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Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) (p135 SynGAP)

 SYGP1_RAT               Reviewed;        1308 AA.
Q9QUH6; O88449; Q9ESK6; Q9ET81; Q9QX02; Q9QX06; Q9QX12;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
18-JUL-2018, entry version 141.
RecName: Full=Ras/Rap GTPase-activating protein SynGAP;
AltName: Full=Neuronal RasGAP;
AltName: Full=Synaptic Ras GTPase-activating protein 1;
Short=Synaptic Ras-GAP 1;
AltName: Full=p135 SynGAP;
Name=Syngap1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
16-276 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1264-1290 (ISOFORM
5), AND PROTEIN SEQUENCE OF 32-47; 242-248; 259-272; 300-321; 325-329;
340-354; 419-429; 588-596; 804-815; 923-940; 968-1002; 1086-1102 AND
1276-1286.
STRAIN=Sprague-Dawley;
PubMed=9620694; DOI=10.1016/S0896-6273(00)80471-7;
Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
"A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by
CaM kinase II.";
Neuron 20:895-904(1998).
[2]
ERRATUM.
Oh J.S., Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
Neuron 33:151-151(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND INTERACTION WITH
DLG3 AND DLG4.
TISSUE=Hippocampus;
PubMed=9581761; DOI=10.1016/S0896-6273(00)81008-9;
Kim J.H., Liao D., Lau L.-F., Huganir R.L.;
"SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90
protein family.";
Neuron 20:683-691(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
STRAIN=Sprague-Dawley;
PubMed=11278737; DOI=10.1074/jbc.M010744200;
Li W., Okano A., Tian Q.B., Nakayama K., Furihata T., Nawa H.,
Suzuki T.;
"Characterization of a novel synGAP isoform, synGAP-beta.";
J. Biol. Chem. 276:21417-21424(2001).
[5]
INTERACTION WITH MPDZ; DLG4; CAMK2A AND CAMK2B, PHOSPHORYLATION, AND
FUNCTION.
PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
"SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase
activity and NMDA receptor-dependent synaptic AMPA receptor
potentiation.";
Neuron 43:563-574(2004).
[6]
FUNCTION.
PubMed=15500970; DOI=10.1016/j.neulet.2004.08.044;
Yang S.-N., Huang C.-B., Yang C.-H., Lai M.-C., Chen W.-F.,
Wang C.-L., Wu C.-L., Huang L.-T.;
"Impaired SynGAP expression and long-term spatial learning and memory
in hippocampal CA1 area from rats previously exposed to perinatal
hypoxia-induced insults: beneficial effects of A68930.";
Neurosci. Lett. 371:73-78(2004).
[7]
INTERACTION WITH KLHL17.
PubMed=16054660; DOI=10.1016/j.neuropharm.2005.05.022;
Chen Y., Li M.;
"Interactions between CAP70 and actinfilin are important for integrity
of actin cytoskeleton structures in neurons.";
Neuropharmacology 49:1026-1041(2005).
[8]
TISSUE SPECIFICITY.
PubMed=16507876; DOI=10.1074/mcp.D500009-MCP200;
Cheng D., Hoogenraad C.C., Rush J., Ramm E., Schlager M.A.,
Duong D.M., Xu P., Wijayawardana S.R., Hanfelt J., Nakagawa T.,
Sheng M., Peng J.;
"Relative and absolute quantification of postsynaptic density proteome
isolated from rat forebrain and cerebellum.";
Mol. Cell. Proteomics 5:1158-1170(2006).
[9]
FUNCTION.
PubMed=16537406; DOI=10.1073/pnas.0600084103;
Rumbaugh G., Adams J.P., Kim J.H., Huganir R.L.;
"SynGAP regulates synaptic strength and mitogen-activated protein
kinases in cultured neurons.";
Proc. Natl. Acad. Sci. U.S.A. 103:4344-4351(2006).
[10]
PHOSPHORYLATION AT SER-379; SER-385; SER-449; SER-466; SER-836;
SER-840; SER-842 AND SER-895, AND MUTAGENESIS OF SER-385; SER-449;
SER-840 AND SER-842.
