ID   CASP1_SOYBN             Reviewed;         195 AA.
AC   C6T2E7;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Casparian strip membrane protein 1;
DE            Short=GmCASP1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL   Submitted (AUG-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   -!- 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; BT091606; ACU15802.1; -; mRNA.
DR   RefSeq; NP_001237549.1; NM_001250620.2.
DR   AlphaFoldDB; C6T2E7; -.
DR   STRING; 3847.GLYMA02G36170.1; -.
DR   PRIDE; C6T2E7; -.
DR   EnsemblPlants; KRH72259; KRH72259; GLYMA_02G201100.
DR   GeneID; 100500661; -.
DR   Gramene; KRH72259; KRH72259; GLYMA_02G201100.
DR   KEGG; gmx:100500661; -.
DR   eggNOG; ENOG502QZV7; Eukaryota.
DR   HOGENOM; CLU_066104_3_1_1; -.
DR   InParanoid; C6T2E7; -.
DR   OMA; KANWIAI; -.
DR   OrthoDB; 1230007at2759; -.
DR   Proteomes; UP000008827; Chromosome 2.
DR   GO; GO:0048226; C:Casparian strip; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0042545; P:cell wall modification; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
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; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..195
FT                   /note="Casparian strip membrane protein 1"
FT                   /id="PRO_0000391523"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..116
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..195
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   195 AA;  20399 MW;  829DB5F16CFC4E31 CRC64;
     MSTTIEIPES SKVAKGKAVA VVAPARPGGW KKGVAIMDFI LRLGAIAAAL GAAATMGTSD
     QTLPFFTQFF QFEASYDSFT TFQFFVITMS LVGGYLVLSL PFSIVAIVRP HAVGPRLFLI
     ILDTAFLTLA TAGGASAAAI VYLAHNGDQD TNWLAICNQF GDFCAQTSAA VVSSFVAVVV
     LVLLIIMSAL AIGKP