CASP3_ARATH
ID CASP3_ARATH Reviewed; 221 AA.
AC Q9ZQI2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Casparian strip membrane protein 3;
DE Short=AtCASP3;
GN Name=CASP3; OrderedLocusNames=At2g27370; ORFNames=F10A12.5, F12K2.5;
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 CASP1; CASP2; 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, 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, CASP4 and CASP5. {ECO:0000269|PubMed:21593871}.
CC -!- INTERACTION:
CC Q9ZQI2; Q9SIH4: CASP1; NbExp=2; IntAct=EBI-15927653, EBI-4451446;
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 -!- 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; AC006232; AAM15182.1; -; Genomic_DNA.
DR EMBL; AC006233; AAD41993.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07986.1; -; Genomic_DNA.
DR EMBL; BT003063; AAO23628.1; -; mRNA.
DR EMBL; AK227595; BAE99586.1; -; mRNA.
DR PIR; B84672; B84672.
DR RefSeq; NP_180305.1; NM_128296.4.
DR AlphaFoldDB; Q9ZQI2; -.
DR DIP; DIP-59179N; -.
DR IntAct; Q9ZQI2; 4.
DR STRING; 3702.AT2G27370.1; -.
DR iPTMnet; Q9ZQI2; -.
DR PaxDb; Q9ZQI2; -.
DR PRIDE; Q9ZQI2; -.
DR ProteomicsDB; 223910; -.
DR EnsemblPlants; AT2G27370.1; AT2G27370.1; AT2G27370.
DR GeneID; 817280; -.
DR Gramene; AT2G27370.1; AT2G27370.1; AT2G27370.
DR KEGG; ath:AT2G27370; -.
DR Araport; AT2G27370; -.
DR TAIR; locus:2038638; AT2G27370.
DR eggNOG; ENOG502RXQU; Eukaryota.
DR HOGENOM; CLU_066104_3_1_1; -.
DR InParanoid; Q9ZQI2; -.
DR OMA; IMDKHKQ; -.
DR OrthoDB; 1230007at2759; -.
DR PhylomeDB; Q9ZQI2; -.
DR PRO; PR:Q9ZQI2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQI2; baseline and differential.
DR Genevisible; Q9ZQI2; 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 GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS: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; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="Casparian strip membrane protein 3"
FT /id="PRO_0000308656"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 221 AA; 24161 MW; 456B6F1F7A25E4C4 CRC64;
MDIEKAGSRR EEEEPIVQRP KLDKGKGKAH VFAPPMNYNR IMDKHKQEKM SPAGWKRGVA
IFDFVLRLIA AITAMAAAAK MATTEETLPF FTQFLQFQAD YTDLPTMSSF VIVNSIVGGY
LTLSLPFSIV CILRPLAVPP RLFLILCDTV MMGLTLMAAS ASAAIVYLAH NGNSSSNWLP
VCQQFGDFCQ GTSGAVVASF IAATLLMFLV ILSAFALKRT T
