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Database: UniProt
Entry: A0A2C9TZB9_MANES
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ID   A0A2C9TZB9_MANES        Unreviewed;       933 AA.
AC   A0A2C9TZB9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glutamate receptor {ECO:0000256|PIRNR:PIRNR037090};
GN   ORFNames=MANES_18G003400 {ECO:0000313|EMBL:OAY22500.1};
OS   Manihot esculenta (Cassava) (Jatropha manihot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC   Manihot.
OX   NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY22500.1, ECO:0000313|Proteomes:UP000091857};
RN   [1] {ECO:0000313|EMBL:OAY22500.1, ECO:0000313|Proteomes:UP000091857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY22500.1};
RA   Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA   Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA   Stites J., Rounsley S., Rokhsar D.S.;
RT   "WGS assembly of Manihot esculenta.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC       cation channel. {ECO:0000256|PIRNR:PIRNR037090}.
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, ECO:0000256|PIRNR:PIRNR037090}.
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DR   EMBL; CM004404; OAY22500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9TZB9; -.
DR   STRING; 3983.A0A2C9TZB9; -.
DR   EnsemblPlants; OAY22500; OAY22500; MANES_18G003400.
DR   Gramene; OAY22500; OAY22500; MANES_18G003400.
DR   Proteomes; UP000091857; Chromosome lg18.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
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; 3.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR044440; GABAb_receptor_plant_PBP1.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR000337; GPCR_3.
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   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966:SF422; KAINATE-TYPE IONOTROPIC GLUTAMATE RECEPTOR SUBUNIT 1D; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PIRSF; PIRSF037090; Iontro_Glu-like_rcpt_pln; 1.
DR   PRINTS; PR01176; GABABRECEPTR.
DR   PRINTS; PR00248; GPCRMGR.
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, ECO:0000256|PIRNR:PIRNR037090};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|PIRNR:PIRNR037090};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW   ECO:0000256|PIRNR:PIRNR037090};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037090};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037090}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..933
FT                   /note="Glutamate receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012835830"
FT   TRANSMEM        579..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        649..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        829..849
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          468..809
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   REGION          881..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        758..812
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037090-50"
SQ   SEQUENCE   933 AA;  103109 MW;  B2610DC2628D6923 CRC64;
     MNAIVLLSFF FAVCGLFSSI HSRNFTSRPA VVNIGAIFSF ETTIGRVAKI AIEEAVKDVN
     ANSSILRGSK LVVSMHSSNC SGFTGMVEAL RFMETDAVAI IGPQSSVVAH IISQVVNELR
     VPLLSFAATD PTLDSLQFPF FVRTTRSDLY QMAAIAEIVD YYGWKQVIAI FIDDDNGRNG
     ILALSDKLAE RRSKISYKVG IPPDSGVTRG DIMDILVKVA LMEPRVVVLH VNPKLGFSIF
     SVAKYLGMMS NGYVWIATDW LSSYLDSSSP LPSETMNIMQ GVLALRQYTP DSDRKRSFSS
     RWSNLTGGSL GLNSYGLYAY DSVWLVAHAI DAFFEQGGVI SFSNDSRLRS EGGDLHLDAM
     SIFDDGLLLL KNVLRSDLVG LTGPLKFDSD RSLILPAYDV INVIGTGYRQ IGYWSNYSGL
     STVPPETFYM RPPNRSSANQ QLYSVIWPGE TVLKPRGWVF PNNGKQLRIG VPIRVSFKEF
     VTKVQGTDMF KGFCIDVFTA AVSLLPYAVP YQFIPFGNGK ENPSYTELVN LITTGFFDAV
     VGDIAIVTNR TKIVDYTQPF VASGLVVVAP FRKLNSGAWA FLLPFSPLMW IVTACFFIGV
     GTVVWILEHR INDEFRGPPK RQIITILWFS LSTLFFAHRE NTVSTLGRFV LIIWLFVVLI
     INSSYTASLT SILTVQQLFS PISGIDSLKE SDEPIGYQVG SFAEYYLSQE LGISKSRLVP
     LGSPEAYARA LELGPKKGGV AAVVDELPYV ELFLSTQCTF RIVGQEFTKS GWGFAFPRDS
     PLAIDMSTAI LALSENGDLQ RIHDKWLMHS GCSSDSTELE SDRLQLKSFS GLFLICGLAC
     FLALFIYFLQ IIRQLYSAPT VEAASPVQGS SRSGRLHRLL SLMDEKEDQS RQKNKRRKVE
     RSLSENDGDA KSGSNTKRKG IEMTSGSNIN PIS
//
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