SYM8_PEA
ID SYM8_PEA Reviewed; 894 AA.
AC Q4VY51; A9Q1K1; A9Q1K2; A9Q1K4; A9Q1K5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Probable ion channel SYM8;
DE AltName: Full=DMI1 protein homolog;
GN Name=SYM8; Synonyms=DMI1;
OS Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF ASP-305; ALA-306
RP AND ARG-351.
RC STRAIN=cv. Finale, and cv. Sparkle;
RX PubMed=17918620; DOI=10.1094/mpmi-20-10-1183;
RA Edwards A., Heckmann A.B., Yousafzai F., Duc G., Downie J.A.;
RT "Structural implications of mutations in the pea SYM8 symbiosis gene, the
RT DMI1 ortholog, encoding a predicted ion channel.";
RL Mol. Plant Microbe Interact. 20:1183-1191(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Finale;
RA Novak K.;
RT "Amplification of DMI1 homologue from Pisum sativum L.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=11078515; DOI=10.1073/pnas.230440097;
RA Walker S.A., Viprey V., Downie J.A.;
RT "Dissection of nodulation signaling using pea mutants defective for calcium
RT spiking induced by nod factors and chitin oligomers.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13413-13418(2000).
CC -!- FUNCTION: Required for both rhizobial and mycorrhizal symbiosis.
CC Involved in Nod-factor-induced calcium spiking. May induce a change in
CC membrane polarization that activates the opening of a calcium channel
CC required for calcium spiking. Might be calcium gated.
CC {ECO:0000269|PubMed:11078515, ECO:0000269|PubMed:17918620}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Can restore nodulation to a Medicago truncatula dmi1
CC mutant.
CC -!- SIMILARITY: Belongs to the castor/pollux (TC 1.A.1.23) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF447276; ABX57723.1; -; mRNA.
DR EMBL; EF447277; ABX57724.1; -; mRNA.
DR EMBL; EF447280; ABX57726.1; -; mRNA.
DR EMBL; EF447283; ABX57727.1; -; mRNA.
DR EMBL; AJ973194; CAJ00334.2; -; Genomic_DNA.
DR AlphaFoldDB; Q4VY51; -.
DR SMR; Q4VY51; -.
DR TCDB; 1.A.1.23.1; the voltage-gated ion channel (vic) superfamily.
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:0042802; F:identical protein binding; NAS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; NAS:UniProtKB.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
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..894
FT /note="Probable ion channel SYM8"
FT /id="PRO_0000395342"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..415
FT /evidence="ECO:0000255"
FT COMPBIAS 1..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 87..91
FT /note="ITPNV -> LTPNL (in strain: cv. Sparkle)"
FT MUTAGEN 305
FT /note="D->V: Loss of function."
FT /evidence="ECO:0000269|PubMed:17918620"
FT MUTAGEN 306
FT /note="A->V: In sym8-2; loss of function."
FT /evidence="ECO:0000269|PubMed:17918620"
FT MUTAGEN 351
FT /note="R->I: In sym8-5; loss of function."
FT /evidence="ECO:0000269|PubMed:17918620"
FT CONFLICT 61
FT /note="R -> W (in Ref. 2; CAJ00334)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="A -> G (in Ref. 2; CAJ00334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 99697 MW; 1A47F39923EB602D CRC64;
MAKSNEEPNS NLNTNKPPLK RTKTLAQQPS LNLRVSIAAA DNGIGNSSSS STKTDFEQQQ
RNYPSFLGIG STSRKRRPPP PPKPSNITPN VKPPASDFQT KPHSEPKTSP SSSSPPSLPI
AITKQQQQQH SISSPIFYLF VITCVIFVPY SAFLQYKLAK LKDMKLQLCC QIDFCSGNGK
TSLQKDVVDD GSFSYYILNA DSRTISLYIV LFTLVLPFIL YKYIDYLPQM INFSRRTNSN
KEDVPLKKRV AYMVDVFFSI YPYAKLLALL FATLFLIAFG GLALYAVTGG SMAEALWHSW
TYVADAGNHA ETEGMGQRIV SVSISAGGML IFAMMLGLVS DAISEKVDSL RKGKSEVIER
NHVLILGWSD KLGSLLKQLA IANKSVGGGV IVVLAEKEKE EMEMDIAKLE FDFMGTSVIC
RSGSPLILAD LKKVSVSKAR AIIVLASDEN ADQSDARALR VVLSLTGVKE ALRGHVVVEM
SDLDNEPLVK LVGGELIETV VAHDVIGRLM IQCALQPGLA QIWEDILGFE NAEFYIKRWP
ELDGLLFKDI LISFPDAIPC GVKVSADGGK IVINPDDNYV LRDGDEVLVI AEDDDTYAPG
PLPEVRKGYF PRIRDPPKYP EKILFCGWRR DIDDMIMVLE AFLAPGSELW MFNEVPEKQR
ERKLAAGELD VFGLENIKLV HREGNAVIRR HLESLPLETF DSILILADES VEDSVAHSDS
RSLATLLLIR DIQSRRLPYR DTKSTSLRLS GFSHNSWIRE MQQASDKSII ISEILDSRTR
NLVSVSRISD YVLSNELVSM ALAMVAEDKQ INRVLEELFA EEGNEMCIKP AEFYLFDQEE
LCFYDIMIRG RTRKEIVIGY RLASQERALI NPSEKSMTRK WSLDDVFVVI ASGE
