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CASP1_MEDTR
ID   CASP1_MEDTR             Reviewed;         186 AA.
AC   G7KGQ4;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Casparian strip membrane protein 1;
DE            Short=MtCASP1;
GN   OrderedLocusNames=MTR_5g041900;
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA   Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA   Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA   De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA   Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA   Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA   Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA   Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA   Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA   Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA   Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA   Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA   Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA   O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA   Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA   Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA   Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA   Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA   White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA   Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA   Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
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; CM001221; AES96820.1; -; Genomic_DNA.
DR   RefSeq; XP_003613862.1; XM_003613814.2.
DR   AlphaFoldDB; G7KGQ4; -.
DR   SMR; G7KGQ4; -.
DR   EnsemblPlants; AES96820; AES96820; MTR_5g041900.
DR   GeneID; 11414000; -.
DR   Gramene; AES96820; AES96820; MTR_5g041900.
DR   KEGG; mtr:MTR_5g041900; -.
DR   eggNOG; ENOG502RXTK; Eukaryota.
DR   HOGENOM; CLU_066104_3_2_1; -.
DR   OMA; ANWFAVC; -.
DR   OrthoDB; 1392215at2759; -.
DR   Proteomes; UP000002051; Chromosome 5.
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   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..186
FT                   /note="Casparian strip membrane protein 1"
FT                   /id="PRO_0000417781"
FT   TOPO_DOM        1..26
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..157
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   186 AA;  19978 MW;  6AABAA4313915E0B CRC64;
     MKGGSIELGE VSKNASTNKG VKRGLSIMDF ILRIIAGVAT LASAVAMGTT DERLPFATSF
     VQFRAEYDDL PSFVFFVLAN SIVCGYLALS LILSILHIVR STAVKSRILL IVLDMVMMGL
     LAAAASAAAS IVYIAHYGNT QANWFPICQQ YNSFCERISG SLIGSYIAVA LFIIIILLSQ
     SAISRN
 
 
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