PubMed=21382555; DOI=10.1016/j.neuron.2011.02.004;
Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S.,
Pak D.T.;
"Requirement for Plk2 in orchestrated ras and rap signaling,
homeostatic structural plasticity, and memory.";
Neuron 69:957-973(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-371; SER-752;
SER-766; SER-780; SER-892; SER-895; SER-898; SER-1114; SER-1118;
SER-1121 AND SER-1204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 252-734, FUNCTION, DOMAIN C2,
AND MUTAGENESIS OF ARG-485 AND ASN-487.
PubMed=18323856; DOI=10.1038/embor.2008.20;
Pena V., Hothorn M., Eberth A., Kaschau N., Parret A., Gremer L.,
Bonneau F., Ahmadian M.R., Scheffzek K.;
"The C2 domain of SynGAP is essential for stimulation of the Rap
GTPase reaction.";
EMBO Rep. 9:350-355(2008).
-!- FUNCTION: Major constituent of the PSD essential for postsynaptic
signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of
the NMDAR signaling complex in excitatory synapses, it may play a
role in NMDAR-dependent control of AMPAR potentiation, AMPAR
membrane trafficking and synaptic plasticity. Regulates AMPAR-
mediated miniature excitatory postsynaptic currents. Exhibits dual
GTPase-activating specificity for Ras and Rap. May be involved in
certain forms of brain injury, leading to long-term learning and
memory deficits. {ECO:0000269|PubMed:15312654,
ECO:0000269|PubMed:15500970, ECO:0000269|PubMed:16537406,
ECO:0000269|PubMed:18323856}.
-!- SUBUNIT: Isoforms containing the PDZ-binding domain associate with
DLG4 and DLG3 to form the PSD protein complex colocalized with
GRIN2B at synapses. Interacts with MPDZ, KLHL17 CAMK2A and CAMK2B.
{ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:16054660,
ECO:0000269|PubMed:9581761}.
-!- INTERACTION:
P31016:Dlg4; NbExp=3; IntAct=EBI-2310349, EBI-375655;
Q8K430:Klhl17; NbExp=2; IntAct=EBI-2310349, EBI-7713653;
Q9JJ40:Pdzk1; NbExp=6; IntAct=EBI-2310349, EBI-7713572;
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cell
junction, synapse. Note=Mostly in excitatory glutamatergic
synapses.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9QUH6-1; Sequence=Displayed;
Name=2; Synonyms=SynGAP-a;
IsoId=Q9QUH6-2; Sequence=VSP_026378, VSP_007979;
Name=3; Synonyms=SynGAP-b;
IsoId=Q9QUH6-3; Sequence=VSP_007974;
Name=4; Synonyms=SynGAP-c;
IsoId=Q9QUH6-4; Sequence=VSP_007976, VSP_007980;
Name=5; Synonyms=SynGAP-d, SynGAP-beta;
IsoId=Q9QUH6-5; Sequence=VSP_007975, VSP_007977, VSP_007978;
-!- TISSUE SPECIFICITY: Highly expressed in brain; predominantly in
the cortex, hippocampus and olfactory bulb. Present in the
postsynaptic density of central excitatory synapses.
{ECO:0000269|PubMed:16507876}.
-!- DOMAIN: The PDZ-binding domain interacts with all three PDZ
domains of DGL4. {ECO:0000269|PubMed:18323856}.
-!- DOMAIN: The C2 domain is required for RapGAP activity.
{ECO:0000269|PubMed:18323856}.
-!- PTM: Phosphorylated by CaM-kinase II. Dephosphorylated upon NMDA
receptor activation or SYNGAP1/MPDZ complex disruption.
Phosphorylation by PLK2 promotes its activity.
{ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:21382555}.
-!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator
methionine. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC08071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF048976; AAC08071.1; ALT_INIT; mRNA.
EMBL; AF053938; AAC23491.1; -; mRNA.
