NMD3A_RAT
ID NMD3A_RAT Reviewed; 1135 AA.
AC Q9R1M7; O09098; O09155; Q62800; Q63268; Q9Z2H0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 3A;
DE Short=GluN3A;
DE AltName: Full=Glutamate receptor chi-1;
DE AltName: Full=N-methyl-D-aspartate receptor;
DE AltName: Full=N-methyl-D-aspartate receptor subtype 3A;
DE Short=NMDAR3A;
DE Short=NR3A;
DE AltName: Full=NMDAR-L;
DE AltName: Full=NMDAR-L1;
DE Flags: Precursor;
GN Name=Grin3a;
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 2), CHARACTERIZATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain stem, and Spinal cord;
RX PubMed=7472412; DOI=10.1523/jneurosci.15-10-06498.1995;
RA Ciabarra A.M., Sullivan J.M., Gahn L.G., Pecht G., Heinemann S.,
RA Sevarino K.A.;
RT "Cloning and characterization of chi-1: a developmentally regulated member
RT of a novel class of the ionotropic glutamate receptor family.";
RL J. Neurosci. 15:6498-6508(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Forebrain;
RX PubMed=7472413; DOI=10.1523/jneurosci.15-10-06509.1995;
RA Sucher N.J., Akbarian S., Chi C.L., Leclerc C.L., Awobuluyi M.,
RA Deitcher D.L., Wu M.K., Yuan J.P., Jones E.G., Lipton S.A.;
RT "Developmental and regional expression pattern of a novel NMDA receptor-
RT like subunit (NMDAR-L) in the rodent brain.";
RL J. Neurosci. 15:6509-6520(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Perez-Otano I., Contractor A., Schulteis C.T., Gibb A., Heinemann S.F.;
RT "Altered single channel properties of NMDA receptors containing a novel
RT NMDA receptor subunit splice variant, NR3A-2.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 839-1122 (ISOFORMS 1/2), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9891978; DOI=10.1016/s0014-5793(98)01590-7;
RA Sun L., Margolis F.L., Shipley M.T., Lidow M.S.;
RT "Identification of a long variant of mRNA encoding the NR3 subunit of the
RT NMDA receptor: its regional distribution and developmental expression in
RT the rat brain.";
RL FEBS Lett. 441:392-396(1998).
RN [5]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH
RP GRIN1; GRIN2A OR GRIN2B AND PPP2CB, AND INTERACTION WITH PPP2CB.
RX PubMed=11588171; DOI=10.1523/jneurosci.21-20-07985.2001;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
RN [6]
RP CHARACTERIZATION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B.
RX PubMed=11160393; DOI=10.1523/jneurosci.21-04-01228.2001;
RA Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S.,
RA Sucher N.J., Heinemann S.F.;
RT "Assembly with the NR1 subunit is required for surface expression of NR3A-
RT containing NMDA receptors.";
RL J. Neurosci. 21:1228-1237(2001).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B.
RX PubMed=12391275; DOI=10.1124/mol.62.5.1119;
RA Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.;
RT "Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2
RT subunits.";
RL Mol. Pharmacol. 62:1119-1127(2002).
RN [8]
RP CHARACTERIZATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND
RP IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN2A OR GRIN2B.
RX PubMed=11929923; DOI=10.1152/jn.00531.2001;
RA Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
RA Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
RA Lipton S.A.;
RT "Characterization and comparison of the NR3A subunit of the NMDA receptor
RT in recombinant systems and primary cortical neurons.";
RL J. Neurophysiol. 87:2052-2063(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH GIT1.
RX PubMed=24297929; DOI=10.1073/pnas.1312211110;
RA Fiuza M., Gonzalez-Gonzalez I., Perez-Otano I.;
RT "GluN3A expression restricts spine maturation via inhibition of GIT1/Rac1
RT signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20807-20812(2013).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF 971-TYR--LEU-973 AND 1082-ASN--LEU-1115.
RX PubMed=25009255; DOI=10.1523/jneurosci.5183-13.2014;
RA Kehoe L.A., Bellone C., De Roo M., Zandueta A., Dey P.N., Perez-Otano I.,
RA Muller D.;
RT "GluN3A promotes dendritic spine pruning and destabilization during
RT postnatal development.";
RL J. Neurosci. 34:9213-9221(2014).
