NMDE4_RAT
ID NMDE4_RAT Reviewed; 1323 AA.
AC Q62645; Q63381; Q63382; Q63729; Q63730;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2D;
DE Short=GluN2D;
DE AltName: Full=Glutamate [NMDA] receptor subunit epsilon-4;
DE AltName: Full=N-methyl D-aspartate receptor subtype 2D;
DE Short=NMDAR2D;
DE Short=NR2D;
DE Flags: Precursor;
GN Name=Grin2d; Synonyms=GluN2D;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1265-1356 (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Forebrain;
RX PubMed=8428958; DOI=10.1016/s0021-9258(18)53849-7;
RA Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H., Yokoi M.,
RA Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
RT "Molecular characterization of the family of the N-methyl-D-aspartate
RT receptor subunits.";
RL J. Biol. Chem. 268:2836-2843(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7512349; DOI=10.1016/0896-6273(94)90210-0;
RA Monyer H., Burnashev N., Laurie D.J., Sakmann B., Seeburg P.H.;
RT "Developmental and regional expression in the rat brain and functional
RT properties of four NMDA receptors.";
RL Neuron 12:529-540(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Boulter J., Pecht G.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH DLG4.
RX PubMed=7569905; DOI=10.1126/science.7569905;
RA Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.;
RT "Domain interaction between NMDA receptor subunits and the postsynaptic
RT density protein PSD-95.";
RL Science 269:1737-1740(1995).
RN [5]
RP INTERACTION WITH PATJ.
RX PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 424-827 IN COMPLEXES WITH
RP GLUTAMATE AND N-METHYL-D-ASPARTATE, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DISULFIDE BONDS.
RX PubMed=21522138; DOI=10.1038/ncomms1295;
RA Vance K.M., Simorowski N., Traynelis S.F., Furukawa H.;
RT "Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors.";
RL Nat. Commun. 2:294-294(2011).
RN [7] {ECO:0007744|PDB:4JWY}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 424-564 AND 632-825 IN COMPLEX
RP WITH GRIN1, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=23625947; DOI=10.1124/mol.113.085803;
RA Hansen K.B., Tajima N., Risgaard R., Perszyk R.E., Jorgensen L.,
RA Vance K.M., Ogden K.K., Clausen R.P., Furukawa H., Traynelis S.F.;
RT "Structural determinants of agonist efficacy at the glutamate binding site
RT of N-methyl-D-aspartate receptors.";
RL Mol. Pharmacol. 84:114-127(2013).
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+)
CC (PubMed:7512349, PubMed:21522138, PubMed:23625947). Sensitivity to
CC glutamate and channel kinetics depend on the subunit composition
CC (PubMed:7512349, PubMed:23625947). {ECO:0000269|PubMed:21522138,
CC ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:7512349, ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of
CC two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B,
CC GRIN2C or GRIN2D) (in vitro) (PubMed:21522138, PubMed:23625947). In
CC vivo, the subunit composition may depend on the expression levels of
CC the different subunits (Probable). Interacts with PDZ domains of PATJ
CC and DLG4 (PubMed:7569905, PubMed:9647694).
CC {ECO:0000269|PubMed:21522138, ECO:0000269|PubMed:23625947,
CC ECO:0000269|PubMed:7569905, ECO:0000269|PubMed:9647694, ECO:0000305}.
CC -!- INTERACTION:
CC Q62645; Q63ZW7: Patj; Xeno; NbExp=3; IntAct=EBI-631067, EBI-8366894;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21522138,
CC ECO:0000269|PubMed:23625947, ECO:0000269|PubMed:7512349}; Multi-pass
CC membrane protein {ECO:0000305}. Postsynaptic cell membrane; Multi-pass
CC membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q62645-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q62645-2; Sequence=VSP_000136;
CC -!- TISSUE SPECIFICITY: Expressed in brain, mainly in the subcortical
CC region.
CC -!- DEVELOPMENTAL STAGE: Already detected in embryonic stages, peaks at
CC postnatal day 7, and decreases thereafter to adult levels.
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000250|UniProtKB:Q00960}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2D/GRIN2D subfamily. {ECO:0000305}.
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DR EMBL; D13213; BAA02500.1; -; mRNA.
DR EMBL; D13214; BAA02501.1; -; mRNA.
DR EMBL; L31611; AAC37646.1; -; mRNA.
DR EMBL; L31612; AAC37647.1; -; mRNA.
DR EMBL; U08260; AAA17833.1; -; mRNA.
DR PIR; I78557; I78557.
