CASP1_ARATH
ID CASP1_ARATH Reviewed; 206 AA.
AC Q9SIH4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=AtCASP1;
GN Name=CASP1; OrderedLocusNames=At2g36100; ORFNames=F9C22.3;
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;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DIMERIZATION, AND
RP INTERACTION WITH CASP2; CASP3; CASP4 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 [6]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 72-GLU--PHE-80; 73-THR--GLN-79; 74-LEU--THR-78; ASP-134; GLY-158;
RP 158-GLY--CYS-175; TRP-164; CYS-168; GLN-170; PHE-174 AND CYS-175.
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 CASP2, CASP3, CASP4 and CASP5. {ECO:0000269|PubMed:21593871}.
CC -!- INTERACTION:
CC Q9SIH4; Q9ZQI2: CASP3; NbExp=2; IntAct=EBI-4451446, EBI-15927653;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21593871,
CC ECO:0000269|PubMed:24920445}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21593871, ECO:0000269|PubMed:24920445}. 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 -!- DISRUPTION PHENOTYPE: Disorganised deposition of Casparian strips.
CC {ECO:0000269|PubMed:21593871}.
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
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DR EMBL; AC007135; AAD26967.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09206.1; -; Genomic_DNA.
DR EMBL; BT003113; AAO24545.1; -; mRNA.
DR EMBL; AK228127; BAF00084.1; -; mRNA.
DR PIR; H84776; H84776.
DR RefSeq; NP_181154.1; NM_129169.3.
DR AlphaFoldDB; Q9SIH4; -.
DR BioGRID; 3527; 4.
DR DIP; DIP-59177N; -.
DR IntAct; Q9SIH4; 8.
DR STRING; 3702.AT2G36100.1; -.
DR iPTMnet; Q9SIH4; -.
DR PaxDb; Q9SIH4; -.
DR PRIDE; Q9SIH4; -.
DR ProteomicsDB; 222802; -.
DR EnsemblPlants; AT2G36100.1; AT2G36100.1; AT2G36100.
DR GeneID; 818183; -.
DR Gramene; AT2G36100.1; AT2G36100.1; AT2G36100.
DR KEGG; ath:AT2G36100; -.
DR Araport; AT2G36100; -.
DR TAIR; locus:2053514; AT2G36100.
DR eggNOG; ENOG502R7BC; Eukaryota.
DR HOGENOM; CLU_066104_3_1_1; -.
DR InParanoid; Q9SIH4; -.
DR OMA; MMELTIA; -.
DR OrthoDB; 1230007at2759; -.
DR PhylomeDB; Q9SIH4; -.
DR PRO; PR:Q9SIH4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIH4; baseline and differential.
DR Genevisible; Q9SIH4; 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; IDA: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 Acetylation; Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SQU2"
FT CHAIN 2..206
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000308659"
FT TOPO_DOM 2..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9SQU2"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 72..80
FT /note="Missing: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 73..79
FT /note="Missing: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 74..78
FT /note="Missing: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 134
FT /note="D->H: Not detectable probably due to an impaired
FT folding leading to instability."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 158..175
FT /note="Missing: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 158
FT /note="G->S: Abnormal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 164
FT /note="W->G: Abnormal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 168
FT /note="C->S: Abnormal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 170
FT /note="Q->E: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 174
FT /note="F->V: Abnormal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
FT MUTAGEN 175
FT /note="C->S: Abnormal subcellular localization."
FT /evidence="ECO:0000269|PubMed:24920445"
SQ SEQUENCE 206 AA; 21970 MW; E0BCBE459A96C771 CRC64;
MAKESTTIDV GEPSTVTKSS SHVVKDAKKK GFVAVASRGG AKRGLAIFDF LLRLAAIAVT
IGAASVMYTA EETLPFFTQF LQFQAGYDDL PAFQYFVIAV AVVASYLVLS LPFSIVSIVR
PHAVAPRLIL LICDTLVVTL NTSAAAAAAS ITYLAHNGNQ STNWLPICQQ FGDFCQNVST
AVVADSIAIL FFIVLIIISA IALKRH
