ID NFM_MOUSE Reviewed; 848 AA.
AC P08553; A2VCT5; Q0VDM8; Q3HRJ6; Q3TNS4; Q3TPK2; Q61961; Q8BQ20;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 24-JAN-2024, entry version 208.
DE RecName: Full=Neurofilament medium polypeptide;
DE Short=NF-M;
DE AltName: Full=160 kDa neurofilament protein;
DE AltName: Full=Neurofilament 3;
DE AltName: Full=Neurofilament triplet M protein;
GN Name=Nefm; Synonyms=Nef3, Nfm;
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 [GENOMIC DNA].
RX PubMed=3036526; DOI=10.1111/j.1432-1033.1987.tb13485.x;
RA Levy E., Liem R.K.H., D'Eustachio P., Cowan N.J.;
RT "Structure and evolutionary origin of the gene encoding mouse NF-M, the
RT middle-molecular-mass neurofilament protein.";
RL Eur. J. Biochem. 166:71-77(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Jensen K.H., Brown A.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-848.
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 PROTEIN SEQUENCE OF 167-182; 222-233 AND 410-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 322-540.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, AND IDENTIFICATION BY
RP 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-610; THR-642; SER-669 AND
RP SER-715, AND 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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-430.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-318, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-224; SER-550;
RP SER-551; THR-565; SER-605; SER-610; SER-715; SER-723 AND SER-769, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-42, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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 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:P12839}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22723690}. Cell projection, axon
CC {ECO:0000269|PubMed:22723690}.
CC -!- TISSUE SPECIFICITY: Expressed in the sciatic nerve (at protein level).
CC {ECO:0000269|PubMed:22723690}.
CC -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFM is
CC phosphorylated on a number of the serines in this motif. It is thought
CC that phosphorylation of NFM results in the formation of interfilament
CC cross bridges that are important in the maintenance of axonal caliber.
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.
CC -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC leading to the inhibition of polymerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X05640; CAA29127.1; -; Genomic_DNA.
DR EMBL; DQ201636; ABA46749.1; -; mRNA.
DR EMBL; AK051696; BAC34724.1; -; mRNA.
DR EMBL; AK164318; BAE37734.1; -; mRNA.
DR EMBL; AK165041; BAE38014.1; -; mRNA.
DR EMBL; BC119602; AAI19603.1; -; mRNA.
DR EMBL; BC128564; AAI28565.1; -; mRNA.
DR EMBL; M20481; AAA39815.1; -; mRNA.
DR CCDS; CCDS27233.1; -.
DR PIR; B43772; B43772.
DR PIR; S00030; S00030.
DR RefSeq; NP_032717.2; NM_008691.2.
DR AlphaFoldDB; P08553; -.
DR SMR; P08553; -.
DR BioGRID; 201758; 22.
DR IntAct; P08553; 13.
DR MINT; P08553; -.
DR STRING; 10090.ENSMUSP00000022638; -.
DR GlyCosmos; P08553; 2 sites, No reported glycans.
DR GlyGen; P08553; 16 sites, 1 O-linked glycan (16 sites).
DR iPTMnet; P08553; -.
DR PhosphoSitePlus; P08553; -.
DR SwissPalm; P08553; -.
DR UCD-2DPAGE; P08553; -.
DR EPD; P08553; -.
DR jPOST; P08553; -.
DR MaxQB; P08553; -.
DR PaxDb; 10090-ENSMUSP00000022638; -.
DR PeptideAtlas; P08553; -.
DR ProteomicsDB; 252818; -.
DR DNASU; 18040; -.
DR GeneID; 18040; -.
DR KEGG; mmu:18040; -.
DR UCSC; uc007ulo.1; mouse.
DR AGR; MGI:97314; -.
DR CTD; 4741; -.
DR MGI; MGI:97314; Nefm.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P08553; -.
DR OrthoDB; 4640531at2759; -.
DR PhylomeDB; P08553; -.
DR TreeFam; TF330122; -.
DR BioGRID-ORCS; 18040; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Nefm; mouse.
