ID   CASP3_VITVI             Reviewed;         186 AA.
AC   A7PMY7; F6H5U8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Casparian strip membrane protein 3;
DE            Short=VvCASP3;
GN   OrderedLocusNames=VIT_14s0108g01050;
GN   ORFNames=GSVIVT00020996001, GSVIVT01011443001, VIT_00011443001,
GN   Vv14s0108g01050;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024;
RX   PubMed=17721507; DOI=10.1038/nature06148;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCB47569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FN597038; CCB47569.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A7PMY7; -.
DR   SMR; A7PMY7; -.
DR   EnsemblPlants; Vitvi14g03091_t001; Vitvi14g03091_P001; Vitvi14g03091.
DR   Gramene; Vitvi14g03091_t001; Vitvi14g03091_P001; Vitvi14g03091.
DR   eggNOG; KOG4197; Eukaryota.
DR   HOGENOM; CLU_002706_7_1_1; -.
DR   InParanoid; A7PMY7; -.
DR   OMA; KANWFAF; -.
DR   OrthoDB; 1392215at2759; -.
DR   Proteomes; UP000009183; Chromosome 14.
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   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..186
FT                   /note="Casparian strip membrane protein 3"
FT                   /id="PRO_0000370304"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..74
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..161
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   186 AA;  19875 MW;  E4D2D026865DA15D CRC64;
     MKAGALELGE GSKTSIPRGG VNRGISILDF ILRLITIIGT LGSAIAMGTT NETLPFFTQF
     TQFRAEYDDL PTFTFFVIAN SIVSGYLVLS LPMSILHIVR SGARASRIVL IFFDTAMLAL
     LTAAASAASA IVYLAHKGNA QANWFAICQQ FKSFCERISG SLIGSFGGII LFILLVLLSA
     VALSRC