CASP2_WHEAT
ID CASP2_WHEAT Reviewed; 183 AA.
AC P0DI42;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Casparian strip membrane protein 2;
DE Short=TaCASP2;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. DT4B(CS); TISSUE=Anther;
RX PubMed=16832693; DOI=10.1007/s00438-006-0120-1;
RA Mochida K., Kawaura K., Shimosaka E., Kawakami N., Shin-I T., Kohara Y.,
RA Yamazaki Y., Ogihara Y.;
RT "Tissue expression map of a large number of expressed sequence tags and its
RT application to in silico screening of stress response genes in common
RT wheat.";
RL Mol. Genet. Genomics 276:304-312(2006).
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; CJ652718; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DI42; -.
DR STRING; 4565.Traes_7AS_8EB52BB31.1; -.
DR PRIDE; P0DI42; -.
DR EnsemblPlants; TraesCAD_scaffold_094216_01G000100.1; TraesCAD_scaffold_094216_01G000100.1; TraesCAD_scaffold_094216_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_087687_01G000100.1; TraesCLE_scaffold_087687_01G000100.1; TraesCLE_scaffold_087687_01G000100.
DR EnsemblPlants; TraesCS7D02G190400.1; TraesCS7D02G190400.1; TraesCS7D02G190400.
DR EnsemblPlants; TraesPAR_scaffold_081738_01G000200.1; TraesPAR_scaffold_081738_01G000200.1; TraesPAR_scaffold_081738_01G000200.
DR EnsemblPlants; TraesROB_scaffold_090130_01G000100.1; TraesROB_scaffold_090130_01G000100.1; TraesROB_scaffold_090130_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_103525_01G000100.1; TraesWEE_scaffold_103525_01G000100.1; TraesWEE_scaffold_103525_01G000100.
DR Gramene; TraesCAD_scaffold_094216_01G000100.1; TraesCAD_scaffold_094216_01G000100.1; TraesCAD_scaffold_094216_01G000100.
DR Gramene; TraesCLE_scaffold_087687_01G000100.1; TraesCLE_scaffold_087687_01G000100.1; TraesCLE_scaffold_087687_01G000100.
DR Gramene; TraesCS7D02G190400.1; TraesCS7D02G190400.1; TraesCS7D02G190400.
DR Gramene; TraesPAR_scaffold_081738_01G000200.1; TraesPAR_scaffold_081738_01G000200.1; TraesPAR_scaffold_081738_01G000200.
DR Gramene; TraesROB_scaffold_090130_01G000100.1; TraesROB_scaffold_090130_01G000100.1; TraesROB_scaffold_090130_01G000100.
DR Gramene; TraesWEE_scaffold_103525_01G000100.1; TraesWEE_scaffold_103525_01G000100.1; TraesWEE_scaffold_103525_01G000100.
DR eggNOG; ENOG502RXTK; Eukaryota.
DR OMA; ANSIVCA; -.
DR Proteomes; UP000019116; Unplaced.
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: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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..183
FT /note="Casparian strip membrane protein 2"
FT /id="PRO_0000417817"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 183 AA; 19430 MW; 4134FDB11321C2F0 CRC64;
MDSGEQGETS KAPLNKGVSR GVSILDLILR VIAVISTLAS AIAMGTTNET LPLFTPFIQF
KARYSDLPAL TFFVVANSIV SAYLILSLPL SIAHIIRSGA KYSRLVLIIF DAAMLALVTA
ASSAATAIVY LAHKGNVRAN WLAICQQLDS FCERTSGSLV GSFGAMVLLI LLILLSAMAL
ARR
