NFL_HUMAN
ID NFL_HUMAN Reviewed; 543 AA.
AC P07196; B9ZVN2; Q16154; Q8IU72;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 230.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3034332; DOI=10.1016/0167-4781(87)90041-8;
RA Julien J.-P., Grosveld F., Yazdanbaksh K., Flavell D., Meijer D.,
RA Mushynski W.;
RT "The structure of a human neurofilament gene (NF-L): a unique exon-intron
RT organization in the intermediate filament gene family.";
RL Biochim. Biophys. Acta 909:10-20(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12432080; DOI=10.1242/jcs.00148;
RA Perez-Olle R., Leung C.L., Liem R.K.;
RT "Effects of Charcot-Marie-Tooth-linked mutations of the neurofilament light
RT subunit on intermediate filament formation.";
RL J. Cell Sci. 115:4937-4946(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=8180132;
RA Pospelov V.A., Pospelova T.V., Julien J.-P.;
RT "AP-1 and Krox-24 transcription factors activate the neurofilament light
RT gene promoter in P19 embryonal carcinoma cells.";
RL Cell Growth Differ. 5:187-196(1994).
RN [7]
RP PROTEIN SEQUENCE OF 38-54; 213-224; 340-353; 380-390 AND 422-437, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 468-473.
RC TISSUE=Brain;
RX PubMed=6135695; DOI=10.1093/jb/93.3.825;
RA Nomata Y., Watanabe T., Wada H.;
RT "Highly acidic proteins from human brain: purification and properties of
RT Glu-50 protein.";
RL J. Biochem. 93:825-831(1983).
RN [9]
RP PHOSPHORYLATION BY PKN1.
RX PubMed=8621664; DOI=10.1074/jbc.271.16.9816;
RA Mukai H., Toshimori M., Shibata H., Kitagawa M., Shimakawa M., Miyahara M.,
RA Sunakawa H., Ono Y.;
RT "PKN associates and phosphorylates the head-rod domain of neurofilament
RT protein.";
RL J. Biol. Chem. 271:9816-9822(1996).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP VARIANT CMT2E PRO-332.
RX PubMed=10841809; DOI=10.1086/302962;
RA Mersiyanova I.V., Perepelov A.V., Polyakov A.V., Sitnikov V.F.,
RA Dadali E.L., Oparin R.B., Petrin A.N., Evgrafov O.V.;
RT "A new variant of Charcot-Marie-Tooth disease type 2 is probably the result
RT of a mutation in the neurofilament-light gene.";
RL Am. J. Hum. Genet. 67:37-46(2000).
RN [13]
RP VARIANT CMT2E ARG-8.
RX PubMed=11220745;
RX DOI=10.1002/1531-8249(20010201)49:2<245::aid-ana45>3.0.co;2-a;
RA De Jonghe P., Mersivanova I., Nelis E., Del Favero J., Martin J.-J.,
RA Van Broeckhoven C., Evgrafov O., Timmerman V.;
RT "Further evidence that neurofilament light chain gene mutations can cause
RT Charcot-Marie-Tooth disease type 2E.";
RL Ann. Neurol. 49:245-249(2001).
RN [14]
RP VARIANT CMT2E SER-22.
RX PubMed=12481988; DOI=10.1007/s10048-002-0138-4;
RA Georgiou D.-M., Zidar J., Korosec M., Middleton L.T., Kyriakides T.,
RA Christodoulou K.;
RT "A novel NF-L mutation Pro22Ser is associated with CMT2 in a large
RT Slovenian family.";
RL Neurogenetics 4:93-96(2002).
RN [15]
RP VARIANTS CMT1F ARG-8; LEU-8; GLN-8; LYS-90; SER-98 AND GLU-527 DEL, AND
RP VARIANTS LYS-7 AND ASN-468.
RX PubMed=12566280; DOI=10.1093/brain/awg059;
RA Jordanova A., De Jonghe P., Boerkoel C.F., Takashima H., De Vriendt E.,
RA Ceuterick C., Martin J.-J., Butler I.J., Mancias P., Papasozomenos S.C.,
RA Terespolsky D., Potocki L., Brown C.W., Shy M., Rita D.A., Tournev I.,
RA Kremensky I., Lupski J.R., Timmerman V.;
RT "Mutations in the neurofilament light chain gene (NEFL) cause early onset
RT severe Charcot-Marie-Tooth disease.";
RL Brain 126:590-597(2003).