EMBL; AF055883; AAC23492.1; -; mRNA.
EMBL; AF058789; AAC63510.2; -; mRNA.
EMBL; AF058790; AAC63511.1; -; mRNA.
EMBL; AF050183; AAC40082.2; -; mRNA.
EMBL; AB016962; BAA74972.1; -; mRNA.
PIR; T13958; T13958.
PIR; T14259; T14259.
PIR; T14270; T14270.
UniGene; Rn.9908; -.
PDB; 3BXJ; X-ray; 3.00 A; A/B=252-734.
PDBsum; 3BXJ; -.
ProteinModelPortal; Q9QUH6; -.
SMR; Q9QUH6; -.
CORUM; Q9QUH6; -.
ELM; Q9QUH6; -.
IntAct; Q9QUH6; 6.
MINT; Q9QUH6; -.
STRING; 10116.ENSRNOP00000044041; -.
ChEMBL; CHEMBL2176804; -.
iPTMnet; Q9QUH6; -.
PhosphoSitePlus; Q9QUH6; -.
PaxDb; Q9QUH6; -.
PRIDE; Q9QUH6; -.
UCSC; RGD:621090; rat. [Q9QUH6-1]
RGD; 621090; Syngap1.
eggNOG; KOG3508; Eukaryota.
eggNOG; ENOG410XPU1; LUCA.
HOVERGEN; HBG006492; -.
InParanoid; Q9QUH6; -.
PhylomeDB; Q9QUH6; -.
EvolutionaryTrace; Q9QUH6; -.
PRO; PR:Q9QUH6; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:CACAO.
GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd13375; PH_SynGAP; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR021887; DUF3498.
InterPro; IPR001849; PH_domain.
InterPro; IPR039360; Ras_GTPase.
InterPro; IPR023152; RasGAP_CS.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR037779; SynGAP_PH.
PANTHER; PTHR10194; PTHR10194; 1.
Pfam; PF00168; C2; 1.
Pfam; PF12004; DUF3498; 1.
Pfam; PF00616; RasGAP; 2.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00323; RasGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Complete proteome;
Direct protein sequencing; GTPase activation; Membrane;
Phosphoprotein; Reference proteome; SH3-binding; Synapse.
CHAIN 1 1308 Ras/Rap GTPase-activating protein SynGAP.
/FTId=PRO_0000056655.
DOMAIN 150 251 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 249 347 C2.
DOMAIN 443 635 Ras-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00167}.
REGION 1197 1308 Interaction with MPDZ.
{ECO:0000269|PubMed:15312654}.
MOTIF 785 815 SH3-binding. {ECO:0000255}.
MOTIF 1305 1308 PDZ-binding. {ECO:0000255}.
MOD_RES 34 34 Phosphotyrosine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 39 39 Phosphotyrosine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 371 371 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 379 379 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 385 385 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 449 449 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 466 466 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 823 823 Phosphoserine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 828 828 Phosphothreonine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 836 836 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 840 840 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 842 842 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:21382555}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 895 895 Phosphoserine; by PLK2.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:21382555}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 985 985 Phosphoserine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1118 1118 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1121 1121 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1165 1165 Phosphoserine.
{ECO:0000250|UniProtKB:F6SEU4}.
MOD_RES 1204 1204 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 1 173 Missing (in isoform 4).
{ECO:0000303|PubMed:9581761}.
/FTId=VSP_007976.
VAR_SEQ 1 121 MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDR
PGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLL
RRTVSVPVEGRPHGEHEYHLGRSRRKSVPGGKQYSMEAA
-> MEYF (in isoform 5).
{ECO:0000303|PubMed:11278737,
ECO:0000303|PubMed:9620694}.
/FTId=VSP_007975.
VAR_SEQ 1 98 MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDR
PGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLL
RRTVSVPVEGRPHGEH -> MGLRPPTPTPSGGSGSGSLPP
PSHRQPLRRRCSSCCFPG (in isoform 3).
{ECO:0000303|PubMed:9581761,
ECO:0000303|PubMed:9620694}.
