NFH_RAT
ID NFH_RAT Reviewed; 1072 AA.
AC P16884; O35482; Q540Z7; Q63368;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 4.
DT 25-MAY-2022, entry version 165.
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=Nfh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3143606; DOI=10.1016/0014-5793(88)81064-0;
RA Breen K.C., Robinson P.A., Wion D., Anderton B.H.;
RT "Partial sequence of the rat heavy neurofilament polypeptide (NF-H).
RT Identification of putative phosphorylation sites.";
RL FEBS Lett. 241:213-218(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2230956; DOI=10.1523/jneurosci.10-11-03714.1990;
RA Chin S.S., Liem R.K.;
RT "Transfected rat high-molecular-weight neurofilament (NF-H) coassembles
RT with vimentin in a predominantly nonphosphorylated form.";
RL J. Neurosci. 10:3714-3726(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 230-318 AND 472-554.
RX PubMed=2878828; DOI=10.1016/0014-5793(86)81111-5;
RA Robinson P.A., Wion D., Anderton B.H.;
RT "Isolation of a cDNA for the rat heavy neurofilament polypeptide (NF-H).";
RL FEBS Lett. 209:203-205(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 266-1072.
RX PubMed=2457365; DOI=10.1016/0006-291x(88)90254-9;
RA Dautigny A., Pham-Dinh D., Roussel C., Felix J.M., Nussbaum J.-L.,
RA Jolles P.;
RT "The large neurofilament subunit (NF-H) of the rat: cDNA cloning and in
RT situ detection.";
RL Biochem. Biophys. Res. Commun. 154:1099-1106(1988).
RN [5]
RP PROTEIN SEQUENCE OF 39-52; 165-178; 229-256; 272-290; 349-368; 389-399 AND
RP 401-424, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Pradeep J.J.P., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 559-1072.
RX PubMed=2928342; DOI=10.1073/pnas.86.7.2463;
RA Lieberburg I., Spinner N., Snyder S., Anderson J., Goldgaber D.,
RA Smulowitz M., Carroll Z., Emanuel B.S., Breitner J., Rubin L.;
RT "Cloning of a cDNA encoding the rat high molecular weight neurofilament
RT peptide (NF-H): developmental and tissue expression in the rat, and mapping
RT of its human homologue to chromosomes 1 and 22.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2463-2467(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 559-1072.
RC TISSUE=Brain;
RA Alliel P.M., Langlois C.;
RT "Rat heavy neurofilament (NF-H) polypeptide.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH NEFL AND INA, AND TISSUE SPECIFICITY.
RX PubMed=9388258; DOI=10.1074/jbc.272.49.31073;
RA Athlan E.S., Mushynski W.E.;
RT "Heterodimeric associations between neuronal intermediate filament
RT proteins.";
RL J. Biol. Chem. 272:31073-31078(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-414; SER-417;
RP SER-501; SER-516; SER-522; SER-528; SER-534; SER-540; SER-546; SER-552;
RP SER-558; SER-564; SER-570; SER-576; SER-582; SER-588; SER-594; SER-600;
RP SER-606; SER-618; SER-624; SER-627; SER-630; SER-636; SER-642; SER-648;
RP SER-654; SER-660; SER-666; SER-672; SER-684; SER-687; SER-690; SER-696;
RP SER-702; SER-708; SER-714; SER-720; SER-732; SER-738; SER-744; SER-750;
RP SER-756; SER-762; SER-782; SER-802; SER-808; SER-816; SER-827; THR-832;
RP SER-846; SER-852; SER-860; SER-880 AND SER-937, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19913522; DOI=10.1016/j.brainres.2009.11.011;
RA Reid A.J., Welin D., Wiberg M., Terenghi G., Novikov L.N.;
RT "Peripherin and ATF3 genes are differentially regulated in regenerating and
RT non-regenerating primary sensory neurons.";
RL Brain Res. 1310:1-7(2010).
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 NEF 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) (PubMed:9388258). Forms heterodimers with INA
CC (in vitro) (PubMed:9388258). {ECO:0000269|PubMed:9388258}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P19246}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P19246}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglion neurons (at
CC protein level) (PubMed:9388258). Expressed in cutaneous and muscular
CC sensory neurons (PubMed:19913522). {ECO:0000269|PubMed:19913522,
CC ECO:0000269|PubMed:9388258}.
CC -!- INDUCTION: Down-regulated after nerve injury.
CC {ECO:0000269|PubMed:19913522}.
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 -!- POLYMORPHISM: The number of repeats in the tandem repeat domain is
CC shown to vary between 53 and 55.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA32038.1; Type=Frameshift; Evidence={ECO:0000305};
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; M37227; AAA41693.1; ALT_FRAME; mRNA.
DR EMBL; X13804; CAA32038.1; ALT_FRAME; mRNA.
DR EMBL; AF031879; AAB87068.1; -; mRNA.
DR EMBL; M21964; AAA41695.1; -; mRNA.
DR EMBL; J04517; AAA41692.1; -; mRNA.
DR EMBL; AY112897; AAM49796.1; -; mRNA.
DR PIR; A37221; A37221.
DR PIR; S02003; S02003.
DR AlphaFoldDB; P16884; -.
DR SMR; P16884; -.
DR DIP; DIP-105N; -.
DR IntAct; P16884; 5.
