NFH_MOUSE
ID NFH_MOUSE Reviewed; 1090 AA.
AC P19246; A1E2H9; Q5SVF6; Q61959;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 196.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster; TISSUE=Brain;
RX PubMed=3145094; DOI=10.1016/0169-328x(88)90028-9;
RA Shneidman P.S., Carden M.J., Lees J.F., Lazzarini R.A.;
RT "The structure of the largest murine neurofilament protein (NF-H) as
RT revealed by cDNA and genomic sequences.";
RL Brain Res. 464:217-231(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3220257; DOI=10.1016/0378-1119(88)90033-9;
RA Julien J.-P., Cote F., Beaudet L., Sidky M., Flavell D., Grosveld F.,
RA Mushynski W.;
RT "Sequence and structure of the mouse gene coding for the largest
RT neurofilament subunit.";
RL Gene 68:307-314(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Swiss Webster; TISSUE=Brain;
RA Carden M.J.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP PROTEIN SEQUENCE OF 167-180; 351-370; 382-401 AND 903-917, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 814-961.
RC STRAIN=VM;
RA Huysentruyt L.C., Banerjee D., Seyfried T.N.;
RT "Novel metastatic mouse tumor cells express multiple properties of
RT macrophages.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-529; SER-535;
RP SER-547; SER-559; SER-565; SER-571; SER-577; SER-589; SER-601; SER-607;
RP SER-613; SER-619; SER-625; SER-631; SER-637; SER-655; SER-661; SER-667;
RP SER-673; SER-679; SER-685; SER-697; SER-703; SER-709; SER-715; SER-727;
RP SER-733; SER-739; SER-745; SER-751; SER-757; SER-763; SER-769; SER-783;
RP SER-789; SER-815; SER-834; SER-867 AND SER-888, AND IDENTIFICATION BY MASS
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-122; SER-416;
RP SER-419; SER-535; SER-541; SER-547; SER-553; SER-559; SER-565; SER-571;
RP SER-583; SER-589; SER-595; SER-601; SER-607; SER-619; SER-631; SER-637;
RP SER-643; SER-649; SER-655; SER-661; SER-667; SER-673; SER-679; SER-685;
RP SER-691; SER-697; SER-703; SER-709; SER-727; SER-733; SER-739; SER-745;
RP SER-751; SER-757; SER-763; SER-769; SER-795; SER-834 AND SER-859, AND
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 [9]
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).
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 (PubMed:22723690).
CC {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:P16884}.
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, 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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=AAA39813.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA83229.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M35131; AAA39809.1; -; mRNA.
DR EMBL; M24496; AAA39813.1; ALT_INIT; Genomic_DNA.
DR EMBL; M23349; AAA39813.1; JOINED; Genomic_DNA.
DR EMBL; M24494; AAA39813.1; JOINED; Genomic_DNA.
DR EMBL; M24495; AAA39813.1; JOINED; Genomic_DNA.
DR EMBL; Z31012; CAA83229.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL645522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF101556; ABK96805.1; -; mRNA.
DR CCDS; CCDS36099.1; -.
DR PIR; JT0368; QFMSH.
DR RefSeq; NP_035034.2; NM_010904.3.
DR AlphaFoldDB; P19246; -.
DR SMR; P19246; -.
DR BioGRID; 237594; 16.
DR IntAct; P19246; 5.
DR MINT; P19246; -.
DR STRING; 10090.ENSMUSP00000091061; -.
DR iPTMnet; P19246; -.
DR PhosphoSitePlus; P19246; -.
DR UCD-2DPAGE; P19246; -.
DR EPD; P19246; -.
DR jPOST; P19246; -.
DR MaxQB; P19246; -.
DR PaxDb; P19246; -.
DR PeptideAtlas; P19246; -.
DR PRIDE; P19246; -.
DR ProteomicsDB; 287406; -.
DR Antibodypedia; 3579; 1697 antibodies from 47 providers.
DR DNASU; 380684; -.
DR Ensembl; ENSMUST00000093369; ENSMUSP00000091061; ENSMUSG00000020396.
DR GeneID; 380684; -.
DR KEGG; mmu:380684; -.
DR UCSC; uc007hvm.1; mouse.
DR CTD; 4744; -.
DR MGI; MGI:97309; Nefh.
