NFL_MOUSE
ID NFL_MOUSE Reviewed; 543 AA.
AC P08551; Q8K0Z0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Neurofilament light polypeptide;
DE Short=NF-L;
DE AltName: Full=68 kDa neurofilament protein;
DE AltName: Full=Neurofilament triplet L protein;
GN Name=Nefl; Synonyms=Nf68, Nfl;
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 TISSUE=Brain;
RX PubMed=3103856; DOI=10.1016/0169-328x(86)90030-6;
RA Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F.;
RT "Cloning and developmental expression of the murine neurofilament gene
RT family.";
RL Brain Res. 387:243-250(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=3785173; DOI=10.1128/mcb.6.5.1529-1534.1986;
RA Lewis S.A., Cowan N.J.;
RT "Anomalous placement of introns in a member of the intermediate filament
RT multigene family: an evolutionary conundrum.";
RL Mol. Cell. Biol. 6:1529-1534(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Jensen K.H., Brown A.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=2246261; DOI=10.1016/s0021-9258(17)45441-x;
RA Nakahira K., Ikenaka K., Wada K., Tamura T.A., Furuichi T., Mikoshiba K.;
RT "Structure of the 68-kDa neurofilament gene and regulation of its
RT expression.";
RL J. Biol. Chem. 265:19786-19791(1990).
RN [6]
RP PROTEIN SEQUENCE OF 38-54; 117-126 AND 381-391, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 52-57, AND PHOSPHORYLATION AT SER-56.
RX PubMed=1717455; DOI=10.1016/s0021-9258(18)55143-7;
RA Sihag R.K., Nixon R.A.;
RT "Identification of Ser-55 as a major protein kinase A phosphorylation site
RT on the 70-kDa subunit of neurofilaments. Early turnover during axonal
RT transport.";
RL J. Biol. Chem. 266:18861-18867(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 242-543.
RC TISSUE=Brain;
RX PubMed=3919033; DOI=10.1083/jcb.100.3.843;
RA Lewis S.A., Cowan N.J.;
RT "Genetics, evolution, and expression of the 68,000-mol-wt neurofilament
RT protein: isolation of a cloned cDNA probe.";
RL J. Cell Biol. 100:843-850(1985).
RN [9]
RP INTERACTION WITH ARHGEF28.
RX PubMed=16236762; DOI=10.1093/hmg/ddi392;
RA Lin H., Zhai J., Schlaepfer W.W.;
RT "RNA-binding protein is involved in aggregation of light neurofilament
RT protein and is implicated in the pathogenesis of motor neuron
RT degeneration.";
RL Hum. Mol. Genet. 14:3643-3659(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-532, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND IDENTIFICATION BY
RP 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 [13]
RP INTERACTION WITH TRIM2, AND UBIQUITINATION.
RX PubMed=18687884; DOI=10.1073/pnas.0802261105;
RA Balastik M., Ferraguti F., Pires-da Silva A., Lee T.H., Alvarez-Bolado G.,
RA Lu K.P., Gruss P.;
RT "Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament
RT light chain and neurodegeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12016-12021(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22723690; DOI=10.1523/jneurosci.1081-12.2012;
RA Yuan A., Sasaki T., Kumar A., Peterhoff C.M., Rao M.V., Liem R.K.,
RA Julien J.P., Nixon R.A.;
RT "Peripherin is a subunit of peripheral nerve neurofilaments: implications
RT for differential vulnerability of CNS and peripheral nervous system
RT axons.";
RL J. Neurosci. 32:8501-8508(2012).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-23 AND ARG-30, AND IDENTIFICATION
RP BY MASS 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: Neurofilaments usually contain three intermediate filament
CC proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of
CC neuronal caliber. May additionally cooperate with the neuronal
CC intermediate filament proteins PRPH and INA to form neuronal
CC filamentous networks (PubMed:22723690). {ECO:0000269|PubMed:22723690}.
CC -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Forms
CC heterodimers with NEFH or NEFM; which can further hetero-oligomerize
CC (in vitro) (By similarity). Forms heterodimers with INA (in vitro) (By
CC similarity). Interacts with ARHGEF28. Interacts with TRIM2.
CC {ECO:0000250|UniProtKB:P19527, ECO:0000269|PubMed:16236762,
CC ECO:0000269|PubMed:18687884}.
CC -!- INTERACTION:
CC P08551; Q9ESN6: Trim2; NbExp=2; IntAct=EBI-445199, EBI-8315064;
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:22723690}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22723690}.
CC -!- TISSUE SPECIFICITY: Expressed in the sciatic nerve (at protein level).
CC {ECO:0000269|PubMed:22723690}.
CC -!- DOMAIN: The extra mass and high charge density that distinguish the
CC neurofilament proteins from all other intermediate filament proteins
CC are due to the tailpiece extensions. This region may form a charged
CC scaffolding structure suitable for interaction with other neuronal
CC components or ions.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16452088}.
CC -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC leading to the inhibition of polymerization. {ECO:0000250}.
CC -!- PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1.
CC {ECO:0000269|PubMed:18687884}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of Nefm, Nefh and Prph in the
CC sciatic nerve and reduced numbers of neurofilaments in sciatic axons.
CC {ECO:0000269|PubMed:22723690}.
