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Entry version 57 (02 Jun 2021)
Sequence version 1 (03 Mar 2009)
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Protein

Glutamate receptor ionotropic, NMDA 2A

Gene

grin2a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg2+ (PubMed:28232581).

Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). Plays a role in dendritic branching in brain neurons and in synaptic plasticity (PubMed:18216193).

Curated2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi120Zinc; via tele nitrogenBy similarity1
Metal bindingi274ZincBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei510GlutamateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport
LigandCalcium, Magnesium, Metal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glutamate receptor ionotropic, NMDA 2A
Short name:
GluN2A
Alternative name(s):
N-methyl D-aspartate receptor subtype 2A
Short name:
NMDAR2A
Short name:
NR2A1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:grin2a
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-1021446, grin2a.L

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini21 – 547Extracellular1 PublicationAdd BLAST527
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei548 – 568Helical1 PublicationAdd BLAST21
Topological domaini569 – 592Cytoplasmic1 PublicationAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei593 – 612Discontinuously helical1 PublicationAdd BLAST20
Topological domaini613 – 617Cytoplasmic1 Publication5
Transmembranei618 – 637Helical1 PublicationAdd BLAST20
Topological domaini638 – 808Extracellular1 PublicationAdd BLAST171
Transmembranei809 – 829Helical1 PublicationAdd BLAST21
Topological domaini830 – 1451Cytoplasmic1 PublicationAdd BLAST622

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500286423121 – 1451Glutamate receptor ionotropic, NMDA 2AAdd BLAST1431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi67N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi79 ↔ 312Combined sources1 Publication
Glycosylationi332N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi372N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi421 ↔ 447Combined sources1 Publication
Disulfide bondi428 ↔ 448Combined sources1 Publication
Glycosylationi435N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi436N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi533N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi679N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi737 ↔ 792Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer. Forms heterotetrameric channels composed of two zeta subunits (grin1), and two epsilon subunits (grin2a, grin2b, grin2c or grin2d) (in vitro) (PubMed:28232581). In vivo, the subunit composition may depend on the expression levels of the different subunits (Probable).

Curated1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
B7ZSK1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni503 – 505Glutamate bindingBy similarity3
Regioni591 – 612Pore-formingCuratedAdd BLAST22
Regioni681 – 682Glutamate bindingBy similarity2
Regioni722 – 723Glutamate bindingBy similarity2
Regioni1011 – 1080DisorderedSequence analysisAdd BLAST70
Regioni1100 – 1165DisorderedSequence analysisAdd BLAST66

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1011 – 1031Polar residuesSequence analysisAdd BLAST21
Compositional biasi1032 – 1046Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi1100 – 1117Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi1138 – 1156Basic and acidic residuesSequence analysisAdd BLAST19

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains an N-terminal domain, a ligand-binding domain and a transmembrane domain. Agonist binding to the extracellular ligand-binding domains triggers channel gating.1 Publication
A hydrophobic region that gives rise to the prediction of a transmembrane span does not cross the membrane, but is part of a discontinuously helical region that dips into the membrane and is probably part of the pore and of the selectivity filter.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
188544at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001828, ANF_lig-bd_rcpt
IPR019594, Glu/Gly-bd
IPR001508, Iono_rcpt_met
IPR001320, Iontro_rcpt
IPR018884, NMDAR2_C
IPR028082, Peripla_BP_I

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01094, ANF_receptor, 1 hit
PF00060, Lig_chan, 1 hit
PF10613, Lig_chan-Glu_bd, 1 hit
PF10565, NMDAR2_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00177, NMDARECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00918, Lig_chan-Glu_bd, 1 hit
SM00079, PBPe, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53822, SSF53822, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

