CSPL2_PICSI
ID CSPL2_PICSI Reviewed; 150 AA.
AC A9NTU2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=CASP-like protein 2;
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;
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF084742; ABK24053.1; -; mRNA.
DR AlphaFoldDB; A9NTU2; -.
DR OMA; HADWFSI; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
DR InterPro; IPR006459; CASP/CASPL.
DR InterPro; IPR006702; CASP_dom.
DR InterPro; IPR000682; PCMT.
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..150
FT /note="CASP-like protein 2"
FT /id="PRO_0000412030"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 150 AA; 16038 MW; 9291399C73AF1015 CRC64;
MKPEAGDGRS GWRWVATFDL ILRLAAIVAT STAVLAAMGK TFVVVVNGVA CFYLLMSLPV
SIFNIMRPGA CPANRAVLTA LDMVTVALVT AGALVAGILY LVHKAGDTHA DWFSIWSQLD
SLSYLAVLAL ILHVLLSGSI LYKQALNIMF