DR RefSeq; NP_073634.1; NM_022797.1. [Q62645-1]
DR RefSeq; XP_008757539.1; XM_008759317.2. [Q62645-2]
DR PDB; 3OEK; X-ray; 1.90 A; A=424-564, A=686-827.
DR PDB; 3OEL; X-ray; 1.90 A; A=424-564, A=686-827.
DR PDB; 3OEM; X-ray; 1.90 A; A=424-564, A=686-827.
DR PDB; 3OEN; X-ray; 1.80 A; A=424-564, A=686-827.
DR PDB; 4JWY; X-ray; 2.00 A; A=424-564, A=686-827.
DR PDBsum; 3OEK; -.
DR PDBsum; 3OEL; -.
DR PDBsum; 3OEM; -.
DR PDBsum; 3OEN; -.
DR PDBsum; 4JWY; -.
DR AlphaFoldDB; Q62645; -.
DR SMR; Q62645; -.
DR BioGRID; 246577; 3.
DR ComplexPortal; CPX-288; NMDA receptor complex, GluN1-GluN2D.
DR IntAct; Q62645; 4.
DR MINT; Q62645; -.
DR STRING; 10116.ENSRNOP00000028615; -.
DR BindingDB; Q62645; -.
DR ChEMBL; CHEMBL303; -.
DR DrugCentral; Q62645; -.
DR GuidetoPHARMACOLOGY; 459; -.
DR GlyGen; Q62645; 7 sites.
DR iPTMnet; Q62645; -.
DR PhosphoSitePlus; Q62645; -.
DR PaxDb; Q62645; -.
DR PRIDE; Q62645; -.
DR Ensembl; ENSRNOT00000028615; ENSRNOP00000028615; ENSRNOG00000021063. [Q62645-1]
DR GeneID; 24412; -.
DR KEGG; rno:24412; -.
DR UCSC; RGD:2740; rat. [Q62645-1]
DR CTD; 2906; -.
DR RGD; 2740; Grin2d.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000159109; -.
DR HOGENOM; CLU_002039_3_1_1; -.
DR InParanoid; Q62645; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q62645; -.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-RNO-9609736; Assembly and cell surface presentation of NMDA receptors.
DR EvolutionaryTrace; Q62645; -.
DR PRO; PR:Q62645; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021063; Expressed in testis and 13 other tissues.
DR ExpressionAtlas; Q62645; baseline and differential.
DR Genevisible; Q62645; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:RGD.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IC:ComplexPortal.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; IDA:RGD.
DR GO; GO:0016595; F:glutamate binding; IMP:RGD.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042165; F:neurotransmitter binding; IMP:RGD.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IBA:GO_Central.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:ComplexPortal.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:ComplexPortal.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IC:ComplexPortal.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:RGD.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Methylation; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1323
FT /note="Glutamate receptor ionotropic, NMDA 2D"
FT /id="PRO_0000011585"
FT TOPO_DOM 28..581
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 582..600
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 601..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT INTRAMEM 628..647
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 648..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 655..670
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 671..841
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 842..861
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 862..1323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT REGION 628..647
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT REGION 897..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1321..1323
FT /note="PDZ-binding"
FT COMPBIAS 899..930
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1033
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1096
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1243
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 536..538
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21522138,
FT ECO:0007744|PDB:3OEL, ECO:0007744|PDB:3OEN"
FT BINDING 538
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 543
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21522138,
FT ECO:0007744|PDB:3OEL, ECO:0007744|PDB:3OEN"
FT BINDING 714..715
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21522138,
FT ECO:0007744|PDB:3OEL, ECO:0007744|PDB:3OEN"
FT BINDING 756
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21522138,
FT ECO:0007744|PDB:3OEL, ECO:0007744|PDB:3OEN"
FT SITE 639
FT /note="Functional determinant of NMDA receptors"
FT /evidence="ECO:0000250"