B7ZSK1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMFVLLLYT FLYAGDLGHG AEKSFPVLNI AVILGRTRYI TERDIRSLWT
60 70 80 90 100
RDMSLDFDVN VVTLLVNQTD PKSIITHVCD LMSGTKIHGV VFGDDTDQEA
110 120 130 140 150
IAQILDFVSS QTFIPILGIH GGSSMIMADK DEMSTFFQFG ASIKQQATVM
160 170 180 190 200
LNIMEEYDWH VFSVITSNFP GYRDFISFIK TTVDNSFVGW EVQNYITLDT
210 220 230 240 250
SYTDAQTLTQ LKKIHSSVIL LYCSKDEATY IFEEARSLGL MGYGFVWIVP
260 270 280 290 300
SLVTGNTDII PYEFPSGLVS VSYDDWDYGI EARVRDGLGI ITTAASAMLE
310 320 330 340 350
KHSVIPEAKT SCYGQNERND PPLHTLHNFM INVTWDGKDL SFTEDGYQAN
360 370 380 390 400
PKLVVLLLNM EREWEKVGKW ENKSLNMKYP VWPRITASLD SDHDDNHLSI
410 420 430 440 450
VTLEEAPFVI VENIDYLTGT CVRNTVPCRK YFRLNNSTTE GTSVKKCCKG
460 470 480 490 500
FCIDILKKLS KTVKFTYDLY LVTNGKHGKK IKNVWNGMIG EVVYKRAVMA
510 520 530 540 550
VGSLTINEER SVAVDFSVPF VETGISVMVS RSNGTVSPSA FLEPFSASVW
560 570 580 590 600
VMMFVMLLLV SAMAVFIFEY FSPVGYNRNL AQGKDPHGPS FTIGKAVWLL
610 620 630 640 650
WGLVFNNSVP VQNPKGTTSK IIVSIWAFFA VIFLASYTAN LAAFMIQEEF
660 670 680 690 700
VDQVTGLSDN KFQRPHDYSP PFRFGTVPNG STERNIRNNY PDMHQYMVKF
710 720 730 740 750
HQKGVQDALV SLKTGKLDAF IYDAAVLNYM AGRDEGCKLV TIGSGYIFAT
760 770 780 790 800
TGYGIALQKG SRWKRPIDLA LLQFVGDGEM EELEKLWLTG ICHTEKNEVM
810 820 830 840 850
SSQLDIDNMA GVFYMLAAAM ALSLITFVWE HLFYWKLRFC FTGVCTGTPG
860 870 880 890 900
LLFSISRGIY SCIHGVHIEE KKKSPDFSFT ASQTNMLKLL RASKNIANLS
910 920 930 940 950
NLNQSQCNSP KRTSDYIQRN SLLTDMVLDK GNLTYSDNRP FQQKDIYSEN
960 970 980 990 1000
TYDLAMLSAN CPKDNLNNYV FQGQHPLTLN ESNPNTVEVA VSAEAKVNTR
1010 1020 1030 1040 1050
PRQLWKKSVE TLRQTQGSVN ENGTEESKSS IKNQRFLPED GHFSDVSEAS
1060 1070 1080 1090 1100
SRATCHIDSE NNNKHRKSKD NLKKRPVSAK YARECSEVEL SYLKIKHGPN
1110 1120 1130 1140 1150
RDKVYTIDGD KEPSFIMDQP KYSENSPDQD DEDYPDVYQD HNDNYRKTEP
1160 1170 1180 1190 1200
LQSDRTPLHS EGRLPNNDIQ YKLFSKHYNL KEKNTSMSDA NDRHRQNSTH
1210 1220 1230 1240 1250
CRSCLSNMPN YTGHYTARSP YKCDDCLHTG KLYDIDEDQM LHEAANSMHS
1260 1270 1280 1290 1300
EDFYEHNWLE NNALHFQKKN KLRINRQHSC DNINKPREHD LGRPPRSLSL
1310 1320 1330 1340 1350
KEKERYIQEN PFAKFVIVPP EKLLGNNASL FTDSLKDSKR SKSLYPDNSS
1360 1370 1380 1390 1400
DNPFLHSYQE TQKLSHGRSS SDIYKQSSLP KARNDNYLRS SIKSTTSYSS
1410 1420 1430 1440 1450
RDGRVPDDMC VSEYALPYVT SNNSVYSAPR VVNSCSNRRV FKKMPSLESD

V
Length:1,451
Mass (Da):164,602
Last modified:March 3, 2009 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD15245B98B954F4C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti259I → M in ABX60543 (PubMed:18216193).Curated1
Sequence conflicti760G → V in ABX60543 (PubMed:18216193).Curated1
Sequence conflicti965N → S in ABX60543 (PubMed:18216193).Curated1
Sequence conflicti1031I → T in AAI70552 (Ref. 2) Curated1
Sequence conflicti1431V → G in ABX60543 (PubMed:18216193).Curated1
Sequence conflicti1432V → G in AAI70552 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EU275164 mRNA Translation: ABX60543.1
BC170551 mRNA Translation: AAI70551.1
BC170552 mRNA Translation: AAI70552.1

NCBI Reference Sequences

More...
RefSeqi
NP_001106367.1, NM_001112896.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100127346

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:100127346

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU275164 mRNA Translation: ABX60543.1
BC170551 mRNA Translation: AAI70551.1
BC170552 mRNA Translation: AAI70552.1
RefSeqiNP_001106367.1, NM_001112896.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5UOWelectron microscopy4.50B1-834[»]
5UP2electron microscopy6.00B1-834[»]
SMRiB7ZSK1
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

GeneIDi100127346
KEGGixla:100127346

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
100127346
XenbaseiXB-GENE-1021446, grin2a.L

Phylogenomic databases

OrthoDBi188544at2759

Family and domain databases

InterProiView protein in InterPro
IPR001828, ANF_lig-bd_rcpt
IPR019594, Glu/Gly-bd
IPR001508, Iono_rcpt_met
IPR001320, Iontro_rcpt
IPR018884, NMDAR2_C
IPR028082, Peripla_BP_I
PfamiView protein in Pfam
PF01094, ANF_receptor, 1 hit
PF00060, Lig_chan, 1 hit
PF10613, Lig_chan-Glu_bd, 1 hit
PF10565, NMDAR2_C, 1 hit
PRINTSiPR00177, NMDARECEPTOR
SMARTiView protein in SMART
SM00918, Lig_chan-Glu_bd, 1 hit
SM00079, PBPe, 1 hit
SUPFAMiSSF53822, SSF53822, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNMDE1_XENLA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B7ZSK1
Secondary accession number(s): A9QW72, B7ZSK2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2017
Last sequence update: March 3, 2009
Last modified: June 2, 2021
This is version 57 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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