NFH_HUMAN
ID NFH_HUMAN Reviewed; 1026 AA.
AC P12036; B4DYY4; Q96HF8; Q9UJS7; Q9UQ14;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Neurofilament heavy polypeptide;
DE Short=NF-H;
DE AltName: Full=200 kDa neurofilament protein;
DE AltName: Full=Neurofilament triplet H protein;
GN Name=NEFH; Synonyms=KIAA0845, NFH;
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], AND VARIANT ALA-811.
RX PubMed=3138108; DOI=10.1002/j.1460-2075.1988.tb03032.x;
RA Lees J.F., Shneidman P.S., Skuntz S.F., Carden M.J., Lazzarini R.A.;
RT "The structure and organization of the human heavy neurofilament subunit
RT (NF-H) and the gene encoding it.";
RL EMBO J. 7:1947-1955(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhu Y., Han Y.;
RT "Molecular Cloning of human hSTE cDNA.";
RL Beijing Yi Ke Da Xue Xue Bao 31:531-531(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 606-1026 (ISOFORM 2).
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-574; SER-628;
RP SER-674 AND SER-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN CMT2CC.
RX PubMed=27040688; DOI=10.1016/j.ajhg.2016.02.022;
RA Rebelo A.P., Abrams A.J., Cottenie E., Horga A., Gonzalez M., Bis D.M.,
RA Sanchez-Mejias A., Pinto M., Buglo E., Markel K., Prince J., Laura M.,
RA Houlden H., Blake J., Woodward C., Sweeney M.G., Holton J.L., Hanna M.,
RA Dallman J.E., Auer-Grumbach M., Reilly M.M., Zuchner S.;
RT "Cryptic amyloidogenic elements in the 3' UTRs of neurofilament genes
RT trigger axonal neuropathy.";
RL Am. J. Hum. Genet. 98:597-614(2016).
RN [10]
RP VARIANT ALS LYS-796 DEL.
RX PubMed=7849698; DOI=10.1093/hmg/3.10.1757;
RA Figlewicz D.A., Krizus A., Martinoli M.G., Meininger V., Dib M.,
RA Rouleau G.A., Julien J.-P.;
RT "Variants of the heavy neurofilament subunit are associated with the
RT development of amyotrophic lateral sclerosis.";
RL Hum. Mol. Genet. 3:1757-1761(1994).
CC -!- FUNCTION: Neurofilaments usually contain three intermediate filament
CC proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of
CC neuronal caliber. NEFH has an important function in mature axons that
CC is not subserved by the two smaller NF proteins. May additionally
CC cooperate with the neuronal intermediate filament proteins PRPH and INA
CC to form neuronal filamentous networks (By similarity).
CC {ECO:0000250|UniProtKB:P19246}.
CC -!- SUBUNIT: Forms heterodimers with NEFL; which can further hetero-
CC oligomerize (in vitro) (By similarity). Forms heterodimers with INA (in
CC vitro) (By similarity). {ECO:0000250|UniProtKB:P16884}.
CC -!- INTERACTION:
CC P12036; P05067: APP; NbExp=3; IntAct=EBI-2880271, EBI-77613;
CC P12036; P10809: HSPD1; NbExp=3; IntAct=EBI-2880271, EBI-352528;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:27040688}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P19246}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12036-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12036-2; Sequence=VSP_036706;
CC -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFH is
CC phosphorylated on a number of the serines in this motif. It is thought
CC that phosphorylation of NFH results in the formation of interfilament
CC cross bridges that are important in the maintenance of axonal caliber.
CC {ECO:0000269|PubMed:8621664}.
CC -!- PTM: Phosphorylation seems to play a major role in the functioning of
CC the larger neurofilament polypeptides (NF-M and NF-H), the levels of
CC phosphorylation being altered developmentally and coincidentally with a
CC change in the neurofilament function. {ECO:0000269|PubMed:8621664}.
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 -!- POLYMORPHISM: The number of repeats is shown to vary between 29 and 30.
CC -!- DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A
CC neurodegenerative disorder affecting upper motor neurons in the brain
CC and lower motor neurons in the brain stem and spinal cord, resulting in
CC fatal paralysis. Sensory abnormalities are absent. The pathologic
CC hallmarks of the disease include pallor of the corticospinal tract due
CC to loss of motor neurons, presence of ubiquitin-positive inclusions
CC within surviving motor neurons, and deposition of pathologic
CC aggregates. The etiology of amyotrophic lateral sclerosis is likely to
CC be multifactorial, involving both genetic and environmental factors.
CC The disease is inherited in 5-10% of the cases.
CC {ECO:0000269|PubMed:7849698}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2CC (CMT2CC) [MIM:616924]: An
CC 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:27040688}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74868.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG63896.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
CC -!- WEB RESOURCE: Name=Alsod; Note=ALS genetic mutations db;
CC URL="https://alsod.ac.uk/";
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DR EMBL; X15306; CAA33366.1; -; Genomic_DNA.
DR EMBL; X15307; CAA33366.1; JOINED; Genomic_DNA.
