CASTO_LOTJA
ID CASTO_LOTJA Reviewed; 853 AA.
AC Q5H8A6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Ion channel CASTOR;
GN Name=CASTOR;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
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; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INDUCTION, AND MUTAGENESIS OF THR-249; ALA-264; GLY-383; ASP-444;
RP ARG-590; VAL-598; PRO-698; ALA-760 AND 846-PHE-VAL-847.
RC STRAIN=cv. Gifu / B-129;
RX PubMed=15616514; DOI=10.1038/nature03237;
RA Imaizumi-Anraku H., Takeda N., Charpentier M., Perry J., Miwa H.,
RA Umehara Y., Kouchi H., Murakami Y., Mulder L., Vickers K., Pike J.,
RA Downie J.A., Wang T., Sato S., Asamizu E., Tabata S., Yoshikawa M.,
RA Murooka Y., Wu G.-J., Kawaguchi M., Kawasaki S., Parniske M., Hayashi M.;
RT "Plastid proteins crucial for symbiotic fungal and bacterial entry into
RT plant roots.";
RL Nature 433:527-531(2005).
RN [2]
RP FUNCTION.
RX PubMed=16903357; DOI=10.1094/mpmi-19-0914;
RA Miwa H., Sun J., Oldroyd G.E., Downie J.A.;
RT "Analysis of Nod-factor-induced calcium signaling in root hairs of
RT symbiotically defective mutants of Lotus japonicus.";
RL Mol. Plant Microbe Interact. 19:914-923(2006).
RN [3]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF ALA-264 AND 479-LEU-ALA-480, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19106374; DOI=10.1105/tpc.108.063255;
RA Charpentier M., Bredemeier R., Wanner G., Takeda N., Schleiff E.,
RA Parniske M.;
RT "Lotus japonicus CASTOR and POLLUX are ion channels essential for
RT perinuclear calcium spiking in legume root endosymbiosis.";
RL Plant Cell 20:3467-3479(2008).
CC -!- FUNCTION: Ion channel with a moderate preference for potassium over
CC sodium and calcium. Involved in perinuclear calcium spiking but not in
CC cytosolic calcium influx. Closed at negative voltages in presence of
CC magnesium. Required for early signal transduction events leading to
CC endosymbiosis. Acts early in a signal transduction chain leading from
CC the perception of Nod factor to the activation of calcium spiking. Also
CC involved in fungal entry into root epidermal cells during the
CC establishment of the arbuscular mycorrhizal symbiosis.
CC {ECO:0000269|PubMed:16903357, ECO:0000269|PubMed:19106374}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:19106374}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15616514,
CC ECO:0000269|PubMed:19106374}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15616514, ECO:0000269|PubMed:19106374}. Note=The
CC chloroplastic localization proposed by PubMed:15616514 is probably an
CC overexpression artifact.
CC -!- TISSUE SPECIFICITY: Expressed in infected and uninfected roots, leaves,
CC seed pods, and flower buds. {ECO:0000269|PubMed:15616514,
CC ECO:0000269|PubMed:19106374}.
CC -!- INDUCTION: Slightly repressed during the first 2 days after bacterial
CC or Nod factor treatment. {ECO:0000269|PubMed:15616514}.
CC -!- SIMILARITY: Belongs to the castor/pollux (TC 1.A.1.23) family.
CC {ECO:0000305}.
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DR EMBL; AB162157; BAD89021.1; -; mRNA.
DR EMBL; AB162016; BAD89019.1; -; Genomic_DNA.
DR PDB; 6O6J; X-ray; 1.60 A; A=312-853.
DR PDB; 6O7A; X-ray; 3.30 A; A/B/C/D=312-853.
DR PDB; 6O7C; X-ray; 1.85 A; A=312-853.
DR PDBsum; 6O6J; -.
DR PDBsum; 6O7A; -.
DR PDBsum; 6O7C; -.
DR AlphaFoldDB; Q5H8A6; -.
DR SMR; Q5H8A6; -.
DR TCDB; 1.A.1.23.2; the voltage-gated ion channel (vic) superfamily.
DR OMA; VPEMDRE; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR044849; CASTOR/POLLUX/SYM8-like.
DR InterPro; IPR010420; CASTOR/POLLUX/SYM8_dom.
DR PANTHER; PTHR31563; PTHR31563; 1.
