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CSPL1_PINCO
ID   CSPL1_PINCO             Reviewed;         185 AA.
AC   P0DI64;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=CASP-like protein 5A1;
DE            Short=PcCASPL5A1;
OS   Pinus contorta (Shore pine) (Lodgepole pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Xylem;
RA   Keeling C.I., Henderson H., Li M., Liao N., Docking R., Chan S., Taylor G.,
RA   Moore R., Munro S., Mayo M., Jefferson K., Lee H.W., Leung A., Thorne K.,
RA   Trinh E., Matsuo C., Chand S., Brown-John M., McMurtrie H., Cruz K.,
RA   Smith J., Holt R., Jones S., Marra M., Cooke J.E.K., Bohlmann J.;
RT   "Expressed sequence tags from the lodgepole pine, Pinus contorta.";
RL   Submitted (OCT-2009) 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; GT265686; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DI64; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006702; CASP_dom.
DR   InterPro; IPR045009; CASPL-5.
DR   PANTHER; PTHR32021; PTHR32021; 1.
DR   Pfam; PF04535; DUF588; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..185
FT                   /note="CASP-like protein 5A1"
FT                   /id="PRO_0000418683"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..76
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..160
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   185 AA;  19853 MW;  75659107BA5C5907 CRC64;
     MNVSHPAVHP VGVPPALGGQ AVPPRMRMRV RMEYLVFQGM PLPGSLGGLM LRLGQFCSAL
     IAFSVMVSIR DFSVTAFCYL LAATVLQCLW SLALAVIDVY ALLVKRSLRN PLLVSIFVVG
     DGVTATLTFA AACASAGVVV LIGNDISMCK SNPCANYEAA IIMAFLSWFM VSISFVLTFW
     MLATL
 
 
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