RN [16]
RP VARIANT CMT2E PRO-336, AND VARIANT CMT1F LYS-396.
RX PubMed=15241803; DOI=10.1002/humu.9261;
RA Choi B.-O., Lee M.S., Shin S.H., Hwang J.H., Choi K.-G., Kim W.-K.,
RA Sunwoo I.N., Kim N.K., Chung K.W.;
RT "Mutational analysis of PMP22, MPZ, GJB1, EGR2 and NEFL in Korean Charcot-
RT Marie-Tooth neuropathy patients.";
RL Hum. Mutat. 24:185-186(2004).
RN [17]
RP VARIANT CMTDIG LYS-396.
RX PubMed=14733962; DOI=10.1016/j.nmd.2003.10.003;
RA Zuechner S., Vorgerd M., Sindern E., Schroeder J.M.;
RT "The novel neurofilament light (NEFL) mutation Glu397Lys is associated with
RT a clinically and morphologically heterogeneous type of Charcot-Marie-Tooth
RT neuropathy.";
RL Neuromuscul. Disord. 14:147-157(2004).
RN [18]
RP VARIANTS MET-213 AND ASN-468, VARIANTS CMT2E SER-22; PRO-268 AND
RP 322-CYS--ASN-326 DEL, AND VARIANT CMTDIG LYS-396.
RX PubMed=17052987; DOI=10.1093/brain/awl284;
RA Fabrizi G.M., Cavallaro T., Angiari C., Cabrini I., Taioli F., Malerba G.,
RA Bertolasi L., Rizzuto N.;
RT "Charcot-Marie-Tooth disease type 2E, a disorder of the cytoskeleton.";
RL Brain 130:394-403(2007).
RN [19]
RP VARIANTS CMT2E ARG-8; SER-22 AND LYS-396.
RX PubMed=22206013; DOI=10.1371/journal.pone.0029393;
RA Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H.,
RA Antonellis A., Lee Y.C.;
RT "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2
RT among the Han Chinese in Taiwan.";
RL PLoS ONE 6:E29393-E29393(2011).
RN [20]
RP VARIANT CMTDIG LYS-396, AND INVOLVEMENT IN CMTDIG.
RX PubMed=25877835; DOI=10.1007/s00415-015-7709-4;
RA Berciano J., Garcia A., Peeters K., Gallardo E., De Vriendt E.,
RA Pelayo-Negro A.L., Infante J., Jordanova A.;
RT "NEFL E396K mutation is associated with a novel dominant intermediate
RT Charcot-Marie-Tooth disease phenotype.";
RL J. Neurol. 262:1289-1300(2015).
RN [21]
RP VARIANTS CMT2E CYS-265; PRO-268; PRO-336 AND LEU-440.
RX PubMed=25802885; DOI=10.1002/mgg3.126;
RA Drew A.P., Zhu D., Kidambi A., Ly C., Tey S., Brewer M.H., Ahmad-Annuar A.,
RA Nicholson G.A., Kennerson M.L.;
RT "Improved inherited peripheral neuropathy genetic diagnosis by whole-exome
RT sequencing.";
RL Mol. Genet. Genomic Med. 3:143-154(2015).
RN [22]
RP VARIANT CMTDIG SER-98, AND INVOLVEMENT IN CMTDIG.
RX PubMed=26645395; DOI=10.1007/s00415-015-7985-z;
RA Berciano J., Peeters K., Garcia A., Lopez-Alburquerque T., Gallardo E.,
RA Hernandez-Fabian A., Pelayo-Negro A.L., De Vriendt E., Infante J.,
RA Jordanova A.;
RT "NEFL N98S mutation: another cause of dominant intermediate Charcot-Marie-
RT Tooth disease with heterogeneous early-onset phenotype.";
RL J. Neurol. 263:361-369(2016).
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 (By similarity). {ECO:0000250|UniProtKB:P08551}.
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, ECO:0000250|UniProtKB:P19527}.
