DMI1_MEDTR
ID DMI1_MEDTR Reviewed; 882 AA.
AC Q6RHR6; Q1SKV5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Ion channel DMI1 {ECO:0000303|PubMed:14963334};
DE AltName: Full=Does not make infections protein 1 {ECO:0000303|PubMed:14963334};
GN Name=DMI1 {ECO:0000303|PubMed:14963334};
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], INDUCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Root;
RX PubMed=14963334; DOI=10.1126/science.1092986;
RA Ane J.-M., Kiss G.B., Riely B.K., Penmetsa R.V., Oldroyd G.E., Ayax C.,
RA Levy J., Debelle F., Baek J.-M., Kalo P., Rosenberg C., Roe B.A.,
RA Long S.R., Denarie J., Cook D.R.;
RT "Medicago truncatula DMI1 required for bacterial and fungal symbioses in
RT legumes.";
RL Science 303:1364-1367(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG The International Medicago Genome Annotation Group;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17173544; DOI=10.1111/j.1365-313x.2006.02957.x;
RA Riely B.K., Lougnon G., Ane J.M., Cook D.R.;
RT "The symbiotic ion channel homolog DMI1 is localized in the nuclear
RT membrane of Medicago truncatula roots.";
RL Plant J. 49:208-216(2007).
RN [4]
RP FUNCTION.
RX PubMed=17631529; DOI=10.1104/pp.107.097261;
RA Peiter E., Sun J., Heckmann A.B., Venkateshwaran M., Riely B.K.,
RA Otegui M.S., Edwards A., Freshour G., Hahn M.G., Cook D.R., Sanders D.,
RA Oldroyd G.E., Downie J.A., Ane J.M.;
RT "The Medicago truncatula DMI1 protein modulates cytosolic calcium
RT signaling.";
RL Plant Physiol. 145:192-203(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CNGC15A; CNGC15B AND CNGC15C.
RX PubMed=27230377; DOI=10.1126/science.aae0109;
RA Charpentier M., Sun J., Martins T.V., Radhakrishnan G.V., Findlay K.,
RA Soumpourou E., Thouin J., Very A.A., Sanders D., Morris R.J., Oldroyd G.E.;
RT "Nuclear-localized cyclic nucleotide-gated channels mediate symbiotic
RT calcium oscillations.";
RL Science 352:1102-1105(2016).
CC -!- FUNCTION: 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 mycorrhizal symbiosis. May be involved in the regulation of
CC the calcium channel responsible for calcium spiking by mobilizing
CC another cation, and thereby altering the membrane potential.
CC {ECO:0000269|PubMed:17631529}.
CC -!- SUBUNIT: Interacts (via c-terminus) with CNGC15A, CNGC15B and CNGC15C
CC (via N-terminus). The Nod factor has no effect on these interactions,
CC implying that the complex is maintained after activation.
CC {ECO:0000269|PubMed:27230377}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:17173544,
CC ECO:0000269|PubMed:27230377}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17173544}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots and nodules. Also
CC detected in pods, flowers, leaves, and stems.
CC {ECO:0000269|PubMed:14963334, ECO:0000269|PubMed:17173544}.
CC -!- INDUCTION: Not induced after bacterial or Nod factor treatment.
CC {ECO:0000269|PubMed:14963334}.
CC -!- DOMAIN: The N-terminal domain (1-76) is sufficient, but not required,
CC to target DMI1 to the nucleus.
CC -!- DISRUPTION PHENOTYPE: Loss of microbial symbioses. Undergoes typical
CC root hairs growth deformation in response to Nod factors, but exhibits
CC no calcium spiking and nodule formation. {ECO:0000269|PubMed:14963334}.
CC -!- SIMILARITY: Belongs to the castor/pollux (TC 1.A.1.23) family.
CC {ECO:0000305}.
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DR EMBL; AY497771; AAS49490.1; -; mRNA.
DR EMBL; AC140550; ABE79577.1; -; Genomic_DNA.
DR RefSeq; XP_003592931.1; XM_003592883.2.
DR AlphaFoldDB; Q6RHR6; -.
DR SMR; Q6RHR6; -.
DR STRING; 3880.AES63182; -.
DR EnsemblPlants; AES63182; AES63182; MTR_2g005870.
DR GeneID; 11433851; -.
DR Gramene; AES63182; AES63182; MTR_2g005870.
DR eggNOG; ENOG502QU6W; Eukaryota.
DR HOGENOM; CLU_012980_0_0_1; -.
DR OMA; NHADTEG; -.
DR OrthoDB; 181406at2759; -.
DR ExpressionAtlas; Q6RHR6; differential.
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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR31563; PTHR31563; 1.
DR Pfam; PF06241; Castor_Poll_mid; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Ion channel; Ion transport; Membrane; Nucleus; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..882
FT /note="Ion channel DMI1"
FT /id="PRO_0000165855"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..403
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 98442 MW; 3A2E2DE0E54E6AB9 CRC64;
MAKSNEESSN LNVMNKPPLK KTKTLPSLNL RVSVTPPNPN DNNGIGGTST TKTDFSEQQW
NYPSFLGIGS TSRKRRQPPP PPSKPPVNLI PPHPRPLSVN DHNKTTSSLL PQPSSSSITK
QQQQHSTSSP IFYLLVICCI ILVPYSAYLQ YKLAKLKDMK LQLCGQIDFC SRNGKTSIQE
EVDDDDNADS RTIALYIVLF TLILPFVLYK YLDYLPQIIN FLRRTESNKE DVPLKKRVAY
MVDVFFSIYP YAKLLALLCA TLFLIAFGGL ALYAVTGGSM AEALWHSWTY VADAGNHAET
EGTGQRIVSV SISAGGMLIF AMMLGLVSDA ISEKVDSLRK GKSEVIERNH VLILGWSDKL
GSLLKQLAIA NKSVGGGVIV VLAEKEKEEM EMDIAKLEFD FMGTSVICRS GSPLILADLK
KVSVSKARAI IVLAADENAD QSDARALRVV LSLAGVKEGL RGHVVVEMSD LDNEPLVKLV
GGELIETVVA HDVIGRLMIQ CALQPGLAQI WEDILGFENA EFYIKRWPEL DDLLFKDILI
SFPDAIPCGV KVAADGGKIV INPDDNYVLR DGDEVLVIAE DDDTYAPGPL PEVRKGYFPR
IRDPPKYPEK ILFCGWRRDI DDMIMVLEAF LAPGSELWMF NEVPEKERER KLAAGELDVF
GLENIKLVHR EGNAVIRRHL ESLPLETFDS ILILADESVE DSVAHSDSRS LATLLLIRDI
QSRRLPYRDT KSTSLRLSGF SHNSWIREMQ QASDKSIIIS EILDSRTRNL VSVSRISDYV
LSNELVSMAL AMVAEDKQIN RVLEELFAEE GNEMCIKPAE FYLFDQEELC FYDIMIRGRT
RKEIVIGYRL ANQERAIINP SEKSVPRKWS LDDVFVVLAS GE
