PRAX_MOUSE
ID PRAX_MOUSE Reviewed; 1391 AA.
AC O55103; O55104;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Periaxin;
GN Name=Prx;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9488714; DOI=10.1074/jbc.273.10.5794;
RA Dytrych L., Sherman D.L., Gillespie C.S., Brophy P.J.;
RT "Two PDZ domain proteins encoded by the murine periaxin gene are the result
RT of alternative intron retention and are differentially targeted in Schwann
RT cells.";
RL J. Biol. Chem. 273:5794-5800(1998).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10671475; DOI=10.1074/jbc.275.7.4537;
RA Sherman D.L., Brophy P.J.;
RT "A tripartite nuclear localization signal in the PDZ-domain protein L-
RT periaxin.";
RL J. Biol. Chem. 275:4537-4540(2000).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10839370; DOI=10.1016/s0896-6273(00)81184-8;
RA Gillespie C.S., Sherman D.L., Fleetwood-Walker S.M., Cottrell D.F.,
RA Tait S., Garry E.M., Wallace V.C., Ure J., Griffiths I.R., Smith A.,
RA Brophy P.J.;
RT "Peripheral demyelination and neuropathic pain behavior in periaxin-
RT deficient mice.";
RL Neuron 26:523-531(2000).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION IN A
RP COMPLEX WITH DRP2; DMD; DAG1 AND UTRN.
RX PubMed=11430802; DOI=10.1016/s0896-6273(01)00327-0;
RA Sherman D.L., Fabrizi C., Gillespie C.S., Brophy P.J.;
RT "Specific disruption of a Schwann cell dystrophin-related protein complex
RT in a demyelinating neuropathy.";
RL Neuron 30:677-687(2001).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15356632; DOI=10.1038/nature02841;
RA Court F.A., Sherman D.L., Pratt T., Garry E.M., Ribchester R.R.,
RA Cottrell D.F., Fleetwood-Walker S.M., Brophy P.J.;
RT "Restricted growth of Schwann cells lacking Cajal bands slows conduction in
RT myelinated nerves.";
RL Nature 431:191-195(2004).
RN [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18205176; DOI=10.1002/glia.20620;
RA Court F.A., Brophy P.J., Ribchester R.R.;
RT "Remodeling of motor nerve terminals in demyelinating axons of periaxin-
RT null mice.";
RL Glia 56:471-479(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; SER-1279; SER-1283;
RP SER-1285; SER-1293; SER-1337 AND SER-1369, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
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 [8]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; BFSP1; BFSP2;
RP ANK2; PLEC; VIM AND SPECTRIN.
RX PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
RA Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.;
RT "Periaxin is required for hexagonal geometry and membrane organization of
RT mature lens fibers.";
RL Dev. Biol. 357:179-190(2011).
RN [9]
RP FUNCTION, AND DOMAIN.
RX PubMed=23022068; DOI=10.1016/j.cub.2012.08.025;
RA Wu L.M., Williams A., Delaney A., Sherman D.L., Brophy P.J.;
RT "Increasing internodal distance in myelinated nerves accelerates nerve
RT conduction to a flat maximum.";
RL Curr. Biol. 22:1957-1961(2012).
RN [10]
RP INTERACTION WITH DRP2, AND FUNCTION.
RX PubMed=22764250; DOI=10.1523/jneurosci.1220-12.2012;
RA Sherman D.L., Wu L.M., Grove M., Gillespie C.S., Brophy P.J.;
RT "Drp2 and periaxin form Cajal bands with dystroglycan but have distinct
RT roles in Schwann cell growth.";
RL J. Neurosci. 32:9419-9428(2012).