CC -!- INTERACTION:
CC P07196; P20933: AGA; NbExp=3; IntAct=EBI-475646, EBI-1223922;
CC P07196; P13928: ANXA8; NbExp=3; IntAct=EBI-475646, EBI-2556915;
CC P07196; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-475646, EBI-2875816;
CC P07196; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-475646, EBI-14199987;
CC P07196; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-475646, EBI-4290814;
CC P07196; O95817: BAG3; NbExp=3; IntAct=EBI-475646, EBI-747185;
CC P07196; Q8IXM2: BAP18; NbExp=3; IntAct=EBI-475646, EBI-4280811;
CC P07196; Q8N865: C7orf31; NbExp=3; IntAct=EBI-475646, EBI-10174456;
CC P07196; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-475646, EBI-751596;
CC P07196; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-475646, EBI-25850646;
CC P07196; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-475646, EBI-10961312;
CC P07196; P0C7W6: CCDC172; NbExp=3; IntAct=EBI-475646, EBI-2548868;
CC P07196; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-475646, EBI-10181422;
CC P07196; Q6P2R3: CEP57L1; NbExp=3; IntAct=EBI-475646, EBI-12696312;
CC P07196; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-475646, EBI-11953200;
CC P07196; Q9Y240: CLEC11A; NbExp=3; IntAct=EBI-475646, EBI-3957044;
CC P07196; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-475646, EBI-2872414;
CC P07196; Q7L576: CYFIP1; NbExp=3; IntAct=EBI-475646, EBI-1048143;
CC P07196; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-475646, EBI-25842815;
CC P07196; P17661: DES; NbExp=7; IntAct=EBI-475646, EBI-1055572;
CC P07196; P63172: DYNLT1; NbExp=3; IntAct=EBI-475646, EBI-1176455;
CC P07196; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-475646, EBI-12920100;
CC P07196; Q9H6S3: EPS8L2; NbExp=3; IntAct=EBI-475646, EBI-3940939;
CC P07196; Q99504: EYA3; NbExp=3; IntAct=EBI-475646, EBI-9089567;
CC P07196; Q6P587-2: FAHD1; NbExp=3; IntAct=EBI-475646, EBI-12902289;
CC P07196; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-475646, EBI-8468186;
CC P07196; Q8TC84: FANK1; NbExp=3; IntAct=EBI-475646, EBI-21975404;
CC P07196; Q53R41: FASTKD1; NbExp=3; IntAct=EBI-475646, EBI-3957005;
CC P07196; Q7L622: G2E3; NbExp=3; IntAct=EBI-475646, EBI-751757;
CC P07196; P14136: GFAP; NbExp=9; IntAct=EBI-475646, EBI-744302;
CC P07196; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-475646, EBI-8799578;
CC P07196; Q08379: GOLGA2; NbExp=3; IntAct=EBI-475646, EBI-618309;
CC P07196; Q9BQQ3: GORASP1; NbExp=3; IntAct=EBI-475646, EBI-2561458;
CC P07196; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-475646, EBI-14103818;
CC P07196; Q14005-2: IL16; NbExp=3; IntAct=EBI-475646, EBI-17178971;
CC P07196; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-475646, EBI-739493;
CC P07196; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-475646, EBI-14069005;
CC P07196; Q6P597-2: KLC3; NbExp=3; IntAct=EBI-475646, EBI-11033402;
CC P07196; P13646: KRT13; NbExp=3; IntAct=EBI-475646, EBI-1223876;
CC P07196; P19012: KRT15; NbExp=3; IntAct=EBI-475646, EBI-739566;
CC P07196; P05783: KRT18; NbExp=3; IntAct=EBI-475646, EBI-297888;
CC P07196; P08727: KRT19; NbExp=3; IntAct=EBI-475646, EBI-742756;
CC P07196; Q14525: KRT33B; NbExp=3; IntAct=EBI-475646, EBI-1049638;
CC P07196; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-475646, EBI-10261141;
CC P07196; Q14847-2: LASP1; NbExp=3; IntAct=EBI-475646, EBI-9088686;
CC P07196; A2RU56: LOC401296; NbExp=3; IntAct=EBI-475646, EBI-9088215;
CC P07196; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-475646, EBI-10182361;
CC P07196; P51608: MECP2; NbExp=3; IntAct=EBI-475646, EBI-1189067;
CC P07196; Q15049: MLC1; NbExp=3; IntAct=EBI-475646, EBI-8475277;
CC P07196; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-475646, EBI-10699187;
CC P07196; Q13614: MTMR2; NbExp=2; IntAct=EBI-475646, EBI-475631;
CC P07196; Q99608: NDN; NbExp=4; IntAct=EBI-475646, EBI-718177;
CC P07196; O76041: NEBL; NbExp=3; IntAct=EBI-475646, EBI-2880203;
