CASP4_ORYSJ
ID CASP4_ORYSJ Reviewed; 201 AA.
AC Q6Z2U5; A0A0N7KG31;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Casparian strip membrane protein 4;
DE Short=OsCASP4;
GN OrderedLocusNames=Os02g0743900, LOC_Os02g51010; ORFNames=OJ1734_E02.23;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD16116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005297; BAD16116.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS80881.1; -; Genomic_DNA.
DR RefSeq; XP_015624545.1; XM_015769059.1.
DR AlphaFoldDB; Q6Z2U5; -.
DR STRING; 4530.OS02T0743900-00; -.
DR PaxDb; Q6Z2U5; -.
DR PRIDE; Q6Z2U5; -.
DR EnsemblPlants; Os02t0743900-00; Os02t0743900-00; Os02g0743900.
DR GeneID; 107275435; -.
DR Gramene; Os02t0743900-00; Os02t0743900-00; Os02g0743900.
DR KEGG; osa:107275435; -.
DR eggNOG; ENOG502RXTK; Eukaryota.
DR HOGENOM; CLU_066104_3_2_1; -.
DR InParanoid; Q6Z2U5; -.
DR OMA; ANWFAVC; -.
DR OrthoDB; 1392215at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6Z2U5; OS.
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 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..201
FT /note="Casparian strip membrane protein 4"
FT /id="PRO_0000370292"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 201 AA; 21106 MW; EA555A61C0D8468B CRC64;
MEGKAAVTTS TEHGDGEASR TAARTVVSGS SRGGAASRAL SVADLILRVV AVVAIVDSAI
AMGTTNQTLP FFTQFLRFKA QYSDLPTLTL FVVANSAVTA YLVLSIPLSV VHIIRSRASY
SRLVLIFLDS VMLALVAAVA SASAAIVYLA HKGNVRANWF AVCQQFDSFC ERISGPLIGS
FAAMAVLLLL VLLSAAALAR R