CC -!- FUNCTION: Scaffolding protein that functions as part of a dystroglycan
CC complex in Schwann cells, and as part of EZR and AHNAK-containing
CC complexes in eye lens fiber cells (PubMed:11430802, PubMed:21745462,
CC PubMed:22764250). Required for the maintenance of the peripheral myelin
CC sheath that is essential for normal transmission of nerve impulses and
CC normal perception of sensory stimuli (PubMed:10839370). Required for
CC normal transport of MBP mRNA from the perinuclear to the paranodal
CC regions (PubMed:15356632). Required for normal remyelination after
CC nerve injury (PubMed:10839370). Required for normal elongation of
CC Schwann cells and normal length of the internodes between the nodes of
CC Ranvier. The demyelinated nodes of Ranvier permit saltatory
CC transmission of nerve impulses; shorter internodes cause slower
CC transmission of nerve impulses (PubMed:15356632, PubMed:23022068).
CC Required for the formation of appositions between the abaxonal surface
CC of the myelin sheath and the Schwann cell plasma membrane; the Schwann
CC cell cytoplasm is restricted to regions between these appositions
CC (PubMed:15356632, PubMed:23022068). Required for the formation of Cajal
CC bands and of Schmidt-Lanterman incisures that correspond to short,
CC cytoplasm-filled regions on myelinated nerves (PubMed:23022068,
CC PubMed:22764250). Recruits DRP2 to the Schwann cell plasma membrane
CC (PubMed:11430802, PubMed:23022068, PubMed:22764250). Required for
CC normal protein composition of the eye lens fiber cell plasma membrane
CC and normal eye lens fiber cell morphology (PubMed:21745462).
CC {ECO:0000269|PubMed:10839370, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:15356632, ECO:0000269|PubMed:22764250,
CC ECO:0000269|PubMed:23022068}.
CC -!- SUBUNIT: Homodimer (via PDZ domain) (By similarity). Interacts with
CC SCN10A. Found in a complex with SCN10A (By similarity). Interacts with
CC DRP2 (PubMed:22764250). Identified in a dystroglycan complex that
CC contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802).
CC Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By
CC similarity). Identified in a complex with EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, VIM and spectrin (PubMed:21745462).
CC {ECO:0000250|UniProtKB:E1BM58, ECO:0000250|UniProtKB:Q63425,
CC ECO:0000250|UniProtKB:Q9BXM0, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:22764250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21745462}. Cell
CC junction {ECO:0000269|PubMed:21745462}. Note=Colocalizes with ACTB at
CC tricellular junctions between eye lens fiber cells.
CC {ECO:0000269|PubMed:21745462}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:9488714}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus
CC {ECO:0000269|PubMed:10671475}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BXM0}. Note=Detected in the Schwann cell
CC nucleus prior to the onset of myelination (PubMed:10671475). Detected
CC in Schwann cells at periaxonal myelin membranes. Associated with the
CC cell membrane during myelination (PubMed:9488714).
CC {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:9488714}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:10671475, ECO:0000269|PubMed:9488714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-periaxin;
CC IsoId=O55103-1; Sequence=Displayed;
CC Name=2; Synonyms=S-periaxin;
CC IsoId=O55103-2; Sequence=VSP_004366, VSP_004367;
CC -!- TISSUE SPECIFICITY: Detected in myelinating Schwann cells in
CC intramuscular nerves in triangularis sterni (PubMed:18205176). Detected
CC in sciatic nerve (PubMed:11430802). Detected in eye lens fiber cells
CC (PubMed:21745462). Isoform 1 is detected in myelinating Schwann cells
CC in sciatic nerve (PubMed:9488714, PubMed:10671475, PubMed:10839370).
CC Isoform 2 is detected in myelinating Schwann cells in sciatic nerve (at
CC protein level) (PubMed:9488714, PubMed:10839370). Detected in sciatic
CC nerve (PubMed:9488714, PubMed:10839370). {ECO:0000269|PubMed:10671475,
CC ECO:0000269|PubMed:10839370, ECO:0000269|PubMed:11430802,
CC ECO:0000269|PubMed:18205176, ECO:0000269|PubMed:21745462,
CC ECO:0000269|PubMed:9488714}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic eye lens; levels increase
CC steadily from 10.5 dpc onto birth and continue to increase during the
CC first three weeks after birth. {ECO:0000269|PubMed:21745462}.
CC -!- DOMAIN: Has a remarkable domain of repetitive pentameric units
CC sometimes followed by a tripeptide spacer, it may separate two
CC functional basic and acidic domains. {ECO:0000305}.
