CASP1_POPTR
ID CASP1_POPTR Reviewed; 199 AA.
AC B9HBX2;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Casparian strip membrane protein 1;
DE Short=PtCASP1;
GN ORFNames=POPTRDRAFT_763057;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nisqually;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S.,
RA Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S.,
RA Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M.,
RA Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B.,
RA Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D.,
RA Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J.,
RA Tuskan G., Rokhsar D.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CM009295; EEE92938.1; -; Genomic_DNA.
DR RefSeq; XP_002309415.1; XM_002309379.1.
DR AlphaFoldDB; B9HBX2; -.
DR STRING; 3694.POPTR_0006s22510.1; -.
DR EnsemblPlants; PNT32796; PNT32796; POPTR_006G208800v3.
DR GeneID; 7492240; -.
DR Gramene; PNT32796; PNT32796; POPTR_006G208800v3.
DR KEGG; pop:7492240; -.
DR eggNOG; ENOG502RJHP; Eukaryota.
DR HOGENOM; CLU_066104_3_1_1; -.
DR InParanoid; B9HBX2; -.
DR OMA; MPRRTHH; -.
DR Proteomes; UP000006729; Chromosome 6.
DR ExpressionAtlas; B9HBX2; differential.
DR GO; GO:0048226; C:Casparian strip; IBA:GO_Central.
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:0042545; P:cell wall modification; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
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; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..199
FT /note="Casparian strip membrane protein 1"
FT /id="PRO_0000391535"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 199 AA; 21101 MW; 30C8A885041C6778 CRC64;
MKSESAAIDI PESSSVAKGK APLIAVSRNE KGGYRKGIAI FDFILRLAAI ATALAAAAAM
GTSDETLPFF TQFFQFQASY DDLPTFQFFV IAIAIVGGYL VLSLPFSIVA IVRPHAVGPR
LLLIILDAVA LTLNTAAGAA AAAIVYLAHN GNSNTNWLAI CQQYGDFCQK VSGAVVASFI
TVVIFVFLIV LSAFALRRH