DR PRO; PR:P08553; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P08553; Protein.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0097418; C:neurofibrillary tangle; ISO:MGI.
DR GO; GO:0005883; C:neurofilament; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; 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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IGI:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
DR GO; GO:0045105; P:intermediate filament polymerization or depolymerization; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR GO; GO:0033693; P:neurofilament bundle assembly; ISO:MGI.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR PANTHER; PTHR45652:SF3; NEUROFILAMENT MEDIUM POLYPEPTIDE; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT CHAIN 2..848
FT /note="Neurofilament medium polypeptide"
FT /id="PRO_0000063795"
FT DOMAIN 99..410
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..102
FT /note="Head"
FT REGION 103..134
FT /note="Coil 1A"
FT REGION 135..147
FT /note="Linker 1"
FT REGION 148..246
FT /note="Coil 1B"
FT REGION 247..263
FT /note="Linker 12"
FT REGION 264..285
FT /note="Coil 2A"
FT REGION 286..289
FT /note="Linker 2"
FT REGION 290..410
FT /note="Coil 2B"
FT REGION 411..848
FT /note="Tail"
FT REGION 482..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..537
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..785
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:O77788"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 42
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 642
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 47
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000305|PubMed:16452088"
FT CARBOHYD 430
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000305|PubMed:16452088"
FT CONFLICT 17
FT /note="V -> VP (in Ref. 1; CAA29127)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="K -> T (in Ref. 1; CAA29127)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> V (in Ref. 1; CAA29127)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="S -> R (in Ref. 1; CAA29127)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="S -> F (in Ref. 6; AAA39815)"
FT /evidence="ECO:0000305"
FT CONFLICT 539..540
FT /note="QA -> RR (in Ref. 6; AAA39815)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="Q -> H (in Ref. 2; ABA46749 and 3; BAC34724/
FT BAE37734)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="E -> K (in Ref. 3; BAC34724)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="P -> L (in Ref. 2; ABA46749 and 3; BAC34724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 95916 MW; 0783F50558A7D4C3 CRC64;
MSYTLDSLGN PSAYRRVTET RSSFSRVSGS PSSGFRSQSW SRGSPSTVSS SYKRSALAPR
LAYSSAMLSS AESSLDFSQS SSLLNGGSGG DYKLSRSNEK EQLQGLNDRF AGYIEKVHYL
EQQNKEIEAE IQALRQKQAS HAQLGDAYDQ EIRELRATLE MVNHEKAQVQ LDSDHLEEDI
HRLKERFEEE ARLRDDTEAA IRALRKDIEE SSMVKVELDK KVQSLQDEVA FLRSNHEEEV
ADLLAQIQAS HITVERKDYL KTDISTALKE IRSQLECHSD QNMHQAEEWF KCRYAKLTEA
AEQNKEAIRS AKEEIAEYRR QLQSKSIELE SVRGTKESLE RQLSDIEERH NHDLSSYQDT
IQQLENELRG TKWEMARHLR EYQDLLNVKM ALDIEIAAYR KLLEGEETRF STFSGSITGP
LYTHRQPSVT ISSKIQKTKV EAPKLKVQHK FVEEIIEETK VEDEKSEMEE TLTAIAEELA
ASAKEEKEEA EEKEEEPEAE KSPVKSPEAK EEEEEGEKEE EEEGQEEEEE EDEGVKSDQA
EEGGSEKEGS SEKDEGEQEE EEGETEAEGE GEEAEAKEEK KIEGKVEEVA VKEEIKVEKP
EKAKSPMPKS PVEEVKPKPE AKAGKGEQKE EEKVEEEKKE VTKESPKEEK VEKKEEKPKD
VADKKKAESP VKEKAVEEVI TISKSVKVSL EKDTKEEKPQ PQEKVKEKAE EEGGSEEEGS
DRSPQESKKE DIAINGEVEG KEEEEQETQE KGSGREEEKG VVTNGLDVSP AEEKKGEDSS
DDKVVVTKKV EKITSEGGDG ATKYITKSVT VTQKVEEHEE TFEEKLVSTK KVEKVTSHAI
VKEVTQGD
//