DR VEuPathDB; HostDB:ENSMUSG00000020396; -.
DR eggNOG; ENOG502QYDU; Eukaryota.
DR GeneTree; ENSGT00940000161893; -.
DR HOGENOM; CLU_012560_7_2_1; -.
DR InParanoid; P19246; -.
DR OMA; IKMVEKS; -.
DR OrthoDB; 898483at2759; -.
DR PhylomeDB; P19246; -.
DR TreeFam; TF330122; -.
DR BioGRID-ORCS; 380684; 3 hits in 71 CRISPR screens.
DR PRO; PR:P19246; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P19246; protein.
DR Bgee; ENSMUSG00000020396; Expressed in ventral horn of spinal cord and 133 other tissues.
DR Genevisible; P19246; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0150017; C:basal proximal dendrite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO: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:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IMP:SynGO.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR GO; GO:0061564; P:axon development; IMP:BHF-UCL.
DR GO; GO:0031103; P:axon regeneration; ISO:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP: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: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:0001552; P:ovarian follicle atresia; ISO:MGI.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:MGI.
DR GO; GO:1903935; P:response to sodium arsenite; ISO:MGI.
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; 17.
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 Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Intermediate filament; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1090
FT /note="Neurofilament heavy polypeptide"
FT /id="PRO_0000063801"
FT DOMAIN 95..411
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REPEAT 522..527
FT /note="1"
FT REPEAT 528..533
FT /note="2"
FT REPEAT 534..539
FT /note="3"
FT REPEAT 540..545
FT /note="4"
FT REPEAT 546..551
FT /note="5"
FT REPEAT 552..557
FT /note="6"
FT REPEAT 558..563
FT /note="7"
FT REPEAT 564..569
FT /note="8"
FT REPEAT 570..575
FT /note="9"
FT REPEAT 576..581
FT /note="10"
FT REPEAT 582..587
FT /note="11"
FT REPEAT 588..593
FT /note="12"
FT REPEAT 594..599
FT /note="13"
FT REPEAT 600..605
FT /note="14"
FT REPEAT 606..611
FT /note="15"
FT REPEAT 612..617
FT /note="16"
FT REPEAT 618..623
FT /note="17"
FT REPEAT 624..629
FT /note="18"
FT REPEAT 630..635
FT /note="19"
FT REPEAT 636..641
FT /note="20"
FT REPEAT 642..647
FT /note="21"
FT REPEAT 648..653
FT /note="22"
FT REPEAT 654..659
FT /note="23"
FT REPEAT 660..665
FT /note="24"
FT REPEAT 666..671
FT /note="25"
FT REPEAT 672..677
FT /note="26"
FT REPEAT 678..683
FT /note="27"
FT REPEAT 684..689
FT /note="28"
FT REPEAT 690..695
FT /note="29"
FT REPEAT 696..701
FT /note="30"
FT REPEAT 702..707
FT /note="31"
FT REPEAT 708..713
FT /note="32"
FT REPEAT 714..719
FT /note="33"
FT REPEAT 720..725
FT /note="34"
FT REPEAT 726..731
FT /note="35"
FT REPEAT 732..737
FT /note="36"
FT REPEAT 738..743
FT /note="37"
FT REPEAT 744..749
FT /note="38"
FT REPEAT 750..755
FT /note="39"
FT REPEAT 756..761
FT /note="40"
FT REPEAT 762..767
FT /note="41"
FT REPEAT 768..773
FT /note="42"
FT REPEAT 774..779
FT /note="43; approximate"
FT REPEAT 782..787
FT /note="44"
FT REPEAT 788..793