CC P07196; P07197: NEFM; NbExp=4; IntAct=EBI-475646, EBI-1105035;
CC P07196; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-475646, EBI-11750983;
CC P07196; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-475646, EBI-744782;
CC P07196; Q6X4W1-6: NSMF; NbExp=3; IntAct=EBI-475646, EBI-25842707;
CC P07196; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-475646, EBI-1210753;
CC P07196; O43482: OIP5; NbExp=3; IntAct=EBI-475646, EBI-536879;
CC P07196; Q9P286: PAK5; NbExp=3; IntAct=EBI-475646, EBI-741896;
CC P07196; Q9BRX2: PELO; NbExp=3; IntAct=EBI-475646, EBI-1043580;
CC P07196; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-475646, EBI-12339509;
CC P07196; Q16512: PKN1; NbExp=3; IntAct=EBI-475646, EBI-602382;
CC P07196; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-475646, EBI-2557469;
CC P07196; Q8NI37: PPTC7; NbExp=3; IntAct=EBI-475646, EBI-9089276;
CC P07196; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-475646, EBI-746228;
CC P07196; Q96PK6: RBM14; NbExp=3; IntAct=EBI-475646, EBI-954272;
CC P07196; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-475646, EBI-1504830;
CC P07196; Q8TCX5: RHPN1; NbExp=3; IntAct=EBI-475646, EBI-746325;
CC P07196; Q8N488: RYBP; NbExp=3; IntAct=EBI-475646, EBI-752324;
CC P07196; P25815: S100P; NbExp=3; IntAct=EBI-475646, EBI-743700;
CC P07196; P12757: SKIL; NbExp=6; IntAct=EBI-475646, EBI-2902468;
CC P07196; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-475646, EBI-8463848;
CC P07196; Q13573: SNW1; NbExp=3; IntAct=EBI-475646, EBI-632715;
CC P07196; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-475646, EBI-11959123;
CC P07196; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-475646, EBI-11285923;
CC P07196; Q9BQG1: SYT3; NbExp=3; IntAct=EBI-475646, EBI-17284568;
CC P07196; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-475646, EBI-18173581;
CC P07196; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-475646, EBI-745958;
CC P07196; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-475646, EBI-3923210;
CC P07196; Q13569: TDG; NbExp=3; IntAct=EBI-475646, EBI-348333;
CC P07196; P54274: TERF1; NbExp=2; IntAct=EBI-475646, EBI-710997;
CC P07196; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-475646, EBI-9090990;
CC P07196; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-475646, EBI-10964469;
CC P07196; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-475646, EBI-9088812;
CC P07196; O75604: USP2; NbExp=3; IntAct=EBI-475646, EBI-743272;
CC P07196; P45880: VDAC2; NbExp=3; IntAct=EBI-475646, EBI-354022;
CC P07196; P08670: VIM; NbExp=3; IntAct=EBI-475646, EBI-353844;
CC P07196; P58304: VSX2; NbExp=3; IntAct=EBI-475646, EBI-6427899;
CC P07196; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-475646, EBI-14104088;
CC P07196; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-475646, EBI-2602314;
CC P07196; Q9UJW8-4: ZNF180; NbExp=3; IntAct=EBI-475646, EBI-12055755;
CC P07196; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-475646, EBI-12988373;
CC P07196; Q9C0F3: ZNF436; NbExp=3; IntAct=EBI-475646, EBI-8489702;
CC P07196; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-475646, EBI-25831733;
CC P07196; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-475646, EBI-8490788;
CC P07196; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-475646, EBI-10172590;
CC P07196; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-475646, EBI-12939666;
CC P07196; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-475646, EBI-18036029;
CC P07196; O15535: ZSCAN9; NbExp=3; IntAct=EBI-475646, EBI-751531;
CC P07196; Q86V28; NbExp=3; IntAct=EBI-475646, EBI-10259496;
CC P07196; P14079: tax; Xeno; NbExp=4; IntAct=EBI-475646, EBI-9675698;
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P08551}.
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:0000250}.
CC -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC leading to the inhibition of polymerization.