CC -!- DOMAIN: The PDZ domain contains the signal for export from the nucleus
CC (By similarity). The N-terminal region including the PDZ domain is
CC required for the formation of Cajal bands on myelinated nerves.
CC {ECO:0000250|UniProtKB:Q9BXM0, ECO:0000269|PubMed:23022068}.
CC -!- DOMAIN: The Arg/Lys-rich basic domain functions as a tripartite nuclear
CC localization signal. {ECO:0000250|UniProtKB:Q63425}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate and
CC appear grossly normal during the first six weeks of life. After six to
CC nine months, they display pronounced unsteadiness of gait and
CC difficulty in supporting themselves on their hindlimbs, weight loss due
CC to an inability to feed and labored respiration (PubMed:10839370).
CC Their sensory, motor and vagus nerves show extensive demyelination with
CC demyelinated segments surrounded by focal thickenings (PubMed:10839370,
CC PubMed:18205176). In contrast, the predominantly sensory saphenous
CC nerves are extensively hypermyelinated, resulting in myelin sheath
CC infolding and axon compression (PubMed:10839370). At eight months,
CC naked or thinly myelinated axons are common in sciatic nerve fibers
CC (PubMed:10839370). Already at six weeks, mutant mice display markedly
CC increased sensitivity to noxious mechanical and thermal stimuli
CC (PubMed:10839370). Besides, four month old mutant mice display impaired
CC remyelination after crush injury (PubMed:10839370). Schwann cells from
CC mutant mice display a reduced rate of elongation, leading to decreased
CC distances between nodes of Ranvier and reduced velocity of the
CC transmission of nerve impulses; this results in impaired motor skills
CC on the RotaRod in three week old mice (PubMed:15356632). Peripheral
CC nerves show decreased conduction velocity, due to defects in the myelin
CC sheath (PubMed:10839370). Motor axons from five month old mice show an
CC increased number of preterminal branches that arise from demyelinated
CC regions close to the neuromuscular junction (PubMed:18205176). In
CC contrast, axon branching close to the neuromuscular junction appears
CC normal in three week old mice (PubMed:18205176). At the molecular
CC level, gene disruption impairs formation of Cajal bands and location of
CC Drp2 in patches that colocalize with appositions between the abaxonal
CC surface of the myelin sheath and the Schwann cell plasma membrane
CC (PubMed:15356632). Cytoplasm from mutant Schwann cells forms a
CC concentric ring under the cell membrane, instead of being strictly
CC compartmentalized at Cajal bands (PubMed:15356632). The transport of
CC the mRNA coding for Mbp is impaired; the mRNA level is highest in the
CC perinuclear region and does not accumulate in the paranodal region
CC (PubMed:15356632). Eye lenses from 90 day old mutant mice appear
CC grossly normal at the macroscopic level, but display altered shape and
CC organization of inner lens fiber cells, together with alteration in the
CC membrane localization of Mip, Ezr and Ahnak (PubMed:21745462).
CC {ECO:0000269|PubMed:10839370, ECO:0000269|PubMed:15356632,
CC ECO:0000269|PubMed:18205176, ECO:0000269|PubMed:21745462}.
CC -!- SIMILARITY: Belongs to the periaxin family. {ECO:0000305}.
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DR EMBL; AJ222968; CAA11022.1; -; mRNA.
DR EMBL; AJ222969; CAA11023.1; -; mRNA.
DR CCDS; CCDS21023.1; -. [O55103-1]
DR CCDS; CCDS39849.1; -. [O55103-2]
DR RefSeq; NP_062285.1; NM_019412.2. [O55103-2]
DR RefSeq; NP_932165.2; NM_198048.2.
DR AlphaFoldDB; O55103; -.
DR SMR; O55103; -.
DR BioGRID; 202408; 1.
DR CORUM; O55103; -.
DR IntAct; O55103; 1.
DR STRING; 10090.ENSMUSP00000096241; -.
DR iPTMnet; O55103; -.
DR PhosphoSitePlus; O55103; -.
DR MaxQB; O55103; -.