/FTId=VSP_007974.
VAR_SEQ 1 15 Missing (in isoform 2).
{ECO:0000303|PubMed:9581761}.
/FTId=VSP_026378.
VAR_SEQ 1195 1196 Missing (in isoform 5).
{ECO:0000303|PubMed:11278737,
ECO:0000303|PubMed:9620694}.
/FTId=VSP_007977.
VAR_SEQ 1265 1308 RLMLVEEELRRDHPAMAEPLPEPKKRLLDAQRGSFPPWVQQ
TRV -> SPSLQADAGGGGAAPGPPRHG (in isoform
5). {ECO:0000303|PubMed:11278737,
ECO:0000303|PubMed:9620694}.
/FTId=VSP_007978.
VAR_SEQ 1296 1308 RGSFPPWVQQTRV -> LLIR (in isoform 2).
{ECO:0000303|PubMed:9581761}.
/FTId=VSP_007979.
VAR_SEQ 1296 1308 RGSFPPWVQQTRV -> VERQLPPLGPTNPRVTLAPPWNGL
APPAPPPPPRLQITENGEFRNTADH (in isoform 4).
{ECO:0000303|PubMed:9581761}.
/FTId=VSP_007980.
MUTAGEN 385 385 S->A: Affects stimulation by PLK2.
{ECO:0000269|PubMed:21382555}.
MUTAGEN 449 449 S->A: Affects stimulation by PLK2.
{ECO:0000269|PubMed:21382555}.
MUTAGEN 485 485 R->K: Decreases RapGAP activity by 100-
fold. {ECO:0000269|PubMed:18323856}.
MUTAGEN 485 485 R->P: Abolishes RapGAP activity.
{ECO:0000269|PubMed:18323856}.
MUTAGEN 487 487 N->T: Decreases RapGAP activity by 20-
fold. {ECO:0000269|PubMed:18323856}.
MUTAGEN 840 840 S->A: Blocks the gel mobility shift
induced by PLK2 and affects stimulation
by PLK2. {ECO:0000269|PubMed:21382555}.
MUTAGEN 842 842 S->A: Blocks the gel mobility shift
induced by PLK2.
{ECO:0000269|PubMed:21382555}.
CONFLICT 308 309 WG -> GY (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 316 316 N -> M (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 427 429 HYR -> GQK (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 937 939 DGP -> ADG (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1002 1002 H -> G (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1088 1088 S -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 1277 1277 H -> L (in Ref. 1; AA sequence).
{ECO:0000305}.
STRAND 257 262 {ECO:0000244|PDB:3BXJ}.
STRAND 403 408 {ECO:0000244|PDB:3BXJ}.
HELIX 414 417 {ECO:0000244|PDB:3BXJ}.
HELIX 418 425 {ECO:0000244|PDB:3BXJ}.
HELIX 428 438 {ECO:0000244|PDB:3BXJ}.
HELIX 441 457 {ECO:0000244|PDB:3BXJ}.
HELIX 463 475 {ECO:0000244|PDB:3BXJ}.
STRAND 477 481 {ECO:0000244|PDB:3BXJ}.
STRAND 486 488 {ECO:0000244|PDB:3BXJ}.
HELIX 489 501 {ECO:0000244|PDB:3BXJ}.
HELIX 503 519 {ECO:0000244|PDB:3BXJ}.
TURN 528 530 {ECO:0000244|PDB:3BXJ}.
TURN 533 535 {ECO:0000244|PDB:3BXJ}.
HELIX 536 555 {ECO:0000244|PDB:3BXJ}.
HELIX 556 560 {ECO:0000244|PDB:3BXJ}.
HELIX 563 578 {ECO:0000244|PDB:3BXJ}.
HELIX 582 593 {ECO:0000244|PDB:3BXJ}.
TURN 594 597 {ECO:0000244|PDB:3BXJ}.
HELIX 598 603 {ECO:0000244|PDB:3BXJ}.
TURN 605 609 {ECO:0000244|PDB:3BXJ}.
