASP-like protein 2A1"
FT /id="PRO_0000370321"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 185 AA; 20456 MW; 33A60413D75068A0 CRC64;
MGTDSNSGHL LQAKRFELLF RVTPLALCIA AMAIMLKNKQ SNQYGALHYS DVGGFKYLVY
ANGICAIYSI LSLLGSVLST GIDYSWTRAW IMFILDQALT YLILTAGVCG VEIMDLAYQG
NEQVSWSRVC VSYGKFCNDA RASVLITMAV LVCFMVLSLL SAHRLFSKYE APIVNNGHHT
DFSQN