DR EMBL; X15308; CAA33366.1; JOINED; Genomic_DNA.
DR EMBL; X15309; CAA33366.1; JOINED; Genomic_DNA.
DR EMBL; AF203032; AAF13722.1; -; mRNA.
DR EMBL; AB020652; BAA74868.2; ALT_INIT; mRNA.
DR EMBL; AK302660; BAG63896.1; ALT_INIT; mRNA.
DR EMBL; AC000035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008648; AAH08648.1; -; mRNA.
DR EMBL; BC073969; AAH73969.1; -; mRNA.
DR PIR; S00979; QFHUH.
DR RefSeq; NP_066554.2; NM_021076.3.
DR AlphaFoldDB; P12036; -.
DR SMR; P12036; -.
DR BioGRID; 110819; 56.
DR IntAct; P12036; 32.
DR MINT; P12036; -.
DR STRING; 9606.ENSP00000311997; -.
DR CarbonylDB; P12036; -.
DR GlyGen; P12036; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P12036; -.
DR PhosphoSitePlus; P12036; -.
DR SwissPalm; P12036; -.
DR BioMuta; NEFH; -.
DR DMDM; 226726294; -.
DR UCD-2DPAGE; P12036; -.
DR EPD; P12036; -.
DR jPOST; P12036; -.
DR MassIVE; P12036; -.
DR MaxQB; P12036; -.
DR PaxDb; P12036; -.
DR PeptideAtlas; P12036; -.
DR PRIDE; P12036; -.
DR ProteomicsDB; 52821; -. [P12036-1]
DR ProteomicsDB; 52822; -. [P12036-2]
DR Antibodypedia; 3579; 1697 antibodies from 47 providers.
DR DNASU; 4744; -.
DR Ensembl; ENST00000310624.7; ENSP00000311997.6; ENSG00000100285.10.
DR GeneID; 4744; -.
DR KEGG; hsa:4744; -.
DR UCSC; uc003afo.4; human. [P12036-1]
DR CTD; 4744; -.
DR DisGeNET; 4744; -.
DR GeneCards; NEFH; -.
DR GeneReviews; NEFH; -.
DR HGNC; HGNC:7737; NEFH.
DR HPA; ENSG00000100285; Group enriched (brain, prostate).
DR MalaCards; NEFH; -.
DR MIM; 105400; phenotype.
DR MIM; 162230; gene.
DR MIM; 616924; phenotype.
DR neXtProt; NX_P12036; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR PharmGKB; PA31540; -.
DR VEuPathDB; HostDB:ENSG00000100285; -.
DR eggNOG; ENOG502QYDU; Eukaryota.
DR HOGENOM; CLU_012560_7_2_1; -.
DR InParanoid; P12036; -.
DR OrthoDB; 898483at2759; -.
DR PhylomeDB; P12036; -.
DR TreeFam; TF330122; -.
DR PathwayCommons; P12036; -.
DR SignaLink; P12036; -.
DR SIGNOR; P12036; -.
DR BioGRID-ORCS; 4744; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; NEFH; human.
DR GenomeRNAi; 4744; -.
DR Pharos; P12036; Tbio.
DR PRO; PR:P12036; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P12036; protein.
DR Bgee; ENSG00000100285; Expressed in dorsal root ganglion and 162 other tissues.
DR Genevisible; P12036; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
DR GO; GO:0097418; C:neurofibrillary tangle; IDA:BHF-UCL.
DR GO; GO:0005883; C:neurofilament; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0070840; F:dynein complex binding; TAS:BHF-UCL.
DR GO; GO:0019894; F:kinesin binding; TAS:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; TAS:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0061564; P:axon development; IMP:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; TAS:BHF-UCL.
DR GO; GO:0030031; P:cell projection assembly; TAS:BHF-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0033693; P:neurofilament bundle assembly; IMP:BHF-UCL.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IEA:Ensembl.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IMP:BHF-UCL.
DR InterPro; IPR010790; DUF1388.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR033183; NF-H.
DR PANTHER; PTHR23214; PTHR23214; 2.
DR Pfam; PF07142; DUF1388; 11.