CC -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with
CC reduced single-channel conductance, low calcium permeability and low
CC voltage-dependent sensitivity to magnesium. Mediated by glycine. During
CC the development of neural circuits, plays a role in the synaptic
CC refinement period, restricting spine maturation and growth. By
CC competing with GIT1 interaction with ARHGEF7/beta-PIX, may reduce
CC GIT1/ARHGEF7-regulated local activation of RAC1, hence affecting
CC signaling and limiting the maturation and growth of inactive synapses
CC (PubMed:25009255, PubMed:24297929). May also play a role in PPP2CB-
CC NMDAR mediated signaling mechanism. {ECO:0000269|PubMed:24297929,
CC ECO:0000269|PubMed:25009255}.
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon
CC subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A
CC or GRIN3B). Does not form functional homomeric channels. Found in a
CC complex with GRIN1, GRIN2A or GRIN2B and PPP2CB. Probably interacts
CC with PPP2CB. No complex with PPP2CB is detected when NMDARs are
CC stimulated by NMDA. Interacts (via C-terminus) with GIT1, but not with
CC GRIA1/GluA1, nor with synaptophysin/SYP; this interaction competes with
CC GIT1 interaction with ARHGEF7/beta-PIX (PubMed:24297929).
CC {ECO:0000269|PubMed:11160393, ECO:0000269|PubMed:11588171,
CC ECO:0000269|PubMed:11929923, ECO:0000269|PubMed:12391275,
CC ECO:0000269|PubMed:24297929}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11160393,
CC ECO:0000269|PubMed:11588171}; Multi-pass membrane protein. Postsynaptic
CC cell membrane. Postsynaptic density. Note=Enriched in postsynaptic
CC plasma membrane and postsynaptic densities. Requires the presence of
CC GRIN1 to be targeted at the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NR3-long, NR3-l, NR3A-2;
CC IsoId=Q9R1M7-1; Sequence=Displayed;
CC Name=2; Synonyms=NR3-short, NR3-s;
CC IsoId=Q9R1M7-2; Sequence=VSP_011512;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in olfactory
CC bulb, frontal occipital, entorhinal and pyriform cortices, hippocampus,
CC striatum, thalamus, cerebellum and spinal cord.
CC {ECO:0000269|PubMed:7472412, ECO:0000269|PubMed:7472413,
CC ECO:0000269|PubMed:9891978}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 and isoform 2 are expressed in spinal
CC cord, medulla, pons, tegmentum, thalamus and hypothalamus at 15 dpc
CC onwards (PubMed:7472412, PubMed:7472413, PubMed:9891978). In the brain
CC cortex and in the hippocampus, strongly expressed during periods of
CC synapse/spine reorganization at postnatal day 8 (P8) to P15. Expression
CC declines after P25 (at protein level) (PubMed:24297929).
CC {ECO:0000269|PubMed:24297929, ECO:0000269|PubMed:7472412,
CC ECO:0000269|PubMed:7472413, ECO:0000269|PubMed:9891978}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11160393}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR3A/GRIN3A subfamily. {ECO:0000305}.
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DR EMBL; L34938; AAA99501.1; -; mRNA.
DR EMBL; U29873; AAB58957.1; -; mRNA.
DR EMBL; AF073379; AAD41650.1; -; mRNA.
DR EMBL; AF061945; AAD11811.1; -; mRNA.
DR PIR; T31068; T31068.
DR RefSeq; NP_001185512.1; NM_001198583.2. [Q9R1M7-2]
DR RefSeq; NP_612555.1; NM_138546.2. [Q9R1M7-1]
DR PDB; 2RC7; X-ray; 1.58 A; A/B=511-660, A/B=776-915.
DR PDB; 2RC8; X-ray; 1.45 A; A/B=511-660, A/B=776-915.
DR PDB; 2RC9; X-ray; 1.96 A; A/B=511-660, A/B=776-915.
DR PDB; 4KCD; X-ray; 1.68 A; A/B=511-660, A/B=776-915.
DR PDBsum; 2RC7; -.
DR PDBsum; 2RC8; -.
DR PDBsum; 2RC9; -.
DR PDBsum; 4KCD; -.
DR AlphaFoldDB; Q9R1M7; -.
DR SMR; Q9R1M7; -.
DR BioGRID; 251320; 2.
DR CORUM; Q9R1M7; -.
DR IntAct; Q9R1M7; 2.
DR STRING; 10116.ENSRNOP00000007957; -.
DR BindingDB; Q9R1M7; -.
DR ChEMBL; CHEMBL342; -.
DR DrugCentral; Q9R1M7; -.
DR GlyGen; Q9R1M7; 11 sites.
DR iPTMnet; Q9R1M7; -.
DR PhosphoSitePlus; Q9R1M7; -.
DR PaxDb; Q9R1M7; -.