DR PaxDb; O55103; -.
DR PeptideAtlas; O55103; -.
DR PRIDE; O55103; -.
DR ProteomicsDB; 291856; -. [O55103-1]
DR ProteomicsDB; 291857; -. [O55103-2]
DR Antibodypedia; 959; 68 antibodies from 16 providers.
DR DNASU; 19153; -.
DR Ensembl; ENSMUST00000108355; ENSMUSP00000103992; ENSMUSG00000053198. [O55103-2]
DR GeneID; 19153; -.
DR KEGG; mmu:19153; -.
DR UCSC; uc009fwj.2; mouse. [O55103-2]
DR CTD; 57716; -.
DR MGI; MGI:108176; Prx.
DR VEuPathDB; HostDB:ENSMUSG00000053198; -.
DR eggNOG; ENOG502QS7Y; Eukaryota.
DR GeneTree; ENSGT00940000160366; -.
DR HOGENOM; CLU_1758219_0_0_1; -.
DR InParanoid; O55103; -.
DR OrthoDB; 71329at2759; -.
DR PhylomeDB; O55103; -.
DR BioGRID-ORCS; 19153; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Prx; mouse.
DR PRO; PR:O55103; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O55103; protein.
DR Bgee; ENSMUSG00000053198; Expressed in sciatic nerve and 165 other tissues.
DR ExpressionAtlas; O55103; baseline and differential.
DR Genevisible; O55103; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032290; P:peripheral nervous system myelin formation; IMP:UniProtKB.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1391
FT /note="Periaxin"
FT /id="PRO_0000058564"
FT DOMAIN 16..99
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REPEAT 432..436
FT /note="1"
FT REPEAT 440..444
FT /note="2"
FT REPEAT 448..452
FT /note="3"
FT REPEAT 456..460
FT /note="4"
FT REPEAT 464..468
FT /note="5"
FT REPEAT 469..473
FT /note="6"
FT REPEAT 474..478
FT /note="7"
FT REPEAT 482..486
FT /note="8"
FT REPEAT 487..491
FT /note="9"
FT REPEAT 495..499
FT /note="10"
FT REPEAT 500..504
FT /note="11"
FT REPEAT 508..512
FT /note="12"
FT REPEAT 513..517
FT /note="13; approximate"
FT REPEAT 521..525
FT /note="14"
FT REPEAT 526..530
FT /note="15"
FT REPEAT 534..538
FT /note="16"
FT REPEAT 539..543
FT /note="17"
FT REPEAT 547..551
FT /note="18"
FT REPEAT 552..556
FT /note="19"
FT REPEAT 560..564
FT /note="20"
FT REPEAT 565..569
FT /note="21"
FT REPEAT 573..577
FT /note="22"
FT REPEAT 578..582
FT /note="23"
FT REPEAT 583..587
FT /note="24"
FT REPEAT 591..595
FT /note="25"
FT REPEAT 596..600
FT /note="26"
FT REPEAT 601..605
FT /note="27"
FT REPEAT 609..613
FT /note="28"
FT REPEAT 614..618
FT /note="29"
FT REPEAT 619..623
FT /note="30"
FT REPEAT 627..631
FT /note="31"
FT REPEAT 632..636
FT /note="32"
FT REPEAT 637..641
FT /note="33"
FT REPEAT 645..649
FT /note="34"
FT REPEAT 650..654
FT /note="35"
FT REPEAT 655..659
FT /note="36"
FT REPEAT 663..667
FT /note="37"
FT REPEAT 671..675
FT /note="38"
FT REPEAT 676..680
