PLPR4_MOUSE
ID PLPR4_MOUSE Reviewed; 766 AA.
AC Q7TME0; B2RQ15; Q6ZQA8; Q8BV73; Q8BXK2; Q8R3R6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phospholipid phosphatase-related protein type 4 {ECO:0000250|UniProtKB:Q7Z2D5};
DE AltName: Full=Brain-specific phosphatidic acid phosphatase-like protein 1 {ECO:0000250|UniProtKB:Q7Z2D5};
DE AltName: Full=Inactive 2-lysophosphatidate phosphatase PLPPR4 {ECO:0000305|PubMed:19766573};
DE AltName: Full=Lipid phosphate phosphatase-related protein type 4 {ECO:0000250|UniProtKB:Q7Z2D5};
DE AltName: Full=Plasticity-related gene 1 protein {ECO:0000305|PubMed:12730698};
DE Short=PRG-1 {ECO:0000303|PubMed:12730698};
GN Name=Plppr4 {ECO:0000312|MGI:MGI:106530};
GN Synonyms=D3Bwg0562e {ECO:0000303|PubMed:15489334},
GN Kiaa0455 {ECO:0000303|PubMed:14621295},
GN Lppr4 {ECO:0000250|UniProtKB:Q7Z2D5}, Php1 {ECO:0000250|UniProtKB:Q7Z2D5},
GN Prg1 {ECO:0000303|PubMed:12730698};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CAUTION.
RC STRAIN=129/J, and BALB/cJ; TISSUE=Brain, and Testis;
RX PubMed=12730698; DOI=10.1038/nn1052;
RA Braeuer A.U., Savaskan N.E., Kuehn H., Prehn S., Ninnemann O., Nitsch R.;
RT "A new phospholipid phosphatase, PRG-1, is involved in axon growth and
RT regenerative sprouting.";
RL Nat. Neurosci. 6:572-578(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-347; SER-439; SER-462
RP AND SER-608, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP CAUTION, AND MUTAGENESIS OF HIS-253.
RX PubMed=19766573; DOI=10.1016/j.cell.2009.06.050;
RA Trimbuch T., Beed P., Vogt J., Schuchmann S., Maier N., Kintscher M.,
RA Breustedt J., Schuelke M., Streu N., Kieselmann O., Brunk I., Laube G.,
RA Strauss U., Battefeld A., Wende H., Birchmeier C., Wiese S., Sendtner M.,
RA Kawabe H., Kishimoto-Suga M., Brose N., Baumgart J., Geist B., Aoki J.,
RA Savaskan N.E., Braeuer A.U., Chun J., Ninnemann O., Schmitz D., Nitsch R.;
RT "Synaptic PRG-1 modulates excitatory transmission via lipid phosphate-
RT mediated signaling.";
RL Cell 138:1222-1235(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-346 AND SER-347,
RP DISRUPTION PHENOTYPE, AND GLYCOSYLATION.
RX PubMed=26671989; DOI=10.15252/emmm.201505677;
RA Vogt J., Yang J.W., Mobascher A., Cheng J., Li Y., Liu X., Baumgart J.,
RA Thalman C., Kirischuk S., Unichenko P., Horta G., Radyushkin K., Stroh A.,
RA Richers S., Sahragard N., Distler U., Tenzer S., Qiao L., Lieb K.,
RA Tuescher O., Binder H., Ferreiros N., Tegeder I., Morris A.J., Gropa S.,
RA Nuernberg P., Toliat M.R., Winterer G., Luhmann H.J., Huai J., Nitsch R.;
RT "Molecular cause and functional impact of altered synaptic lipid signaling
RT due to a prg-1 gene SNP.";
RL EMBO Mol. Med. 8:25-38(2016).
CC -!- FUNCTION: Postsynaptic density membrane protein that indirectly
CC regulates glutamatergic synaptic transmission through lysophosphatidic
CC acid (LPA)-mediated signaling pathways (PubMed:19766573). Binds
CC lysophosphatidic acid (LPA) and mediates its internalization into cells
CC (PubMed:26671989). Could act as receptor or a transporter of this lipid
CC at the post-synaptic membrane (PubMed:19766573, PubMed:26671989).