CC -!- MISCELLANEOUS: NF-L is the most abundant of the three neurofilament
CC proteins and, like the other nonepithelial intermediate filament
CC proteins, it can form homomeric 10-nm filaments.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; M20480; AAA39814.1; -; mRNA.
DR EMBL; M13016; AAA39810.1; -; Genomic_DNA.
DR EMBL; DQ201635; ABA46748.1; -; mRNA.
DR EMBL; BC029203; AAH29203.1; -; mRNA.
DR EMBL; AH002053; AAA39812.1; -; Genomic_DNA.
DR EMBL; X02165; CAB51616.1; -; mRNA.
DR CCDS; CCDS27232.1; -.
DR PIR; A25227; QFMSL.
DR RefSeq; NP_035040.1; NM_010910.1.
DR AlphaFoldDB; P08551; -.
DR SMR; P08551; -.
DR BioGRID; 201757; 34.
DR DIP; DIP-31944N; -.
DR IntAct; P08551; 17.
DR MINT; P08551; -.
DR STRING; 10090.ENSMUSP00000022639; -.
DR GlyGen; P08551; 2 sites.
DR iPTMnet; P08551; -.
DR PhosphoSitePlus; P08551; -.
DR SwissPalm; P08551; -.
DR UCD-2DPAGE; P08551; -.
DR EPD; P08551; -.
DR jPOST; P08551; -.
DR MaxQB; P08551; -.
DR PaxDb; P08551; -.
DR PeptideAtlas; P08551; -.
DR PRIDE; P08551; -.
DR ProteomicsDB; 287500; -.
DR Antibodypedia; 73404; 1087 antibodies from 41 providers.
DR DNASU; 18039; -.
DR Ensembl; ENSMUST00000022639; ENSMUSP00000022639; ENSMUSG00000022055.
DR GeneID; 18039; -.
DR KEGG; mmu:18039; -.
DR UCSC; uc007uln.1; mouse.
DR CTD; 4747; -.
DR MGI; MGI:97313; Nefl.
DR VEuPathDB; HostDB:ENSMUSG00000022055; -.
DR eggNOG; ENOG502QSXY; Eukaryota.
DR GeneTree; ENSGT00940000156208; -.
DR HOGENOM; CLU_012560_7_3_1; -.
DR InParanoid; P08551; -.
DR OMA; YEPYYAT; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P08551; -.
DR TreeFam; TF330122; -.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR BioGRID-ORCS; 18039; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Nefl; mouse.
DR PRO; PR:P08551; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P08551; protein.
DR Bgee; ENSMUSG00000022055; Expressed in motor neuron and 227 other tissues.
DR Genevisible; P08551; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005883; C:neurofilament; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IDA:SynGO.
DR GO; GO:0099182; C:presynaptic intermediate filament cytoskeleton; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IMP:SynGO.
DR GO; GO:0008089; P:anterograde axonal transport; ISO:MGI.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IGI:BHF-UCL.
DR GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
DR GO; GO:0045105; P:intermediate filament polymerization or depolymerization; ISO:MGI.
DR GO; GO:0040011; P:locomotion; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0033693; P:neurofilament bundle assembly; ISO:MGI.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IMP:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:MGI.
DR GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
DR GO; GO:1903937; P:response to acrylamide; IEA:Ensembl.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:1903935; P:response to sodium arsenite; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0008090; P:retrograde axonal transport; ISO:MGI.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0060074; P:synapse maturation; IDA:SynGO.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR027692; NF-L.
DR PANTHER; PTHR45652:SF8; PTHR45652:SF8; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycoprotein; Intermediate filament;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT CHAIN 2..543
FT /note="Neurofilament light polypeptide"
FT /id="PRO_0000063788"
FT DOMAIN 90..401
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..93
FT /note="Head"
FT REGION 94..125
FT /note="Coil 1A"
FT REGION 126..138
FT /note="Linker 1"
FT REGION 139..234
FT /note="Coil 1B"
FT REGION 235..253
FT /note="Linker 12"
FT REGION 254..272
FT /note="Coil 2A"
FT REGION 273..281
FT /note="Linker 2"
FT REGION 282..397
FT /note="Coil 2B"
FT REGION 382..392
FT /note="Epitope; recognized by IF-specific monoclonal
FT antibody"
FT REGION 398..543
FT /note="Tail"
FT REGION 398..444
FT /note="Tail, subdomain A"
FT REGION 445..543
FT /note="Tail, subdomain B (acidic)"
FT REGION 449..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 23
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 23
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1717455"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CARBOHYD 21
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="Y -> S (in Ref. 2; AAA39810)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="Y -> I (in Ref. 2; AAA39810)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="M -> K (in Ref. 2; AAA39810)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="L -> V (in Ref. 2; AAA39810)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="D -> H (in Ref. 2; AAA39810)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> R (in Ref. 1; AAA39814)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="Missing (in Ref. 1; AAA39814)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="Y -> I (in Ref. 2; AAA39810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 61508 MW; BC40F8A8A536CFF5 CRC64;
MSSFGYDPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA
ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE
EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY
AQISVEMDVS SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR
AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD TINKLENELR
STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSIT SGYSQSSQVF
GRSAYSGLQS SSYLMSARSF PAYYTSHVQE EQTEVEETIE ATKAEEAKDE PPSEGEAEEE
EKEKEEGEEE EGAEEEEAAK DESEDTKEEE EGGEGEEEDT KESEEEEKKE ESAGEEQVAK
KKD