FT /note="45"
FT REPEAT 794..799
FT /note="46"
FT REPEAT 808..813
FT /note="47"
FT REPEAT 814..819
FT /note="48"
FT REPEAT 833..838
FT /note="49"
FT REPEAT 858..863
FT /note="50"
FT REPEAT 866..871
FT /note="51"
FT REPEAT 887..892
FT /note="52"
FT REGION 2..98
FT /note="Head"
FT REGION 99..130
FT /note="Coil 1A"
FT REGION 131..143
FT /note="Linker 1"
FT REGION 144..242
FT /note="Coil 1B"
FT REGION 243..264
FT /note="Linker 12"
FT REGION 265..286
FT /note="Coil 2A"
FT REGION 287..290
FT /note="Linker 2"
FT REGION 291..411
FT /note="Coil 2B"
FT REGION 412..1090
FT /note="Tail"
FT REGION 456..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..892
FT /note="52 X 6 AA approximate tandem repeats of K-S-P-
FT [AGISV]-[EATK]-[APVQ]"
FT COMPBIAS 456..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 839
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16884"
FT CONFLICT 134..135
FT /note="QA -> K (in Ref. 2; AAA39813)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Missing (in Ref. 2; AAA39813)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="T -> S (in Ref. 2; AAA39813)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="G -> L (in Ref. 2; AAA39813)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="E -> EEAKSPG (in Ref. 1; AAA39809 and 3; CAA83229)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="G -> R (in Ref. 1; AAA39809 and 3; CAA83229)"
FT /evidence="ECO:0000305"
FT CONFLICT 694..717
FT /note="Missing (in Ref. 1; AAA39809 and 3; CAA83229)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="V -> M (in Ref. 1; AAA39809, 3; CAA83229 and 6;
FT ABK96805)"
FT /evidence="ECO:0000305"
FT CONFLICT 846..847
FT /note="KH -> ND (in Ref. 1; AAA39809, 3; CAA83229 and 6;
FT ABK96805)"
FT /evidence="ECO:0000305"
FT CONFLICT 846..847
FT /note="KH -> TV (in Ref. 2; AAA39813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1090 AA; 116994 MW; B2A7D7D36FF2F448 CRC64;
MMSFGSADAL LGAPFAPLHG GGSLHYSLSR KAGPGGTRSA AGSSSGFHSW ARTSVSSVSA
SPSRFRGAAS STDSLDTLSN GPEGCVVAAV AARSEKEQLQ ALNDRFAGYI DKVRQLEAHN
RSLEGEAAAL RQQQAGRAAM GELYEREVRE MRGAVLRLGA ARGQLRLEQE HLLEDIAHVR
QRLDEEARQR EEAEAAARAL ARFAQEAEAA RVELQKKAQA LQEECGYLRR HHQEEVGELL
GQIQGCGAAQ AQAQAEARDA LKCDVTSALR EIRAQLEGHA VQSTLQSEEW FRVRLDRLSE
AAKVNTDAMR SAQEEITEYR RQLQARTTEL EALKSTKESL ERQRSELEDR HQADIASYQD
AIQQLDSELR NTKWEMAAQL REYQDLLNVK MALDIEIAAY RKLLEGEECR IGFGPSPFSL
TEGLPKIPSI STHIKVKSEE MIKVVEKSEK ETVIVEGQTE EIRVTEGVTE EEDKEAQGQE
GEEAEEGEEK EEEEGAAATS PPAEEAASPE KETKSRVKEE AKSPGEAKSP GEAKSPAEAK
SPGEAKSPGE AKSPGEAKSP AEPKSPAEPK SPAEAKSPAE PKSPATVKSP GEAKSPSEAK
SPAEAKSPAE AKSPAEAKSP AEAKSPAEAK SPAEAKSPAT VKSPGEAKSP SEAKSPAEAK
SPAEAKSPAE AKSPAEVKSP GEAKSPAEPK SPAEAKSPAE VKSPAEAKSP AEVKSPGEAK
SPAAVKSPAE AKSPAAVKSP GEAKSPGEAK SPAEAKSPAE AKSPIEVKSP EKAKTPVKEG
AKSPAEAKSP EKAKSPVKED IKPPAEAKSP EKAKSPVKEG AKPPEKAKPL DVKSPEAQTP
VQEEAKHPTD IRPPEQVKSP AKEKAKSPEK EEAKTSEKVA PKKEEVKSPV KEEVKAKEPP
KKVEEEKTLP TPKTEAKESK KDEAPKEAPK PKVEEKKETP TEKPKDSTAE AKKEEAGEKK
KAVASEEETP AKLGVKEEAK PKEKTETTKT EAEDTKAKEP SKPTETEKPK KEEMPAAPEK
KDTKEEKTTE SRKPEEKPKM EAKVKEDDKS LSKEPSKPKT EKAEKSSSTD QKESQPPEKT
TEDKATKGEK