CC {ECO:0000269|PubMed:8621664}.
CC -!- PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 1F (CMT1F) [MIM:607734]: A
CC dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder
CC of the peripheral nervous system, characterized by progressive weakness
CC and atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are
CC characterized by severely reduced nerve conduction velocities (less
CC than 38 m/sec), segmental demyelination and remyelination with onion
CC bulb formations on nerve biopsy, slowly progressive distal muscle
CC atrophy and weakness, absent deep tendon reflexes, and hollow feet.
CC CMT1F is characterized by onset in infancy or childhood (range 1 to 13
CC years). {ECO:0000269|PubMed:12566280, ECO:0000269|PubMed:15241803}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2E (CMT2E) [MIM:607684]: A
CC dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the
CC peripheral nervous system, characterized by progressive weakness and
CC atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group
CC are characterized by signs of axonal degeneration in the absence of
CC obvious myelin alterations, normal or slightly reduced nerve conduction
CC velocities, and progressive distal muscle weakness and atrophy.
CC {ECO:0000269|PubMed:10841809, ECO:0000269|PubMed:11220745,
CC ECO:0000269|PubMed:12481988, ECO:0000269|PubMed:15241803,
CC ECO:0000269|PubMed:17052987, ECO:0000269|PubMed:22206013,
CC ECO:0000269|PubMed:25802885}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease, dominant intermediate G (CMTDIG)
CC [MIM:617882]: An autosomal dominant, intermediate form of Charcot-
CC Marie-Tooth disease, a disorder of the peripheral nervous system,
CC characterized by progressive weakness and atrophy, initially of the
CC peroneal muscles and later of the distal muscles of the arms. Dominant
CC intermediate forms are characterized by clinical and pathologic
CC features intermediate between demyelinating and axonal peripheral
CC neuropathies, and motor median nerve conduction velocities ranging from
CC 25 to 45 m/sec. CMTDIG is phenotypically variable. Most affected
CC individuals have onset in the first or second decades of slowly
CC progressive distal motor weakness and atrophy, resulting in gait
CC instability and distal upper limb impairment, as well as distal sensory
CC impairment. {ECO:0000269|PubMed:14733962, ECO:0000269|PubMed:17052987,
CC ECO:0000269|PubMed:25877835, ECO:0000269|PubMed:26645395}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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}.
CC -!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
CC URL="https://uantwerpen.vib.be/CMTMutations";
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC ---------------------------------------------------------------------------
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DR EMBL; X05608; CAA29097.1; -; Genomic_DNA.
DR EMBL; AY156690; AAN74826.1; -; mRNA.
DR EMBL; AC107373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63598.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63599.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63600.1; -; Genomic_DNA.
DR EMBL; BC039237; AAH39237.1; -; mRNA.
DR EMBL; S70309; AAD14057.1; -; Genomic_DNA.
DR CCDS; CCDS75712.1; -.
DR PIR; S07144; S07144.
DR RefSeq; NP_006149.2; NM_006158.4.
DR AlphaFoldDB; P07196; -.
DR SMR; P07196; -.
DR BioGRID; 110822; 125.
DR IntAct; P07196; 144.
DR MINT; P07196; -.
DR STRING; 9606.ENSP00000482169; -.
DR GlyGen; P07196; 22 sites, 1 O-linked glycan (20 sites).
DR iPTMnet; P07196; -.
DR PhosphoSitePlus; P07196; -.
DR SwissPalm; P07196; -.
DR BioMuta; NEFL; -.
DR DMDM; 62511894; -.
DR UCD-2DPAGE; P07196; -.
DR EPD; P07196; -.
DR jPOST; P07196; -.
DR MassIVE; P07196; -.
DR MaxQB; P07196; -.
DR PeptideAtlas; P07196; -.
DR PRIDE; P07196; -.
DR ProteomicsDB; 51961; -.
DR ABCD; P07196; 1 sequenced antibody.
DR Antibodypedia; 73404; 1087 antibodies from 41 providers.
DR DNASU; 4747; -.
DR Ensembl; ENST00000610854.2; ENSP00000482169.2; ENSG00000277586.4.
DR GeneID; 4747; -.
DR KEGG; hsa:4747; -.
DR MANE-Select; ENST00000610854.2; ENSP00000482169.2; NM_006158.5; NP_006149.2.
DR UCSC; uc033bfe.2; human.