CC Modulates lysophosphatidic acid (LPA) activity in neuron axonal
CC outgrowth during development by attenuating phospholipid-induced axon
CC collapse (By similarity). {ECO:0000250|UniProtKB:Q7TMB7,
CC ECO:0000269|PubMed:19766573, ECO:0000269|PubMed:26671989}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density membrane
CC {ECO:0000269|PubMed:19766573, ECO:0000269|PubMed:26671989}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Brain-specific, it is exclusively expressed in
CC neurons (at protein level). {ECO:0000269|PubMed:19766573}.
CC -!- PTM: O-glycosylated. Probably at Ser-347.
CC {ECO:0000269|PubMed:26671989}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice lacking Plppr4 are viable but show
CC a severe alteration of synaptic transmission leading to juvenile
CC epileptic seizures (PubMed:19766573). Excitatory transmission in CA1
CC pyramidal neurons is significantly increased (PubMed:19766573). It is
CC associated with transiently reduced weight during development, a
CC reduction in brain size and higher mortality 3 to 4 weeks after birth
CC (PubMed:19766573). Heterozygous knockout mice, show loss of
CC somatosensory filter function and altered resilience during stress-
CC related behaviors (PubMed:26671989). {ECO:0000269|PubMed:19766573,
CC ECO:0000269|PubMed:26671989}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
CC -!- CAUTION: Originally described as a 2-lysophosphatidate/LPA phosphatase
CC (PubMed:12730698). However, following studies suggested it does not
CC have such activity or only a residual one (PubMed:19766573). This is
CC further supported by the fact that the phosphatase sequence motifs as
CC well as the His residue acting as a nucleophile in active phosphatases
CC of the PA-phosphatase related phosphoesterase family are not conserved
CC (PubMed:19766573). {ECO:0000269|PubMed:12730698,
CC ECO:0000269|PubMed:19766573}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC97959.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY266266; AAP41099.1; -; mRNA.
DR EMBL; AY266267; AAP41100.1; -; mRNA.
DR EMBL; AF541279; AAP57768.1; -; mRNA.
DR EMBL; AK129149; BAC97959.1; ALT_INIT; mRNA.
DR EMBL; AK046782; BAC32865.1; -; mRNA.
DR EMBL; AK079635; BAC37711.1; ALT_INIT; mRNA.
DR EMBL; BC024711; AAH24711.1; -; mRNA.
DR EMBL; BC137701; AAI37702.1; -; mRNA.
DR EMBL; BC137702; AAI37703.1; -; mRNA.
DR CCDS; CCDS17795.1; -.
DR RefSeq; NP_808332.3; NM_177664.5.
DR AlphaFoldDB; Q7TME0; -.
DR BioGRID; 230903; 5.
DR IntAct; Q7TME0; 1.
DR STRING; 10090.ENSMUSP00000052306; -.
DR GlyGen; Q7TME0; 9 sites.
DR iPTMnet; Q7TME0; -.
DR PhosphoSitePlus; Q7TME0; -.
DR SwissPalm; Q7TME0; -.
DR MaxQB; Q7TME0; -.
DR PaxDb; Q7TME0; -.
DR PeptideAtlas; Q7TME0; -.
DR PRIDE; Q7TME0; -.
DR ProteomicsDB; 288264; -.
DR Antibodypedia; 1575; 107 antibodies from 25 providers.
DR DNASU; 229791; -.
DR Ensembl; ENSMUST00000061071; ENSMUSP00000052306; ENSMUSG00000044667.
DR GeneID; 229791; -.
DR KEGG; mmu:229791; -.
DR UCSC; uc008rcz.2; mouse.
DR CTD; 9890; -.
DR MGI; MGI:106530; Plppr4.
DR VEuPathDB; HostDB:ENSMUSG00000044667; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000156181; -.