HELIX 617 634 {ECO:0000244|PDB:3BXJ}.
TURN 642 645 {ECO:0000244|PDB:3BXJ}.
HELIX 647 649 {ECO:0000244|PDB:3BXJ}.
HELIX 650 666 {ECO:0000244|PDB:3BXJ}.
HELIX 685 699 {ECO:0000244|PDB:3BXJ}.
HELIX 700 702 {ECO:0000244|PDB:3BXJ}.
HELIX 705 710 {ECO:0000244|PDB:3BXJ}.
TURN 711 713 {ECO:0000244|PDB:3BXJ}.
HELIX 714 724 {ECO:0000244|PDB:3BXJ}.
SEQUENCE 1308 AA; 144722 MW; CA2536782C8C4DCB CRC64;
MSRSRASIHR GSIPAMSYAP FRDVRGPPMH RTQYVHSPYD RPGWNPRFCI ISGNQLLMLD
EDEIHPLLIR DRRSESSRNK LLRRTVSVPV EGRPHGEHEY HLGRSRRKSV PGGKQYSMEA
APAAPFRPSQ GFLSRRLKSS IKRTKSQPKL DRTSSFRQIL PRFRSADHDR ARLMQSFKES
HSHESLLSPS SAAEALELNL DEDSIIKPVH SSILGQEFCF EVTTSSGTKC FACRSAAERD
KWIENLQRAV KPNKDNSRRV DNVLKLWIIE ARELPPKKRY YCELCLDDML YARTTSKPRS
ASGDTVFWGE HFEFNNLPAV RALRLHLYRD SDKKRKKDKA GYVGLVTVPV ATLAGRHFTE
QWYPVTLPTG SGGSGGMGSG GGGGSGGGSG GKGKGGCPAV RLKARYQTMS ILPMELYKEF
AEYVTNHYRM LCAVLEPALN VKGKEEVASA LVHILQSTGK AKDFLSDMAM SEVDRFMERE
HLIFRENTLA TKAIEEYMRL IGQKYLKDAI GEFIRALYES EENCEVDPIK CTASSLAEHQ
ANLRMCCELA LCKVVNSHCV FPRELKEVFA SWRLRCAERG REDIADRLIS ASLFLRFLCP
AIMSPSLFGL MQEYPDEQTS RTLTLIAKVI QNLANFSKFT SKEDFLGFMN EFLELEWGSM
QQFLYEISNL DTLTNSSSFE GYIDLGRELS TLHALLWEVL PQLSKEALLK LGPLPRLLSD
ISTALRNPNI QRQPSRQSER ARSQPMVLRG PSAEMQGYMM RDLNSSIDLQ SFMARGLNSS
MDMARLPSPT KEKPPPPPPG GGKDLFYVSR PPLARSSPAY CTSSSDITEP EQKMLSVNKS
VSMLDLQGDG PGGRLNSSSV SNLAAVGDLL HSSQASLTAA LGLRPAPAGR LSQGSGSSIT
AAGMRLSQMG VTTDGVPAQQ LRIPLSFQNP LFHMAADGPG PPAGHGGSSG HGPPSSHHHH
HHHHHHRGGE PPGDTFAPFH GYSKSEDLST GVPKPPAASI LHSHSYSDEF GPSGTDFTRR
QLSLQDNLQH MLSPPQITIG PQRPAPSGPG GGSGGGSGGG GGGQPPPLQR GKSQQLTVSA
AQKPRPSSGN LLQSPEPSYG PARPRQQSLS KEGSIGGSGG SGGGGGGGLK PSITKQHSQT
PSTLNPTMPA SERTVAWVSN MPHLSADIES AHIEREEYKL KEYSKSMDES RLDRVKEYEE
EIHSLKERLH MSNRKLEEYE RRLLSQEEQT SKILMQYQAR LEQSEKRLRQ QQVEKDSQIK
SIIGRLMLVE EELRRDHPAM AEPLPEPKKR LLDAQRGSFP PWVQQTRV


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