DPYL2_MOUSE
ID DPYL2_MOUSE Reviewed; 572 AA.
AC O08553; Q6P5D0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Dihydropyrimidinase-related protein 2;
DE Short=DRP-2;
DE AltName: Full=Unc-33-like phosphoprotein 2;
DE Short=ULIP-2;
GN Name=Dpysl2; Synonyms=Crmp2, Ulip2;
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=ICR; TISSUE=Brain;
RX PubMed=9652388; DOI=10.1046/j.1432-1327.1998.2540014.x;
RA Byk T., Ozon S., Sobel A.;
RT "The Ulip family phosphoproteins -- common and specific properties.";
RL Eur. J. Biochem. 254:14-24(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 44-56; 174-211; 239-254; 259-268; 391-397; 441-467 AND
RP 533-552, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=9375656; DOI=10.1046/j.1471-4159.1997.69062261.x;
RA Wang L.H., Strittmatter S.M.;
RT "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase.";
RL J. Neurochem. 69:2261-2269(1997).
RN [5]
RP SUBUNIT.
RX PubMed=10956643; DOI=10.1074/jbc.m003277200;
RA Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA Matsuda Y., Noda M.;
RT "Molecular characterization of CRMP5, a novel member of the collapsin
RT response mediator protein family.";
RL J. Biol. Chem. 275:37957-37965(2000).
RN [6]
RP INTERACTION WITH HTR4.
RX PubMed=15466885; DOI=10.1242/jcs.01379;
RA Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA Marin P., Dumuis A., Bockaert J.;
RT "New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a
RT receptor splice variant: roles in receptor targeting.";
RL J. Cell Sci. 117:5367-5379(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15648052; DOI=10.1002/pmic.200401066;
RA Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA Hart G.W., Burlingame A.L.;
RT "Quantitative analysis of both protein expression and serine / threonine
RT post-translational modifications through stable isotope labeling with
RT dithiothreitol.";
RL Proteomics 5:388-398(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-431; TYR-499 AND THR-509, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514; SER-517; SER-518 AND
RP SER-522, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-507; THR-509;
RP THR-512; THR-514; SER-517; SER-518; THR-521; SER-522; SER-537; SER-540 AND
RP SER-542, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [12]
RP FUNCTION, PHOSPHORYLATION AT THR-514, AND MUTAGENESIS OF THR-514.
RX PubMed=22057101; DOI=10.1038/ncb2373;
RA Wakatsuki S., Saitoh F., Araki T.;
RT "ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-
RT dependent CRMP2 phosphorylation.";
RL Nat. Cell Biol. 13:1415-1423(2011).
RN [13]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-565, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays a role in neuronal development and polarity, as well as
CC in axon growth and guidance, neuronal growth cone collapse and cell
CC migration. Necessary for signaling by class 3 semaphorins and
CC subsequent remodeling of the cytoskeleton. May play a role in
CC endocytosis. {ECO:0000269|PubMed:22057101}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL3, DPYSL4 or
CC DPYSL5. Interacts through its C-terminus with the C-terminus of
CC CYFIP1/SRA1. Interacts with HTR4. Interacts with CLN6. Interacts with
CC MICALL1. {ECO:0000269|PubMed:10956643, ECO:0000269|PubMed:15466885,
CC ECO:0000269|PubMed:9375656}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Note=Tightly but
CC non-covalently associated with membranes. {ECO:0000250}.
CC -!- PTM: Phosphorylation by DYRK2 at Ser-522 is required for subsequent
CC phosphorylation by GSK3B (By similarity). Phosphorylation at Thr-514 by
CC GSK3B abolishes tubulin-binding leading to destabilization of
CC microtubule assembly in axons and neurodegeneration. {ECO:0000250,
CC ECO:0000269|PubMed:22057101}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC -!- CAUTION: Lacks most of the conserved residues that are essential for
CC binding the metal cofactor and hence for dihydropyrimidinase activity.
CC Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR EMBL; Y10339; CAA71370.1; -; mRNA.
DR EMBL; BC062955; AAH62955.1; -; mRNA.
DR CCDS; CCDS27224.1; -.
DR RefSeq; NP_034085.2; NM_009955.3.
DR PDB; 5UQC; X-ray; 1.78 A; A/B=15-496.
DR PDBsum; 5UQC; -.
DR AlphaFoldDB; O08553; -.
DR SMR; O08553; -.
DR BioGRID; 198891; 121.
DR CORUM; O08553; -.
DR IntAct; O08553; 29.
DR MINT; O08553; -.
DR STRING; 10090.ENSMUSP00000022629; -.
DR ChEMBL; CHEMBL1075160; -.
DR MEROPS; M38.975; -.
DR iPTMnet; O08553; -.
DR PhosphoSitePlus; O08553; -.
DR SwissPalm; O08553; -.
DR REPRODUCTION-2DPAGE; IPI00114375; -.
DR REPRODUCTION-2DPAGE; O08553; -.
DR UCD-2DPAGE; O08553; -.
DR CPTAC; non-CPTAC-3426; -.
DR CPTAC; non-CPTAC-3911; -.
DR EPD; O08553; -.
DR jPOST; O08553; -.
DR MaxQB; O08553; -.
DR PaxDb; O08553; -.
DR PeptideAtlas; O08553; -.
DR PRIDE; O08553; -.
DR ProteomicsDB; 279482; -.
DR Antibodypedia; 1039; 653 antibodies from 40 providers.
DR DNASU; 12934; -.
DR Ensembl; ENSMUST00000022629; ENSMUSP00000022629; ENSMUSG00000022048.
DR GeneID; 12934; -.
DR KEGG; mmu:12934; -.
DR UCSC; uc007uko.1; mouse.
DR CTD; 1808; -.
DR MGI; MGI:1349763; Dpysl2.
DR VEuPathDB; HostDB:ENSMUSG00000022048; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; O08553; -.
DR OMA; FTHRENF; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; O08553; -.
DR TreeFam; TF314706; -.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR BioGRID-ORCS; 12934; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Dpysl2; mouse.
DR PRO; PR:O08553; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O08553; protein.
DR Bgee; ENSMUSG00000022048; Expressed in medial preoptic region and 220 other tissues.
DR Genevisible; O08553; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0030516; P:regulation of axon extension; IEA:InterPro.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IGI:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; ISO:MGI.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030615; DRP2.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF56; PTHR11647:SF56; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Direct protein sequencing; Membrane; Methylation;
KW Neurogenesis; Phosphoprotein; Reference proteome; S-nitrosylation.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 2"
FT /id="PRO_0000165914"
FT REGION 512..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q16555"
FT MOD_RES 258
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47942"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15648052"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 504
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P47942"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:22057101,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:O02675"
FT MOD_RES 565
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MUTAGEN 514
FT /note="T->A: Delayed neurite degeneration."
FT /evidence="ECO:0000269|PubMed:22057101"
FT CONFLICT 11
FT /note="R -> P (in Ref. 1; CAA71370)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="E -> A (in Ref. 1; CAA71370)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="S -> P (in Ref. 1; CAA71370)"
FT /evidence="ECO:0000305"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:5UQC"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5UQC"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:5UQC"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:5UQC"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:5UQC"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:5UQC"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:5UQC"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5UQC"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:5UQC"
SQ SEQUENCE 572 AA; 62278 MW; C031F3BC038AA737 CRC64;
MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
DQWREWADSK SCCDYSLHVD ITEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ
IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI
TIANQTNCPL YVTKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR ISVGSDADLV IWDPDSVKTI
SAKTHNSALE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK
RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS
LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG
