PLPP_MOUSE
ID PLPP_MOUSE Reviewed; 292 AA.
AC P60487;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chronophin {ECO:0000303|PubMed:24338473};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q3ZBF9};
DE EC=3.1.3.74 {ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190};
DE AltName: Full=Pyridoxal 5'-phosphate phosphatase {ECO:0000303|PubMed:24338473};
DE AltName: Full=Pyridoxal phosphate phosphatase {ECO:0000303|PubMed:24338687};
DE Short=PLP phosphatase {ECO:0000303|PubMed:24338687};
GN Name=Pdxp {ECO:0000312|MGI:MGI:1919282};
GN Synonyms=Cin {ECO:0000303|PubMed:24338687},
GN Plp {ECO:0000303|PubMed:24338687}, Plpp;
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].
RC STRAIN=SWR/J; TISSUE=Brain;
RX PubMed=14522954; DOI=10.1074/jbc.m309619200;
RA Jang Y.M., Kim D.W., Kang T.-C., Won M.H., Baek N.-I., Moon B.J.,
RA Choi S.Y., Kwon O.-S.;
RT "Human pyridoxal phosphatase. Molecular cloning, functional expression, and
RT tissue distribution.";
RL J. Biol. Chem. 278:50040-50046(2003).
RN [2]
RP PROTEIN SEQUENCE OF 100-119 AND 141-154, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-292.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, and Spleen;
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 [5] {ECO:0007744|PDB:4BX0, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:4BX3}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP BERYLLIUM TRIFLUORIDE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 194-ALA-ALA-195, AND ACTIVE
RP SITE.
RX PubMed=24338687; DOI=10.1074/jbc.m113.536482;
RA Kestler C., Knobloch G., Tessmer I., Jeanclos E., Schindelin H., Gohla A.;
RT "Chronophin dimerization is required for proper positioning of its
RT substrate specificity loop.";
RL J. Biol. Chem. 289:3094-3103(2014).
RN [6] {ECO:0007744|PDB:4BKM}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-100 AND 208-233 IN COMPLEX WITH
RP MAGNESIUM, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, AND FUNCTION.
RX PubMed=24338473; DOI=10.1074/jbc.m113.503359;
RA Seifried A., Knobloch G., Duraphe P.S., Segerer G., Manhard J.,
RA Schindelin H., Schultz J., Gohla A.;
RT "Evolutionary and structural analyses of the mammalian haloacid
RT dehalogenase-type phosphatases AUM and chronophin provide insight into the
RT basis of their different substrate specificities.";
RL J. Biol. Chem. 289:3416-3431(2014).
RN [7] {ECO:0007744|PDB:5AES}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX PubMed=25783190; DOI=10.1016/j.bmc.2015.02.049;
RA Knobloch G., Jabari N., Stadlbauer S., Schindelin H., Kohn M., Gohla A.;
RT "Synthesis of hydrolysis-resistant pyridoxal 5'-phosphate analogs and their
RT biochemical and X-ray crystallographic characterization with the pyridoxal
RT phosphatase chronophin.";
RL Bioorg. Med. Chem. 23:2819-2827(2015).
CC -!- FUNCTION: Functions as a pyridoxal phosphate (PLP) phosphatase, which
CC also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP)
CC and pyridoxamine 5'-phosphate (PMP), with order of substrate preference
CC PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism
CC (PubMed:24338473, PubMed:24338687, PubMed:25783190). Also functions as
CC a protein serine phosphatase that specifically dephosphorylates 'Ser-3'
CC in proteins of the actin-depolymerizing factor (ADF)/cofilin family
CC like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin
CC cytoskeleton reorganization, being required for normal progress through
CC mitosis and normal cytokinesis. Does not dephosphorylate
CC phosphothreonines in LIMK1. Does not dephosphorylate peptides
CC containing phosphotyrosine (By similarity).
CC {ECO:0000250|UniProtKB:Q96GD0, ECO:0000269|PubMed:24338473,
CC ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74;
CC Evidence={ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687,
CC ECO:0000269|PubMed:25783190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC Evidence={ECO:0000305|PubMed:24338473};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxine 5'-phosphate = phosphate + pyridoxine;
CC Xref=Rhea:RHEA:25112, ChEBI:CHEBI:15377, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58589; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25113;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + pyridoxamine = H2O + pyridoxamine 5'-phosphate;
CC Xref=Rhea:RHEA:25135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57761, ChEBI:CHEBI:58451; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25137;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:24338473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:24338473};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687,
CC ECO:0000269|PubMed:25783190};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000269|PubMed:24338473};
CC -!- ACTIVITY REGULATION: Inhibited by beryllium trifluoride.
CC {ECO:0000269|PubMed:24338473}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for pyridoxal 5'-phosphate {ECO:0000269|PubMed:24338687,
CC ECO:0000269|PubMed:25783190};
CC Vmax=3.6 umol/min/mg enzyme with pyridoxal 5'-phosphate as substrate
CC {ECO:0000269|PubMed:25783190};
CC Note=kcat varies between 1.5 and 2.0 sec(-1) for the
CC dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 22 degrees
CC Celsius). {ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24338473,
CC ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin
CC cytoskeleton in membrane ruffles and lamellipodia. Diffusely
CC distributed throughout the cytosol during pro-metaphase and metaphase.
CC Detected at the dynamic cell poles during telophase. Detected at the
CC cleavage furrow and contractile ring during cytokinesis. Transiently
CC detected at the plasma membrane in late stages of cytokinesis. Detected
CC at the midbody. {ECO:0000250|UniProtKB:Q96GD0}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. highly expressed in brain (at protein
CC level). {ECO:0000269|PubMed:24338473}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AY366300; AAR12209.1; -; mRNA.