DR Pfam; PF00038; Filament; 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 Alternative splicing; Amyotrophic lateral sclerosis; Cell projection;
KW Charcot-Marie-Tooth disease; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Intermediate filament; Neurodegeneration; Neuropathy;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1026
FT /note="Neurofilament heavy polypeptide"
FT /id="PRO_0000063800"
FT DOMAIN 97..413
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REPEAT 525..530
FT /note="1"
FT REPEAT 531..536
FT /note="2"
FT REPEAT 539..544
FT /note="3"
FT REPEAT 545..550
FT /note="4"
FT REPEAT 559..564
FT /note="5"
FT REPEAT 573..578
FT /note="6"
FT REPEAT 579..584
FT /note="7"
FT REPEAT 593..598
FT /note="8"
FT REPEAT 599..604
FT /note="9"
FT REPEAT 613..618
FT /note="10"
FT REPEAT 627..632
FT /note="11"
FT REPEAT 633..638
FT /note="12"
FT REPEAT 647..652
FT /note="13"
FT REPEAT 653..658
FT /note="14"
FT REPEAT 667..672
FT /note="15"
FT REPEAT 673..678
FT /note="16"
FT REPEAT 681..686
FT /note="17"
FT REPEAT 687..692
FT /note="18"
FT REPEAT 695..700
FT /note="19"
FT REPEAT 701..706
FT /note="20"
FT REPEAT 709..714
FT /note="21"
FT REPEAT 715..720
FT /note="22"
FT REPEAT 723..728
FT /note="23"
FT REPEAT 729..734
FT /note="24"
FT REPEAT 743..748
FT /note="25"
FT REPEAT 751..756
FT /note="26"
FT REPEAT 768..773
FT /note="27"
FT REPEAT 792..797
FT /note="28"
FT REPEAT 800..805
FT /note="29"
FT REPEAT 827..832
FT /note="30"
FT REGION 1..100
FT /note="Head"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..132
FT /note="Coil 1A"
FT REGION 133..145
FT /note="Linker 1"
FT REGION 146..244
FT /note="Coil 1B"
FT REGION 245..266
FT /note="Linker 12"
FT REGION 267..288
FT /note="Coil 2A"
FT REGION 289..292
FT /note="Linker 2"
FT REGION 293..413
FT /note="Coil 2B"
FT REGION 414..1026
FT /note="Tail"
FT REGION 456..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..832
FT /note="30 X 6 AA repeats of K-S-P-[AEPV]-[EAK]-[AEVK]"
FT COMPBIAS 58..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT VAR_SEQ 750..812
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036706"
FT VARIANT 575
FT /note="P -> S (in dbSNP:rs6006164)"
FT /id="VAR_054787"
FT VARIANT 615
FT /note="P -> L (in dbSNP:rs5763269)"
FT /id="VAR_056025"
FT VARIANT 796
FT /note="Missing (in ALS)"
FT /evidence="ECO:0000269|PubMed:7849698"
FT /id="VAR_023063"
FT VARIANT 811
FT /note="E -> A (in dbSNP:rs165602)"
FT /evidence="ECO:0000269|PubMed:3138108"
FT /id="VAR_026163"
FT CONFLICT 647..652
FT /note="Missing (in Ref. 1; CAA33366 and 5; AC000035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1026 AA; 112479 MW; 0879B6A08D208C17 CRC64;
MMSFGGADAL LGAPFAPLHG GGSLHYALAR KGGAGGTRSA AGSSSGFHSW TRTSVSSVSA
SPSRFRGAGA ASSTDSLDTL SNGPEGCMVA VATSRSEKEQ LQALNDRFAG YIDKVRQLEA
HNRSLEGEAA ALRQQQAGRS AMGELYEREV REMRGAVLRL GAARGQLRLE QEHLLEDIAH
VRQRLDDEAR QREEAEAAAR ALARFAQEAE AARVDLQKKA QALQEECGYL RRHHQEEVGE
LLGQIQGSGA AQAQMQAETR DALKCDVTSA LREIRAQLEG HAVQSTLQSE EWFRVRLDRL
SEAAKVNTDA MRSAQEEITE YRRQLQARTT ELEALKSTKD SLERQRSELE DRHQADIASY
QEAIQQLDAE LRNTKWEMAA QLREYQDLLN VKMALDIEIA AYRKLLEGEE CRIGFGPIPF
SLPEGLPKIP SVSTHIKVKS EEKIKVVEKS EKETVIVEEQ TEETQVTEEV TEEEEKEAKE
EEGKEEEGGE EEEAEGGEEE TKSPPAEEAA SPEKEAKSPV KEEAKSPAEA KSPEKEEAKS
PAEVKSPEKA KSPAKEEAKS PPEAKSPEKE EAKSPAEVKS PEKAKSPAKE EAKSPAEAKS
PEKAKSPVKE EAKSPAEAKS PVKEEAKSPA EVKSPEKAKS PTKEEAKSPE KAKSPEKAKS
PEKEEAKSPE KAKSPVKAEA KSPEKAKSPV KAEAKSPEKA KSPVKEEAKS PEKAKSPVKE
EAKSPEKAKS PVKEEAKTPE KAKSPVKEEA KSPEKAKSPE KAKTLDVKSP EAKTPAKEEA
RSPADKFPEK AKSPVKEEVK SPEKAKSPLK EDAKAPEKEI PKKEEVKSPV KEEEKPQEVK
VKEPPKKAEE EKAPATPKTE EKKDSKKEEA PKKEAPKPKV EEKKEPAVEK PKESKVEAKK
EEAEDKKKVP TPEKEAPAKV EVKEDAKPKE KTEVAKKEPD DAKAKEPSKP AEKKEAAPEK
KDTKEEKAKK PEEKPKTEAK AKEDDKTLSK EPSKPKAEKA EKSSSTDQKD SKPPEKATED
KAAKGK