DR CTD; 4747; -.
DR DisGeNET; 4747; -.
DR GeneCards; NEFL; -.
DR GeneReviews; NEFL; -.
DR HGNC; HGNC:7739; NEFL.
DR HPA; ENSG00000277586; Tissue enriched (brain).
DR MalaCards; NEFL; -.
DR MIM; 162280; gene.
DR MIM; 607684; phenotype.
DR MIM; 607734; phenotype.
DR MIM; 617882; phenotype.
DR neXtProt; NX_P07196; -.
DR OpenTargets; ENSG00000277586; -.
DR Orphanet; 99939; Autosomal dominant Charcot-Marie-Tooth disease type 2E.
DR Orphanet; 101085; Charcot-Marie-Tooth disease type 1F.
DR Orphanet; 228374; Charcot-Marie-Tooth disease type 2B5.
DR PharmGKB; PA31542; -.
DR VEuPathDB; HostDB:ENSG00000277586; -.
DR eggNOG; ENOG502QSXY; Eukaryota.
DR GeneTree; ENSGT00940000156208; -.
DR HOGENOM; CLU_012560_7_3_1; -.
DR InParanoid; P07196; -.
DR OMA; YEPYYAT; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P07196; -.
DR PathwayCommons; P07196; -.
DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR Reactome; R-HSA-9620244; Long-term potentiation.
DR SignaLink; P07196; -.
DR SIGNOR; P07196; -.
DR BioGRID-ORCS; 4747; 10 hits in 203 CRISPR screens.
DR ChiTaRS; NEFL; human.
DR GeneWiki; NEFL; -.
DR GenomeRNAi; 4747; -.
DR Pharos; P07196; Tbio.
DR PRO; PR:P07196; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P07196; protein.
DR Bgee; ENSG00000277586; Expressed in dorsal root ganglion and 157 other tissues.
DR Genevisible; P07196; HS.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005883; C:neurofilament; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0099182; C:presynaptic intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
DR GO; GO:0045105; P:intermediate filament polymerization or depolymerization; IEA:Ensembl.
DR GO; GO:0040011; P:locomotion; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0033693; P:neurofilament bundle assembly; IDA:UniProtKB.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
DR GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
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; Charcot-Marie-Tooth disease; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant;
KW Glycoprotein; Intermediate filament; Methylation; Neurodegeneration;
KW Neuropathy; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..543
FT /note="Neurofilament light polypeptide"
FT /id="PRO_0000063787"
FT DOMAIN 90..400
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..92
FT /note="Head"
FT REGION 93..124
FT /note="Coil 1A"
FT REGION 125..137
FT /note="Linker 1"
FT REGION 138..234
FT /note="Coil 1B"
FT REGION 235..252
FT /note="Linker 12"
FT REGION 253..271
FT /note="Coil 2A"
FT REGION 272..280
FT /note="Linker 2"
FT REGION 281..396
FT /note="Coil 2B"
FT REGION 381..391
FT /note="Epitope; recognized by IF-specific monoclonal
FT antibody"
FT REGION 397..543
FT /note="Tail"
FT REGION 397..443
FT /note="Tail, subdomain A"
FT REGION 444..543
FT /note="Tail, subdomain B (acidic)"
FT REGION 462..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..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:0007744|PubMed:22223895"
FT MOD_RES 23
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 23
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 30
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
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 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
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 VARIANT 7
FT /note="E -> K (in a Charcot-Marie-Tooth disease patient;
FT dbSNP:rs57848467)"
FT /evidence="ECO:0000269|PubMed:12566280"
FT /id="VAR_016017"
FT VARIANT 8
FT /note="P -> L (in CMT1F; dbSNP:rs61491953)"
FT /evidence="ECO:0000269|PubMed:12566280"
