ID   CASP3_VIGUN             Reviewed;         224 AA.
AC   P0DI41;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Casparian strip membrane protein 3;
DE            Short=VuCASP3;
OS   Vigna unguiculata (Cowpea).
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; Vigna.
OX   NCBI_TaxID=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Root;
RA   Hearne S.J., Bishop R., Town C.D., Moskal W.A. Jr., Zhuang J.,
RA   Viswanathan L.D., Kriga Y., Shatsman S., Shetty J., Ferguson M.E.,
RA   Hanson J.;
RT   "ESTs from drought stressed and non-stressed leaves, stem meristem and
RT   roots of drought tolerant and drought sensitive cowpea (Vigna
RT   unguiculata).";
RL   Submitted (APR-2008) 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; FF389098; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DI41; -.
DR   PRIDE; P0DI41; -.
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..224
FT                   /note="Casparian strip membrane protein 3"
FT                   /id="PRO_0000417816"
FT   TOPO_DOM        1..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        213..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   224 AA;  24020 MW;  5DAE94B63E816F31 CRC64;
     MESKKEGVAS APTSPESRRT RSNGKGKTIA EATPPSVTVV STKVTPSPRG GWRKGAAILD
     FILRLGAISS AIGAAAVMGN NEQILPFFTQ FFQFHVQWDD FPMFQFFVFA NGAAVVFLIL
     SLPFSIVCIV RPFAVGPRLL LVIVDIFAMA LVIAAASAAA AVVYLAHNGS QDANWIAICQ
     QYTDFCQVTS QAVVASFVAA VFLICLIVLS SVALKKGLKR EFGW