ID A0A0G2JSH8_RAT Unreviewed; 1250 AA.
AC A0A0G2JSH8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118};
GN Name=Grin2c {ECO:0000313|Ensembl:ENSRNOP00000004477.3,
GN ECO:0000313|RGD:2739};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000004477.3, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000004477.3, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000004477.3,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000004477.3}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000004477.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system.
CC {ECO:0000256|RuleBase:RU367118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
CC Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104,
CC ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034104}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000256|RuleBase:RU367118}.
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DR RefSeq; NP_036707.3; NM_012575.3.
DR RefSeq; XP_006247769.1; XM_006247707.2.
DR RefSeq; XP_017452475.1; XM_017596986.1.
DR RefSeq; XP_017452476.1; XM_017596987.1.
DR RefSeq; XP_017452477.1; XM_017596988.1.
DR RefSeq; XP_017452478.1; XM_017596989.1.
DR RefSeq; XP_017452479.1; XM_017596990.1.
DR AlphaFoldDB; A0A0G2JSH8; -.
DR SMR; A0A0G2JSH8; -.
DR Ensembl; ENSRNOT00000004477.6; ENSRNOP00000004477.3; ENSRNOG00000003280.7.
DR GeneID; 24411; -.
DR KEGG; rno:24411; -.
DR CTD; 2905; -.
DR RGD; 2739; Grin2c.
DR GeneTree; ENSGT00940000156964; -.
DR OMA; FPIHYGD; -.
DR OrthoDB; 1034721at2759; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003280; Expressed in cerebellum and 4 other cell types or tissues.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IEA:Ensembl.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IEA:Ensembl.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IEA:Ensembl.
DR GO; GO:0033058; P:directional locomotion; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR CDD; cd06378; PBP1_iGluR_NMDA_NR2; 1.
DR CDD; cd13718; PBP2_iGluR_NMDA_Nr2; 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; 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; IPR018884; NMDAR2_C.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR18966:SF361; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2C; 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 Pfam; PF10565; NMDAR2_C; 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 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367118};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU367118};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286,
KW ECO:0000256|RuleBase:RU367118};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU367118};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU367118};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU367118};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367118};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367118};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}.
FT TRANSMEM 567..590
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 611..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 640..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
FT TRANSMEM 831..854
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367118"
SQ SEQUENCE 1250 AA; 136635 MW; 61E63ABDAA571E34 CRC64;
MPALVSLQDP PVDMGGALGP ALLLTSLLGA WARLGAGQGE QAVTVAVVFG SSGPLQTQAR
TRLTSQNFLD LPLEIQPLTV GVNNTNPSSI LTQICGLLGA ARVHGIVFED NVDTEAVAQL
LDFVSSQTHV PILSISGGSA VVLTPKEPGS AFLQLGVSLE QQLQVLFKVL EEYDWSAFAV
ITSLHPGHAL FLEGVRAVAD ASYLSWRLLD VLTLELGPGG PRARTQRLLR QVDAPVLVAY
CSREEAEVLF AEAAQAGLVG PGHVWLVPNL ALGSTDAPPA AFPVGLISVV TESWRLSLRQ
KVRDGVAILA LGAHSYRRQY GTLPAPAGDC RSHPGPVSPA REAFYRHLLN VTWEGRDFSF
SPGGYLVRPT MVVIALNRHR LWEMVGRWDH GVLYMKYPVW PRYSTSLQPV VDSRHLTVAT
LEERPFVIVE SPDPGTGGCV PNTVPCRRQS NHTFSSGDLT PYTKLCCKGF CIDILKKLAK
VVKFSYDLYL VTNGKHGKRV RGVWNGMIGE VYYKRADMAI GSLTINEERS EIIDFSVPFV
ETGISVMVSR SNGTVSPSAF LEPYSPAVWV MMFVMCLTVV AITVFMFEYF SPVSYNQNLT
KGKKPGGPSF TIGKSVWLLW ALVFNNSVPI ENPRGTTSKI MVLVWAFFAV IFLASYTANL
AAFMIQEQYI DTVSGLSDKK FQRPQDQYPP FRFGTVPNGS TERNIRSNYR DMHTHMVKFN
QRSVEDALTS LKMGKLDAFI YDAAVLNYMA GKDEGCKLVT IGSGKVFATT GYGIAMQKDS
HWKRAIDLAL LQLLGDGETQ KLETVWLSGI CQNEKNEVMS SKLDIDNMAG VFYMLLVAMG
LALLVFAWEH LVYWKLRHSV PNSSQLDFLL AFSRGIYSCF NGVQSLPSPA RPPSPDLTAD
SAQANVLKML QAARDMVNTA DVSSSLDRAT RTIENWGNNR RVPAPTASGP RSSTPGPPGQ
PSPSGWGPPG GGRTPLARRA PQPPARPATC GPPLPDVSRP SCRHASDARW PVRVGHQGPH
VSASERRALP ERSLLPAHCH YSSFPRAERS GRPYLPLFPE PPEPDDLPLL GPEQLARREA
MLRAAWARGP RPRHASLPSS VAEAFTRSNP LPARCTGHAC ACPCPQSRPS CRHLAQAQSL
RLPSYPEACV EGVPAGVATW QPRQHVCLHA HTRLPFCWGT VCRHPPPCTS HSPWLIGTWE
PPAHRVRTLG LGTGYRDSGV LEEVSREACG TQGFPRSCTW RRVSSLESEV
//