FT /note="39"
FT REPEAT 684..688
FT /note="40"
FT REPEAT 689..693
FT /note="41"
FT REPEAT 697..701
FT /note="42"
FT REPEAT 702..706
FT /note="43"
FT REPEAT 707..711
FT /note="44"
FT REPEAT 715..719
FT /note="45"
FT REGION 432..719
FT /note="45 X 5 AA approximate tandem repeats of [LVMGIED]-
FT [PQSKHARMI]-[EDKLVTR]-[LIVMAP]-[AQKHRPEVSD]; that may have
FT a tripeptide spacer of [LVIDEA]-[PMSVI]-[KEATDQ]"
FT REGION 1267..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 70..84
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM0"
FT MOTIF 118..196
FT /note="Nuclear localization signal"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63425"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 128..148
FT /note="NIQSLAPVKKKKMVTGALGTP -> VRVLSPVPVQDSPSDRVAAAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9488714"
FT /id="VSP_004366"
FT VAR_SEQ 149..1391
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9488714"
FT /id="VSP_004367"
SQ SEQUENCE 1391 AA; 147688 MW; B16DF4E5C33D376C CRC64;
MEARSRSAEE LRRAELVEII VETEAQTGVS GFNVAGGGKE GIFVRELRED SPAAKSLSLQ
EGDQLLSARV FFENFKYEDA LRLLQCAEPY KVSFCLKRTV PTGDLALRPG TVSGYEMKGP
RAKVAKLNIQ SLAPVKKKKM VTGALGTPAD LAPVDVEFSF PKFSRLRRGL KAEAVKGPVP
AAPARRRLQL PRLRVREVAE EAQVARMAAA APPPRKAKAE AEAATGAGFT APQIELVGPR
LPSAEVGVPQ VSVPKGTPST EAASGFALHL PTLGLGAPAA PAVEPPATGI QVPQVELPTL
PSLPTLPTLP CLDTQEGAAV VKVPTLDVAA PSMGVDLALP GAEVEAQGEV PEVALKMPRL
SFPRFGIRGK EATEAKVVKG SPEAKAKGPR LRMPTFGLSL LEPRPSGPEA VAESKLKLPT
LKMPSFGIGV AGPEVKAPTG PEVKLPKVPE VKLPKVPEAA IPDVQLPEVQ LPKMSDMKLP
KIPEMVVPDV RLPEVQLPKV PEMKVPEMKL PKWPEMAVPD VHLPDVQLPK VPEMKLPKVP
EMAVPDVHLP DVQLPKVPEM KLPEMKLPKV PEMAVPDVRL PEVQLPKVSE VKLPKMPEMA
VPDVHLPELQ LPKMSEVKLP KMPEMAVPDV RLPEVQLPKV SEMKLPKMPE MTMPDIRLPE
VQLPKVPDIK LPEMKLPEIK LPKVPDMAVP DVPLPELQLP KVSDIRLPEM QVSQVPEVQL
PKMPEMKLSK VPEVQRKSAG AEQAKGTEFS FKLPKMTMPK LGKVGKPGEA SIEVPDKLMT
LPCLQPEVGT EASHVGVPSL SLPSVELDLP GALGLEGQVQ EAVPGKVEKP EGPRVAVGVG
EVGFRVPSVE IVTPQLPTVE VEKEQLEMVE MKVKPSSKFS LPKFGLSGPK AVKGEVEGPG
RATKLKVSKF TISLPKARAG TEAEAKGAGE AGLLPALDLS IPQLSLDAQL PSGKVEVADS
KPKSSRFALP KFGVKGRDSE ADVLVAGEAE LEGKGWGWDG KVKMPKLKMP SFGLSRGKEA
ETQDGRVSPG EKLEAIAGQL KIPAVELVTP GAQETEKVTS GVKPSGLQVS TTGQVVAEGQ
ESVQRVSTLG ISLPQVELAS FGEAGPEIVA PSAEGTAGSR VQVPQVMLEL PGTQVAGGDL
LVGEGIFKMP TVTVPQLELD VGLGHEAQAG EAAKSEGGIK LKLPTLGTGS RGEGVEPQGP
EAQRTFHLSL PDVELTSPVS SHAEYQVVEG DGDGGHKLKV RLPLFGLAKA KEGIEVGEKV
KSPKLRLPRV GFSQSESVSG EGSPSPEEEE EGSGEGASSR RGRVRVRLPR VGLASPSKVS
KGQEGDATSK SPVGEKSPKF RFPRVSLSPK ARSGSRDREE GGFRVRLPSV GFSETAVPGS
TRIEGTQAAA I