DR HOGENOM; CLU_021458_8_0_1; -.
DR InParanoid; Q7TME0; -.
DR OMA; METEPGQ; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q7TME0; -.
DR TreeFam; TF316040; -.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 229791; 3 hits in 41 CRISPR screens.
DR ChiTaRS; Plppr4; mouse.
DR PRO; PR:Q7TME0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TME0; protein.
DR Bgee; ENSMUSG00000044667; Expressed in dorsal striatum and 135 other tissues.
DR ExpressionAtlas; Q7TME0; baseline and differential.
DR Genevisible; Q7TME0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; ISO:MGI.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISO:MGI.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0140354; P:lipid import into cell; IMP:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; ISO:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR InterPro; IPR028684; PLPPR4.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF13; PTHR10165:SF13; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..766
FT /note="Phospholipid phosphatase-related protein type 4"
FT /id="PRO_0000317437"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 454..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TMB7"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TMB7"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
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 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 253
FT /note="H->Q: Loss of function in regulation of
FT glutamatergic synaptic transmission."
FT /evidence="ECO:0000269|PubMed:19766573"
FT MUTAGEN 346
FT /note="R->T: No effect on localization. Decreased O-
FT glycosylation. Loss of function in LPA internalization into
FT cells. Loss of function in regulation of glutamatergic
FT synaptic transmission."
FT /evidence="ECO:0000269|PubMed:26671989"
FT MUTAGEN 347
FT /note="S->A,D: Loss of function in LPA import into cell."
FT /evidence="ECO:0000269|PubMed:26671989"
FT CONFLICT 451
FT /note="Q -> R (in Ref. 3; BAC32865)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..496
FT /note="DH -> ED (in Ref. 4; AAH24711)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="G -> S (in Ref. 4; AAH24711)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="Q -> K (in Ref. 3; BAC32865)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="A -> D (in Ref. 1; AAP41099/AAP41100/AAP57768)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="K -> E (in Ref. 3; BAC37711)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="A -> V (in Ref. 1; AAP41099/AAP41100/AAP57768)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="I -> V (in Ref. 3; BAC32865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 83290 MW; 371D9FA1A829B5B1 CRC64;
MQRAGSSGAR GECDISGAGR LRLEQAARLG GRTVHTSPGG GLGARQAAGM SAKERPKGKV
IKDSVTLLPC FYFVELPILA SSVVSLYFLE LTDVFKPVHS GFSCYDRSLS MPYIEPTQEA
IPFLMLLSLA FAGPAITIMV GEGILYCCLS KRRNGAGLEP NINAGGCNFN SFLRRAVRFV
GVHVFGLCST ALITDIIQLS TGYQAPYFLT VCKPNYTSLN VSCKENSYIV EDICSGSDLT
VINSGRKSFP SQHATLAAFA AVYVSMYFNS TLTDSSKLLK PLLVFTFIIC GIICGLTRIT
QYKNHPVDVY CGFLIGGGIA LYLGLYAVGN FLPSEDSMLQ HRDALRSLTD LNQDPSRVLS
AKNGSSGDGI AHTEGILNRN HRDASSLTNL KRANADVEII TPRSPMGKES MVTFSNTLPR
ANTPSVEDPV RRNASIHASM DSARSKQLLT QWKSKNESRK MSLQVMDTEP EGQSPPRSIE
MRSSSEPSRV GVNGDHHVPG NQYLKIQPGT VPGCNNSMPG GPRVSIQSRP GSSQLVHIPE
ETQENISTSP KSSSARAKWL KAAEKTVACN RSNNQPRIMQ VIAMSKQQGV LQSSPKNAEG
STVTCTGSIR YKTLTDHEPS GIVRVEAHPE NNRPIIQIPS STEGEGSGSW KWKAPEKSSL
RQTYELNDLN RDSESCESLK DSFGSGDRKR SNIDSNEHHH HGITTIRVTP VEGSEIGSET
LSVSSSRDST LRRKGNIILI PERSNSPENT RNIFYKGTSP TRAYKD