FT MOD_RES 1303
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q03391"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03391"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..345
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 452..480
FT /evidence="ECO:0000269|PubMed:21522138"
FT DISULFID 459..481
FT /evidence="ECO:0000269|PubMed:21522138"
FT DISULFID 770..825
FT /evidence="ECO:0000269|PubMed:21522138"
FT VAR_SEQ 1265..1323
FT /note="CPRAAPTRRLTGPSRHARRCPHAAHWGPPLPTASHRRHRGGDLGTRRGSAHF
FT SSLESEV -> RPCPPHRTGDTGAGTWAHAGALRISPAWSPRYDAAPAPTPTPAAPSVS
FT AGHGPRGRAKWTGPSWVGKDRNGPGRTPPGAASCAPTPFALGEL (in isoform
FT 1)"
FT /evidence="ECO:0000303|PubMed:8428958"
FT /id="VSP_000136"
FT CONFLICT 25
FT /note="A -> V (in Ref. 3; AAA17833)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="P -> Q (in Ref. 3; AAA17833)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="G -> V (in Ref. 2; AAC37646)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="R -> P (in Ref. 2; AAC37646/AAC37647)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="R -> A (in Ref. 2; AAC37646/AAC37647)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="A -> G (in Ref. 3; AAA17833)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="E -> D (in Ref. 3; AAA17833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1253
FT /note="A -> G (in Ref. 3; AAA17833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1266..1267
FT /note="PR -> TT (in Ref. 3; AAA17833)"
FT /evidence="ECO:0000305"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:3OEN"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:3OEN"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:3OEK"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 520..526
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 554..563
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:3OEK"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:3OEK"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:3OEK"
FT HELIX 714..722
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 724..730
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 731..733
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 751..756
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 757..766
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 768..770
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 775..778
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 781..786
FT /evidence="ECO:0007829|PDB:3OEN"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 797..809
FT /evidence="ECO:0007829|PDB:3OEN"
FT HELIX 812..821
FT /evidence="ECO:0007829|PDB:3OEN"
SQ SEQUENCE 1323 AA; 143101 MW; 40F7D60192579564 CRC64;
MRGAGGPRGP RGPAKMLLLL ALACASPFPE EVPGPGAVGG GTGGARPLNV ALVFSGPAYA
AEAARLGPAV AAAVRSPGLD VRPVALVLNG SDPRSLVLQL CDLLSGLRVH GVVFEDDSRA
PAVAPILDFL SAQTSLPIVA VHGGAALVLT PKEKGSTFLQ LGSSTEQQLQ VIFEVLEEYD
WTSFVAVTTR APGHRAFLSY IEVLTDGSLV GWEHRGALTL DPGAGEAVLG AQLRSVSAQI
RLLFCAREEA EPVFRAAEEA GLTGPGYVWF MVGPQLAGGG GSGVPGEPLL LPGGSPLPAG
LFAVRSAGWR DDLARRVAAG VAVVARGAQA LLRDYGFLPE LGHDCRTQNR THRGESLHRY
FMNITWDNRD YSFNEDGFLV NPSLVVISLT RDRTWEVVGS WEQQTLRLKY PLWSRYGRFL
QPVDDTQHLT VATLEERPFV IVEPADPISG TCIRDSVPCR SQLNRTHSPP PDAPRPEKRC
CKGFCIDILK RLAHTIGFSY DLYLVTNGKH GKKIDGVWNG MIGEVFYQRA DMAIGSLTIN
EERSEIVDFS VPFVETGISV MVARSNGTVS PSAFLEPYSP AVWVMMFVMC LTVVAVTVFI
FEYLSPVGYN RSLATGKRPG GSTFTIGKSI WLLWALVFNN SVPVENPRGT TSKIMVLVWA
FFAVIFLASY TANLAAFMIQ EEYVDTVSGL SDRKFQRPQE QYPPLKFGTV PNGSTEKNIR
SNYPDMHSYM VRYNQPRVEE ALTQLKAGKL DAFIYDAAVL NYMARKDEGC KLVTIGSGKV
FATTGYGIAL HKGSRWKRPI DLALLQFLGD DEIEMLERLW LSGICHNDKI EVMSSKLDID
NMAGVFYMLL VAMGLSLLVF AWEHLVYWRL RHCLGPTHRM DFLLAFSRGM YSCCSAEAAP
PPAKPPPPPQ PLPSPAYPAA RPPPGPAPFV PRERAAADRW RRAKGTGPPG GAAIADGFHR
YYGPIEPQGL GLGEARAAPR GAAGRPLSPP TTQPPQKPPP SYFAIVREQE PTEPPAGAFP
GFPSPPAPPA AAAAAVGPPL CRLAFEDESP PAPSRWPRSD PESQPLLGGG AGGPSAGAPT
APPPRRAAPP PCAYLDLEPS PSDSEDSESL GGASLGGLEP WWFADFPYPY AERLGPPPGR
YWSVDKLGGW RAGSWDYLPP RGGPAWHCRH CASLELLPPP RHLSCSHDGL DGGWWAPPPP
PWAAGPPPRR RARCGCPRPH PHRPRASHRA PAAAPHHHRH RRAAGGWDFP PPAPTSRSLE
DLSSCPRAAP TRRLTGPSRH ARRCPHAAHW GPPLPTASHR RHRGGDLGTR RGSAHFSSLE
SEV
