ID   CASP1_PINTA             Reviewed;         190 AA.
AC   P0DH80;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Casparian strip membrane protein 1;
DE            Short=PtCASP1;
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Root;
RA   Pratt L., Cordonnier-Pratt M.-M., Lorenz W.W., Zimmermann C., Dean J.F.D.;
RT   "An EST database from nitrogen-deficient loblolly pine (Pinus taeda)
RT   roots.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-190.
RC   TISSUE=Root;
RA   Pratt L., Cordonnier-Pratt M.-M., Lorenz W.W., Zimmermann C., Dean J.F.D.;
RT   "An EST database from untreated loblolly pine (Pinus taeda) roots.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   -!- FUNCTION: Regulates membrane-cell wall junctions and localized cell
CC       wall deposition. Required for establishment of the Casparian strip
CC       membrane domain (CSD) and the subsequent formation of Casparian strips,
CC       a cell wall modification of the root endodermis that determines an
CC       apoplastic barrier between the intraorganismal apoplasm and the
CC       extraorganismal apoplasm and prevents lateral diffusion (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Very restricted localization following a
CC       belt shape within the plasma membrane which coincides with the position
CC       of the Casparian strip membrane domain in the root endodermis.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC       family. {ECO:0000305}.
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DR   EMBL; DR057783; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CF667267; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CF667350; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DH80; -.
DR   SMR; P0DH80; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; Cell wall biogenesis/degradation; Glycoprotein; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..190
FT                   /note="Casparian strip membrane protein 1"
FT                   /id="PRO_0000412208"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..190
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        14..15
FT                   /note="LP -> VF (in Ref. 2; CF667350)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="D -> E (in Ref. 2; CF667267/CF667350)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20690 MW;  86DA624F7D9F0990 CRC64;
     MKAESGSADA KLPLPPPVGR KRRGLAILDF LLRLLAIGAT LSAAIAMGTN NETLKFFTQF
     FQFNARFYNL SAFIYFVIAN ATVGLYLLLS LPFSIFDIVR PRAAAFRVLL IFFDTVMVAV
     CTSGAAAATA IMYVARRGNT KTNWFSICQQ FNSFCDQATG ALGASFAAVV LLILLVLLSA
     STLHRQRADF