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Database: UniProt
Entry: A0A151J2M1_9HYME
LinkDB: A0A151J2M1_9HYME
Original site: A0A151J2M1_9HYME 
ID   A0A151J2M1_9HYME        Unreviewed;      1365 AA.
AC   A0A151J2M1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glutamate [NMDA] receptor subunit 3A {ECO:0000313|EMBL:KYN16338.1};
GN   ORFNames=ALC57_11420 {ECO:0000313|EMBL:KYN16338.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN16338.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN16338.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN16338.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN16338.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000256|ARBA:ARBA00008685}.
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DR   EMBL; KQ980368; KYN16338.1; -; Genomic_DNA.
DR   RefSeq; XP_018367908.1; XM_018512406.1.
DR   STRING; 471704.A0A151J2M1; -.
DR   GeneID; 108764266; -.
DR   OrthoDB; 1034721at2759; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:UniProt.
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; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   PANTHER; PTHR18966:SF448; IONOTROPIC RECEPTOR NMDAR3; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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, ECO:0000313|EMBL:KYN16338.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1365
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007582436"
FT   TRANSMEM        673..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        712..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        742..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        923..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          542..900
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          557..617
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
FT   REGION          1049..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1254..1274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1303..1333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1092
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1365 AA;  151325 MW;  EAF8B56BBC826162 CRC64;
     MPSSYTGVVI LLLLGTSVSV SGTADAAKSL RAAKARLRSS YASWRIVVCL TQPQTPFKAD
     VQKAWEEARL ESFHADMDVS YIETRMTPMT DSLLYPLSVL NKFCTDIEGG KTVLSLIIGG
     GSAARFLVTA AAALNLPALW LPFTHRDFLR QGNLGRFENR IGSSPKEVGA AAAALMHRAN
     WHAFTLLIDT TLLPVTHLLQ TNPPTLTPRA IIHLPTNDRT LRLRLRRVAE ESGSGGVVVM
     ACDLNNARKI LGAAGKFEML SGRFLWLWLD LKAELRPNEP NIISSHLLHS SRVAVATNEN
     LPLLERTINL ALDDKRLPSL NPLPSLANDI HRLQEYRWRD EKIVTKREDK SFNFEDEEEV
     VRLPSDRELN SKSFMPVGML ALRPSGIKIM GGDTILTRML RETSQALDET FLETKTRLGR
     MREAQIKEHF VPECYSDRNA KFMKSDAREN VSAILTSKLR KSMGQISKDK AEFQLLNLQA
     VRFPGNKTQL RWTKVGTIKG GREVRLDTII WPGGGIMPAY LEQGGEKVGM PIYSIVTAQA
     SPFTMITNLQ EGFCLRGLTC RQGKTVMCCY GLSMDLLSLV ARELGFRFNL YLAEDGLFGK
     RNNRNGTWNG VMGELVSGRA QLAFAALSVS THRAKVVDFT TPYYFSGVSF LTAPKLRSEI
     PLFAFLFPFS TELWIAVFTS LNLTAIAVAL YEWFSPFGLN PWGRQRSKNF SIASALWVMW
     GLLCGHLVAF KAPKSWPNKF LINIWGGFSV IFVASYTANI AALIAGLFFH SAVSNYHDKS
     LLSQRVGAPR ASAAEYYVQK ANPELWSHMA RYSLSNVAEG VEKLRNGTLD ILISDTPILD
     YYRETDNGCR LQKIGDTINE DTYAIALTRG HPLKESISKV IANYTSNGLL DILQEKWYGD
     LPCLSGRAGM DLDFDPGGQP RPLGVASVAG VFCLLGMGVV LGSIILAGEH LFYKYTLPRL
     RHRPEDSIWR SRNVMFFSQK LYRFINCVEL VSPHHAAREL VHTVRQGQIA SLFQKSVKRK
     EHEQRRRRKS KAQFFEMIQE IRRVQQEEKI ETVPEENDTA KTAKKDEKLG KGRERSRSKS
     PLMPRSPKRS EKSRSSTNLS ASRLGLSPVS LDAPMKPREF TLSSTNLRAR SPLETVGRRL
     SHGDGGSPPP RLASFGGSAT LRPLAPTRSD STSGGTPTIR RDSAAGGGGV PTPRYPRSPA
     KRGQSFPVFA TLRPPHSAGY QSRSPLLSPN SELTSAIGRK LSREWGSGTI DLTRSSEAIG
     SGSGGGGGGS RGSTYTLNQE MTLSLSRSGE EKTQEEALSI KKPIRRARSH ENRDSSKLMA
     DLPSPRLTQP VVGGQFVSER TKKQLDSELK AILTARAHHR DLHPP
//
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