N24_MEDTR
ID N24_MEDTR Reviewed; 234 AA.
AC O24088;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=CASP-like protein N24;
DE AltName: Full=CASP-like protein 4A1;
DE Short=MtCASPL4A1;
DE AltName: Full=Nodulin 24;
DE Short=MtN24;
GN Name=N24;
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 [MRNA], AND INDUCTION DURING NODULATION.
RC STRAIN=cv. Jemalong J5; TISSUE=Root nodule;
RX PubMed=8634476; DOI=10.1094/mpmi-9-0233;
RA Gamas P., de Carvalho Niebel F., Lescure N., Cullimore J.;
RT "Use of a subtractive hybridization approach to identify new Medicago
RT truncatula genes induced during root nodule development.";
RL Mol. Plant Microbe Interact. 9:233-242(1996).
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 -!- SUBUNIT: Homodimer and heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: During Rhizobium meliloti-mediated root nodulation.
CC {ECO:0000269|PubMed:8634476}.
CC -!- SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP)
CC family. {ECO:0000305}.
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DR EMBL; Y15290; CAA75572.1; -; mRNA.
DR RefSeq; XP_013450803.1; XM_013595349.1.
DR AlphaFoldDB; O24088; -.
DR ProMEX; O24088; -.
DR EnsemblPlants; KEH24843; KEH24843; MTR_6g007160.
DR GeneID; 25495170; -.
DR Gramene; KEH24843; KEH24843; MTR_6g007160.
DR HOGENOM; CLU_048961_5_0_1; -.
DR OrthoDB; 1543616at2759; -.
DR ExpressionAtlas; O24088; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR006702; CASP_dom.
DR Pfam; PF04535; DUF588; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..234
FT /note="CASP-like protein N24"
FT /id="PRO_0000391510"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 234 AA; 26529 MW; C78DBE19296C3ACD CRC64;
MSTINIESLD QDTKDEPKEQ TQEDNNEVLK VLEEKINMMD PKNTSGDTEV VITNFLKSKK
EVKWYVALLV IRVFAFVFCL IAFSVLGASE QRVLVSENLT NWYSSGFTIQ TPYEFHWYKW
DEFRYSFAAN VIGFVYSGLQ ICHLVMYLIT KKHTINPKLQ GYFNVAIDQT LAYILMSASS
SAATAAHLLK DYWLEHGADT FIEMANASVS MSFLAFGAFA LASLVSGIIL CRFT