DR ABCD; Q9R1M7; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000007957; ENSRNOP00000007957; ENSRNOG00000005723. [Q9R1M7-1]
DR GeneID; 191573; -.
DR KEGG; rno:191573; -.
DR UCSC; RGD:621704; rat. [Q9R1M7-1]
DR CTD; 116443; -.
DR RGD; 621704; Grin3a.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000158571; -.
DR InParanoid; Q9R1M7; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q9R1M7; -.
DR TreeFam; TF314731; -.
DR Reactome; R-RNO-9609736; Assembly and cell surface presentation of NMDA receptors.
DR EvolutionaryTrace; Q9R1M7; -.
DR PRO; PR:Q9R1M7; -.
DR Proteomes; UP000002494; Chromosome 5.
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:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO: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:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
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; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; IDA:UniProtKB.
DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0048511; P:rhythmic process; IDA: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; Coiled coil;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1135
FT /note="Glutamate receptor ionotropic, NMDA 3A"
FT /id="PRO_0000011569"
FT TOPO_DOM 24..674
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 770..930
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 931..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 60..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..987
FT /note="PPP2CB binding site"
FT REGION 1082..1115
FT /note="GIT1-binding"
FT /evidence="ECO:0000269|PubMed:24297929"
FT COILED 1080..1129
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1003..1022
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7472412,
FT ECO:0000303|PubMed:7472413"
FT /id="VSP_011512"
FT MUTAGEN 971..973
FT /note="YWL->AAA: Endocytosis-deficient. When transfected in
FT pyramidal neurons transfected, increases the rate of spine
FT elimination and reduction in the stability of preexisting
FT spines, compared to the wild-type protein. No effect on
FT spine growth rate."
FT /evidence="ECO:0000269|PubMed:25009255"
FT MUTAGEN 1082..1115
FT /note="Missing: When expressed in pyramidal neurons,
FT increases spine stability and reduces spine elimination."
FT /evidence="ECO:0000269|PubMed:25009255"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:2RC8"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 551..562
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 573..578
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 579..591
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 593..599
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 615..621
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 648..658
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 783..786
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 801..809
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 811..817
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 825..833
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 840..845
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 846..854
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 857..859
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 861..863
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 868..873
FT /evidence="ECO:0007829|PDB:2RC8"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:4KCD"
FT HELIX 883..896
FT /evidence="ECO:0007829|PDB:2RC8"
FT HELIX 899..907
FT /evidence="ECO:0007829|PDB:2RC8"
SQ SEQUENCE 1135 AA; 127607 MW; 8EC1FEEAE50AB237 CRC64;
MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT
APRAASRAQE GGRAGAQRDD PESGTWRPPA PSQGARWLGS ALHGRGPPGS RKLGEGAGAE
TLWPRDALLF AVENLNRVEG LLPYNLSLEV VMAIEAGLGD LPLMPFSSPS SPWSSDPFSF
LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSSVLHIPV LSIVRHEFPR ESQNPLHLQL
SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTENNSKFH LESVINITAN
LSSTKDLLSF LQVQMDNIRN STPTMVMFGC DMDSIRQIFE MSTQFGLSPP ELHWVLGDSQ
NVEELRTEGL PLGLIAHGKT TQSVFEYYVQ DAMELVARAV ATATMIQPEL ALLPSTMNCM
DVKTTNLTSG QYLSRFLANT TFRGLSGSIK VKGSTIISSE NNFFIWNLQH DPMGKPMWTR
LGSWQGGRIV MDSGIWPEQA QRHKTHFQHP NKLHLRVVTL IEHPFVFTRE VDDEGLCPAG
QLCLDPMTND SSMLDRLFSS LHSSNDTVPI KFKKCCYGYC IDLLEQLAED MNFDFDLYIV
GDGKYGAWKN GHWTGLVGDL LSGTANMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR
DTAAPIGAFM WPLHWTMWLG IFVALHITAI FLTLYEWKSP FGMTPKGRNR NKVFSFSSAL
NVCYALLFGR TAAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI
HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVQ YLKNDPEKLD
AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTSNISEL ISQYKSHGFM
DVLHDKWYKV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVHRLLL
PRIKNKSKLQ YWLHTSQRFH RALNTSFVEE KQPRSKTKRV EKSRWRRWTC KTEGDSELSL
FPRSNLGPQQ LMVWNTSNLS HDNQRKYIFN DEEGQNQLGT QAHQDIPLPQ RRRELPASLT
TNGKADSLNV TRSSVIQELS ELEKQIQVIR QELQLAVSRK TELEEYQKTN RTCES
