ID A0A444X659_ARAHY Unreviewed; 998 AA.
AC A0A444X659;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Ionotropic glutamate receptor C-terminal domain-containing protein {ECO:0000259|SMART:SM00079};
GN ORFNames=Ahy_B10g104659 {ECO:0000313|EMBL:RYQ85170.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ85170.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ85170.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ85170.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000256|ARBA:ARBA00008685}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYQ85170.1}.
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DR EMBL; SDMP01000020; RYQ85170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444X659; -.
DR STRING; 3818.A0A444X659; -.
DR Proteomes; UP000289738; Chromosome b10.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR CDD; cd13686; GluR_Plant; 1.
DR CDD; cd19990; PBP1_GABAb_receptor_plant; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR044440; GABAb_receptor_plant_PBP1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR InterPro; IPR017103; Iontropic_Glu_rcpt_pln.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR18966:SF450; GLUTAMATE RECEPTOR 2.8-RELATED; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PIRSF; PIRSF037090; Iontro_Glu-like_rcpt_pln; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037090-50};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..998
FT /note="Ionotropic glutamate receptor C-terminal domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019461300"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..823
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT REGION 909..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 771..826
FT /evidence="ECO:0000256|PIRSR:PIRSR037090-50"
SQ SEQUENCE 998 AA; 111320 MW; A2B5191530CE5F6D CRC64;
MVKNQRPTTL VLSLFWWFFG VVATVMGQRN REATTLFQTR VVKVGVVLDL GGGIVGKMGS
NSIRMCVNDF YDSHPHYKTR LQLILRDSQR DIVTAAAQVV DLIKNEQVEA VIGPVTTTEA
MFVINLGDKA HVPIVTFSAT SPSLSSLHTP YFFQIAQKDS TQVEAISAII QAFRWKEVVP
IYVDNSYGEG LIPWLTNSLQ KSYIRVPYLS AIDFSATDDA IERELYKLMT MQTRVFVVHM
TPLLGSRLFA IAKTIGMMDQ GYVWIVTDGM ANFFNSLDSS IMESMEGVLG VRPCIPRTKQ
FLDFRARWKR QFLRDNPTLV DINLNAFGIW AYDATTALAM AVEKLDSTLS GFTNVSKNSS
NVTDLENFGV SRNGEKLREA LSNVRFKGVG GDFKLVGGGE LQASAFEIVN AIGNGERNIG
FWMPDKGLIR NMNAKNATTA YSTSKENLGT IIWPGDTYSV PKGWQIPTNG NMLKIGVPVK
DCGYTEFVKI IHDPITNSRK VTGFCIDVFN AVVEALPYAL PFEFIPFEKS NGEMAGTYDD
LITQVYYGKF DGVVGDTTIT ANRSSYVDFT LPYTESGVTM VVPIKDNRKK NAWAFLKPLT
WDLWVTTFCS FVFIGFVVWV LEHRINNHFR GPPSYQIGTS LWFSFSTMVF SHRERVASNC
GRFVVIVWVF VVQILVQSYT ASLTSLLTVE QLRPVITDVH QLLKNRLNVG YLDGSFVREI
LKDLGFQESQ LRIYRSAEEC NDLFIKGTAN GGIDAAFDEV PYVTHLLQIY CSKYTMIEPR
FKTGGFGFVF PKGSPLVADI SRAILNVTQG AKMKTIENAW LNGSSCPESN AQISSASLGL
ESFWGLFLVI GVSCALALMF FLATFLYQYR HILSSHQPST SIWTRIGTLL SIFNEKDLSS
HTFKKSAKQD ASVASSPAHH HGIGSAEASP STHCPSSPYS YTESNFSFYG DQVMFSPDRH
DYGTHQGHET QDREMRVVHD DTQEVATTNS NNTNSQAT
//