DR EMBL; BC058388; AAH58388.1; -; mRNA.
DR CCDS; CCDS27627.1; -.
DR RefSeq; NP_064667.2; NM_020271.3.
DR PDB; 4BKM; X-ray; 2.65 A; A/B/C/D=1-100, A/B/C/D=208-292.
DR PDB; 4BX0; X-ray; 1.75 A; A=1-292.
DR PDB; 4BX2; X-ray; 2.19 A; A/B=1-292.
DR PDB; 4BX3; X-ray; 2.19 A; A/B=1-292.
DR PDB; 5AES; X-ray; 2.75 A; A/B=1-292.
DR PDBsum; 4BKM; -.
DR PDBsum; 4BX0; -.
DR PDBsum; 4BX2; -.
DR PDBsum; 4BX3; -.
DR PDBsum; 5AES; -.
DR AlphaFoldDB; P60487; -.
DR SMR; P60487; -.
DR IntAct; P60487; 1.
DR BindingDB; P60487; -.
DR ChEMBL; CHEMBL3425392; -.
DR iPTMnet; P60487; -.
DR PhosphoSitePlus; P60487; -.
DR SwissPalm; P60487; -.
DR REPRODUCTION-2DPAGE; P60487; -.
DR EPD; P60487; -.
DR MaxQB; P60487; -.
DR PaxDb; P60487; -.
DR PeptideAtlas; P60487; -.
DR PRIDE; P60487; -.
DR ProteomicsDB; 289453; -.
DR Antibodypedia; 34919; 109 antibodies from 27 providers.
DR DNASU; 57028; -.
DR Ensembl; ENSMUST00000089378; ENSMUSP00000086796; ENSMUSG00000116165.
DR GeneID; 57028; -.
DR KEGG; mmu:57028; -.
DR UCSC; uc007wru.1; mouse.
DR CTD; 57026; -.
DR MGI; MGI:1919282; Pdxp.
DR VEuPathDB; HostDB:ENSMUSG00000116165; -.
DR GeneTree; ENSGT00940000162045; -.
DR HOGENOM; CLU_043473_0_1_1; -.
DR InParanoid; P60487; -.
DR OMA; MDGVLIH; -.
DR OrthoDB; 982374at2759; -.
DR PhylomeDB; P60487; -.
DR TreeFam; TF314344; -.
DR BRENDA; 3.1.3.74; 3474.
DR BioGRID-ORCS; 57028; 1 hit in 39 CRISPR screens.
DR ChiTaRS; Pdxp; mouse.
DR PRO; PR:P60487; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P60487; protein.
DR Bgee; ENSMUSG00000116165; Expressed in basal forebrain and 99 other tissues.
DR Genevisible; P60487; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0070938; C:contractile ring; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; IDA:UniProtKB.
DR GO; GO:0031247; P:actin rod assembly; ISO:MGI.
DR GO; GO:0071318; P:cellular response to ATP; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0032361; P:pyridoxal phosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..292
FT /note="Chronophin"
FT /id="PRO_0000068838"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:24338687,
FT ECO:0000305|PubMed:25783190, ECO:0007744|PDB:4BX2,
FT ECO:0007744|PDB:5AES"
FT ACT_SITE 27
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24338687,
FT ECO:0000305|PubMed:25783190, ECO:0007744|PDB:4BX2,
FT ECO:0007744|PDB:5AES"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24338473,
FT ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190,
FT ECO:0007744|PDB:4BKM, ECO:0007744|PDB:4BX0,
FT ECO:0007744|PDB:4BX2, ECO:0007744|PDB:4BX3,
FT ECO:0007744|PDB:5AES"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24338473,
FT ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190,
FT ECO:0007744|PDB:4BKM, ECO:0007744|PDB:4BX0,
FT ECO:0007744|PDB:4BX2, ECO:0007744|PDB:4BX3,
FT ECO:0007744|PDB:5AES"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24338687,
FT ECO:0000269|PubMed:25783190, ECO:0007744|PDB:4BX2,
FT ECO:0007744|PDB:5AES"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25783190,
FT ECO:0007744|PDB:5AES"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24338687,
FT ECO:0000269|PubMed:25783190, ECO:0007744|PDB:4BX2,
FT ECO:0007744|PDB:5AES"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24338473,
FT ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190,
FT ECO:0007744|PDB:4BKM, ECO:0007744|PDB:4BX0,
FT ECO:0007744|PDB:4BX2, ECO:0007744|PDB:4BX3,
FT ECO:0007744|PDB:5AES"
FT MUTAGEN 194..195
FT /note="AA->KK: Abolishes homodimerization. Strongly
FT decreases affinity for pyridoxal phosphate."
FT /evidence="ECO:0000269|PubMed:24338687"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4BX0"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:4BX0"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4BX2"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4BX0"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4BX0"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4BX0"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:4BX0"
SQ SEQUENCE 292 AA; 31512 MW; B5F1B2C7E71A585D CRC64;
MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLARA GKNTLFVSNN
SRRARPELAL RFARLGFAGL RAEQLFSSAL CAARLLRQRL SGPPDASGAV FVLGGEGLRA
ELRAAGLRLA GDPGEDPRVR AVLVGYDEQF SFSRLTEACA HLRDPDCLLV ATDRDPWHPL
SDGSRTPGTG SLAAAVETAS GRQALVVGKP SPYMFQCITE DFSVDPARTL MVGDRLETDI
LFGHRCGMTT VLTLTGVSSL EEAQAYLTAG QRDLVPHYYV ESIADLMEGL ED
