ID   CASP1_CUCME             Reviewed;         209 AA.
AC   P0DI61;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Casparian strip membrane protein 1;
DE            Short=CmCASP1;
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Root;
RX   PubMed=17767721; DOI=10.1186/1471-2164-8-306;
RA   Gonzalez-Ibeas D., Blanca J., Roig C., Gonzalez-To M., Pico B.,
RA   Truniger V., Gomez P., Deleu W., Cano-Delgado A., Arus P., Nuez F.,
RA   Garcia-Mas J., Puigdomenech P., Aranda M.A.;
RT   "MELOGEN: an EST database for melon functional genomics.";
RL   BMC Genomics 8:306-306(2007).
RN   [2]
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; AM720593; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_008462597.1; XM_008464375.2.
DR   AlphaFoldDB; P0DI61; -.
DR   EnsemblPlants; MELO3C024564.2.1; maker-chr08-exonerate_est2genome-gene-83.9-mRNA-1:cds; MELO3C024564.2.
DR   GeneID; 103500916; -.
DR   Gramene; MELO3C024564.2.1; maker-chr08-exonerate_est2genome-gene-83.9-mRNA-1:cds; MELO3C024564.2.
DR   KEGG; cmo:103500916; -.
DR   eggNOG; ENOG502RYTF; Eukaryota.
DR   OrthoDB; 1230007at2759; -.
DR   PhylomeDB; P0DI61; -.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..209
FT                   /note="Casparian strip membrane protein 1"
FT                   /id="PRO_0000417765"
FT   TOPO_DOM        1..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..129
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   209 AA;  21861 MW;  90D1443414D12C28 CRC64;
     MKTGESTAID IAPETNNSGP IGKKKSTTPL LAAPVPDRGT HRMKRGLAIF DFVLRIGVLA
     SALAAAAAMG TSEQTLPFFT QFFQFEASYD DLPTFQFFVV AMAVVAGYVV LSIPFSIVCI
     IRPHAAGPRV LLLILDSVAL TLNTAAAGAA AAVVSLAHSG NSSTNWLAIC NQFGDFCQQA
     SGAVVGSFAA VLLFLLLILF SALSLKNSH