FT /id="VAR_016018"
FT VARIANT 8
FT /note="P -> Q (in CMT1F; dbSNP:rs61491953)"
FT /evidence="ECO:0000269|PubMed:12566280"
FT /id="VAR_016019"
FT VARIANT 8
FT /note="P -> R (in CMT2E and CMT1F; dbSNP:rs60261494)"
FT /evidence="ECO:0000269|PubMed:11220745,
FT ECO:0000269|PubMed:12566280, ECO:0000269|PubMed:22206013"
FT /id="VAR_016020"
FT VARIANT 22
FT /note="P -> S (in CMT2E; dbSNP:rs28928910)"
FT /evidence="ECO:0000269|PubMed:12481988,
FT ECO:0000269|PubMed:17052987, ECO:0000269|PubMed:22206013"
FT /id="VAR_016021"
FT VARIANT 90
FT /note="E -> K (in CMT1F; dbSNP:rs58332872)"
FT /evidence="ECO:0000269|PubMed:12566280"
FT /id="VAR_016022"
FT VARIANT 98
FT /note="N -> S (in CMT1F and CMTDIG; dbSNP:rs58982919)"
FT /evidence="ECO:0000269|PubMed:12566280,
FT ECO:0000269|PubMed:26645395"
FT /id="VAR_016023"
FT VARIANT 213
FT /note="I -> M (in dbSNP:rs62636522)"
FT /evidence="ECO:0000269|PubMed:17052987"
FT /id="VAR_081565"
FT VARIANT 265
FT /note="Y -> C (in CMT2E; unknown pathological significance;
FT dbSNP:rs587777880)"
FT /evidence="ECO:0000269|PubMed:25802885"
FT /id="VAR_081566"
FT VARIANT 268
FT /note="L -> P (in CMT2E; dbSNP:rs62636502)"
FT /evidence="ECO:0000269|PubMed:17052987,
FT ECO:0000269|PubMed:25802885"
FT /id="VAR_081567"
FT VARIANT 322..326
FT /note="Missing (in CMT2E; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:17052987"
FT /id="VAR_081568"
FT VARIANT 332
FT /note="Q -> P (in CMT2E; dbSNP:rs59443585)"
FT /evidence="ECO:0000269|PubMed:10841809"
FT /id="VAR_009703"
FT VARIANT 336
FT /note="L -> P (in CMT2E; unknown pathological significance;
FT dbSNP:rs587777881)"
FT /evidence="ECO:0000269|PubMed:15241803,
FT ECO:0000269|PubMed:25802885"
FT /id="VAR_021613"
FT VARIANT 396
FT /note="E -> K (in CMTDIG and CMT2E; dbSNP:rs62636503)"
FT /evidence="ECO:0000269|PubMed:14733962,
FT ECO:0000269|PubMed:15241803, ECO:0000269|PubMed:17052987,
FT ECO:0000269|PubMed:22206013, ECO:0000269|PubMed:25877835"
FT /id="VAR_021614"
FT VARIANT 440
FT /note="P -> L (in CMT2E; unknown pathological significance;
FT dbSNP:rs587777882)"
FT /evidence="ECO:0000269|PubMed:25802885"
FT /id="VAR_081569"
FT VARIANT 468
FT /note="D -> N (in dbSNP:rs57153321)"
FT /evidence="ECO:0000269|PubMed:12566280,
FT ECO:0000269|PubMed:17052987"
FT /id="VAR_016024"
FT VARIANT 527
FT /note="Missing (in CMT1F; dbSNP:rs3832558)"
FT /evidence="ECO:0000269|PubMed:12566280"
FT /id="VAR_016025"
FT CONFLICT 28
FT /note="Missing (in Ref. 1; CAA29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="N -> TN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="Q -> R (in Ref. 1; CAA29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> EE (in Ref. 1; CAA29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> R (in Ref. 1; CAA29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="I -> T (in Ref. 1; CAA29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="A -> S (in Ref. 1; CAA29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="S -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 61517 MW; 98C1712D8ACFF33A CRC64;
MSSFSYEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA
ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE
EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI SFLKKVHEEE IAELQAQIQY
AQISVEMDVT KPDLSAALKD IRAQYEKLAA KNMQNAEEWF KSRFTVLTES AAKNTDAVRA
AKDEVSESRR LLKAKTLEIE ACRGMNEALE KQLQELEDKQ NADISAMQDT INKLENELRT
TKSEMARYLK EYQDLLNVKM ALDIEIAAYR KLLEGEETRL SFTSVGSITS GYSQSSQVFG
RSAYGGLQTS SYLMSTRSFP SYYTSHVQEE QIEVEETIEA AKAEEAKDEP PSEGEAEEEE
KDKEEAEEEE AAEEEEAAKE ESEEAKEEEE GGEGEEGEET KEAEEEEKKV EGAGEEQAAK
KKD
