CASP4_ARATH
ID CASP4_ARATH Reviewed; 202 AA.
AC Q9FFZ7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Casparian strip membrane protein 4;
DE Short=AtCASP4;
GN Name=CASP4; OrderedLocusNames=At5g06200; ORFNames=MBL20.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DIMERIZATION, AND INTERACTION WITH CASP1;
RP CASP2; CASP3 AND CASP5.
RC STRAIN=cv. Columbia;
RX PubMed=21593871; DOI=10.1038/nature10070;
RA Roppolo D., De Rybel B., Denervaud Tendon V., Pfister A., Alassimone J.,
RA Vermeer J.E.M., Yamazaki M., Stierhof Y.-D., Beeckman T., Geldner N.;
RT "A novel protein family directs Casparian strip formation in the
RT endodermis.";
RL Nature 473:380-383(2011).
RN [4]
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.
CC {ECO:0000269|PubMed:21593871}.
CC -!- SUBUNIT: Homodimer and heterodimers with other CASP proteins. Interacts
CC with CASP1, CASP2, CASP3 and CASP5. {ECO:0000269|PubMed:21593871}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21593871};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21593871}. Note=Very
CC restricted localization following a belt shape within the plasma
CC membrane which coincides with the position of the Casparian strip
CC membrane domain.
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
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DR EMBL; AP002544; BAB09685.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90983.1; -; Genomic_DNA.
DR RefSeq; NP_196238.1; NM_120702.2.
DR AlphaFoldDB; Q9FFZ7; -.
DR DIP; DIP-59180N; -.
DR IntAct; Q9FFZ7; 4.
DR STRING; 3702.AT5G06200.1; -.
DR PaxDb; Q9FFZ7; -.
DR PRIDE; Q9FFZ7; -.
DR ProteomicsDB; 223882; -.
DR EnsemblPlants; AT5G06200.1; AT5G06200.1; AT5G06200.
DR GeneID; 830507; -.
DR Gramene; AT5G06200.1; AT5G06200.1; AT5G06200.
DR KEGG; ath:AT5G06200; -.
DR Araport; AT5G06200; -.
DR TAIR; locus:2160747; AT5G06200.
DR eggNOG; ENOG502RYTF; Eukaryota.
DR HOGENOM; CLU_066104_3_1_1; -.
DR InParanoid; Q9FFZ7; -.
DR OMA; MFFVIGM; -.
DR OrthoDB; 1230007at2759; -.
DR PhylomeDB; Q9FFZ7; -.
DR PRO; PR:Q9FFZ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFZ7; baseline and differential.
DR Genevisible; Q9FFZ7; AT.
DR GO; GO:0048226; C:Casparian strip; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0042545; P:cell wall modification; IMP:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; IDA:UniProtKB.
DR InterPro; IPR006459; CASP/CASPL.
DR InterPro; IPR006702; CASP_dom.
DR Pfam; PF04535; DUF588; 1.
DR TIGRFAMs; TIGR01569; A_tha_TIGR01569; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..202
FT /note="Casparian strip membrane protein 4"
FT /id="PRO_0000308684"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 202 AA; 21112 MW; 488DA4E999CF0A0F CRC64;
MKSDSIAVDV PAESSSVIKG KAPLLGLARD HTGSGGYKRG LSIFDFLLRL AAIVAALAAA
ATMGTSDETL PFFTQFLQFE ASYDDLPTFQ FFVVAIAIVA GYLVLSLPFS VVTIVRPLAV
APRLLLLVLD TAALALDTAA ASAAAAIVYL AHNGNTNTNW LPICQQFGDF CQKTSGAVVS
AFASVTFLAI LVVISGVSLK RP