DR Pfam; PF06241; Castor_Poll_mid; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Ion channel; Ion transport; Membrane; Nucleus;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..853
FT /note="Ion channel CASTOR"
FT /id="PRO_0000004682"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..137
FT /evidence="ECO:0000255"
FT COMPBIAS 1..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 249
FT /note="T->I: In castor-15; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 264
FT /note="A->T: In castor-2 / Ljsym4-2; altered selectivity of
FT the pore resulting in a defective calcium spiking. No
FT nodules formation or arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514,
FT ECO:0000269|PubMed:19106374"
FT MUTAGEN 383
FT /note="G->E: In castor-3 / Ljsym22-1 and castor-16; no
FT nodules formation or arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 444
FT /note="D->N: In castor-13; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 479..480
FT /note="Missing: In castor-1 / Ljsym4-1; loss of
FT multimerization, no nodules formation or arbuscular
FT mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:19106374"
FT MUTAGEN 590
FT /note="R->H: In castor-17; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 598
FT /note="V->I: In castor-7; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 698
FT /note="P->L: In castor-6; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 760
FT /note="A->T: In castor-14; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 846..847
FT /note="FV->LW: In castor-11; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT /evidence="ECO:0000269|PubMed:15616514"
FT MUTAGEN 848..853
FT /note="Missing: In castor-11; no nodules formation or
FT arbuscular mycorrhizal symbiosis."
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 332..343
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 411..426
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 433..441
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 446..453
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 479..487
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 517..523
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 546..553
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 592..602
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 607..615
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 635..643
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:6O7A"
FT HELIX 649..653
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 661..665
FT /evidence="ECO:0007829|PDB:6O6J"
FT TURN 669..673
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 675..695
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 728..734
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 736..741
FT /evidence="ECO:0007829|PDB:6O6J"
FT TURN 742..744
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 746..750
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 755..766
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 770..778
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 779..789
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 790..792
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:6O6J"
FT HELIX 802..810
FT /evidence="ECO:0007829|PDB:6O6J"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 814..820
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 822..825
FT /evidence="ECO:0007829|PDB:6O7A"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 835..839
FT /evidence="ECO:0007829|PDB:6O6J"
FT STRAND 845..851
FT /evidence="ECO:0007829|PDB:6O6J"
SQ SEQUENCE 853 AA; 95180 MW; FF56464C638EE6C0 CRC64;
MSLDSEVSVS SSSGRDWFFP SPSFFRSSPS QYGRRFHTNS NTHSAPSSTY PSGIRHRRRV
KFSRTPTTSS NEKPQISIVS DKPSAISKNN LNWLSQFGLQ FALVTLTIVF LLLLLLRNTH
LESQVNKLQG EILRLHACHQ LDTLNVSSST AHKSQDTHPC SCENFKRNLA LFLSFMLLLI
PLIIFKYIDY VSRSRLSENI SEQVSLNKQI AYRVDVFLSV YPYAKPLVLL VATLLLIFLG
GLTLFGVTTE DLGHCLWLSW TYVADSGNHA SSEGIGPRLV AVSISFGGML IFAMMLGLVS
DAISEKFDSL RKGKSEVVEQ NHTLILGWSD KLGSLLNQLA IANESLGGGT IAVMAERDKE
DMELDIGKME FDFKGTSVIC RSGSPLILAD LKKVSVSKAR TIIVLAEDGN ADQSDARALR
TVLSLTGVKE GLRGHIVVEM SDLDNEVLVK LVGGDLVETV VAHDVIGRLM IQCARQPGLA
QIWEDILGFE NCEFYIKRWP QLDGMLFEDV LISFPAAIPC GIKVASYGGK IILNPDDSYV
LQEGDEVLVI AEDDDTYAPA PLPMVRRGSL PKDFVYPKSP ERILFCGWRR DMEDMITVLD
ASLAPDSELW MFNDVPEKER EKKLIDGGLD ISRLENISLV NREGNAVIRR HLESLPLESF
DSILILADES VEDSAIQADS RSLATLLLIR DIQARRLPYV AMASQTQGGN FSKGSWIGEM
KQASDKTVII SEILDPRTKN LLSMSKISDY VLSNELVSMA LAMVAEDRQI NDVLEELFAE
EGNEMHIRQA DIYLREGEEM SFYEIMLRAR QRREILIGYR LANAERAVIN PPAKTGRRKW
SLKDVFVVIT EKE