DR MINT; P16884; -.
DR STRING; 10116.ENSRNOP00000011604; -.
DR iPTMnet; P16884; -.
DR PhosphoSitePlus; P16884; -.
DR jPOST; P16884; -.
DR PaxDb; P16884; -.
DR PRIDE; P16884; -.
DR UCSC; RGD:3159; rat.
DR RGD; 3159; Nefh.
DR eggNOG; ENOG502QYDU; Eukaryota.
DR InParanoid; P16884; -.
DR PhylomeDB; P16884; -.
DR PRO; PR:P16884; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0150017; C:basal proximal dendrite; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
DR GO; GO:0097418; C:neurofibrillary tangle; ISO:RGD.
DR GO; GO:0005883; C:neurofilament; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; ISO:RGD.
DR GO; GO:0015643; F:toxic substance binding; IDA:RGD.
DR GO; GO:0061564; P:axon development; ISO:RGD.
DR GO; GO:0031103; P:axon regeneration; IDA:RGD.
DR GO; GO:0007420; P:brain development; IDA:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IEP:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IGI:BHF-UCL.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0033693; P:neurofilament bundle assembly; ISO:RGD.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IEP:RGD.
DR GO; GO:0001552; P:ovarian follicle atresia; IDA:RGD.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; ISO:RGD.
DR GO; GO:1903937; P:response to acrylamide; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:1903935; P:response to sodium arsenite; IDA:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
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..1072
FT /note="Neurofilament heavy polypeptide"
FT /id="PRO_0000063803"
FT DOMAIN 94..409
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REPEAT 507..512
FT /note="1"
FT REPEAT 515..520
FT /note="2"
FT REPEAT 521..526
FT /note="3"
FT REPEAT 527..532
FT /note="4"
FT REPEAT 533..538
FT /note="5"
FT REPEAT 539..544
FT /note="6"
FT REPEAT 545..550
FT /note="7"
FT REPEAT 551..556
FT /note="8"
FT REPEAT 557..562
FT /note="9"
FT REPEAT 563..568
FT /note="10"
FT REPEAT 569..574
FT /note="11"
FT REPEAT 575..580
FT /note="12"
FT REPEAT 581..586
FT /note="13"
FT REPEAT 587..592
FT /note="14"
FT REPEAT 593..598
FT /note="15"
FT REPEAT 599..604
FT /note="16"
FT REPEAT 605..610
FT /note="17"
FT REPEAT 611..616
FT /note="18"
FT REPEAT 617..622
FT /note="19"
FT REPEAT 623..628
FT /note="20"
FT REPEAT 629..634
FT /note="21"
FT REPEAT 635..640
FT /note="22"
FT REPEAT 641..646
FT /note="23"
FT REPEAT 647..652
FT /note="24"
FT REPEAT 653..658
FT /note="25"
FT REPEAT 659..664
FT /note="26"
FT REPEAT 665..670
FT /note="27"
FT REPEAT 671..676
FT /note="28"
FT REPEAT 677..682
FT /note="29"
FT REPEAT 683..688
FT /note="30"
FT REPEAT 689..694
FT /note="31"
FT REPEAT 695..700
FT /note="32"
FT REPEAT 701..706
FT /note="33"
FT REPEAT 707..712
FT /note="34"
FT REPEAT 713..718
FT /note="35"
FT REPEAT 719..724
FT /note="36"
FT REPEAT 725..730
FT /note="37; approximate"
FT REPEAT 731..736
FT /note="38"
FT REPEAT 737..742
FT /note="39"
FT REPEAT 743..748
FT /note="40"
FT REPEAT 749..754
FT /note="41"
FT REPEAT 755..760
FT /note="42"
FT REPEAT 761..766
FT /note="43"
FT REPEAT 767..772
FT /note="44"
FT REPEAT 775..780
FT /note="45; approximate"
FT REPEAT 781..786
FT /note="46"
FT REPEAT 787..792
FT /note="47"
FT REPEAT 795..800
FT /note="48; approximate"
FT REPEAT 801..806
FT /note="49"
FT REPEAT 807..812
FT /note="50"
FT REPEAT 815..820
FT /note="51"
FT REPEAT 826..831
FT /note="52"
FT REPEAT 851..856
FT /note="53"
FT REPEAT 859..864
FT /note="54"
FT REPEAT 879..884
FT /note="55"
FT REGION 278..643
FT /note="55 X 6 AA approximate tandem repeats of K-S-P-
FT [VAGSE]-[KEVTSGA]-[EAVK]"
FT REGION 454..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..132
FT /evidence="ECO:0000255"
FT COILED 174..222
FT /evidence="ECO:0000255"
FT COILED 293..380
FT /evidence="ECO:0000255"
FT COMPBIAS 458..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19246"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 832
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 393
FT /note="I -> L (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="S -> I (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="L -> T (in Ref. 4; AAA41695)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="M -> T (in Ref. 4; AAA41695)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="E -> V (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="E -> T (in Ref. 2; AAB87068)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="K -> N (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="V -> A (in Ref. 4 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="E -> G (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="P -> S (in Ref. 4 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 811..812
FT /note="KE -> RK (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="T -> P (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 968
FT /note="A -> V (in Ref. 6; AAA41692)"
FT /evidence="ECO:0000305"
FT CONFLICT 998..1000
FT /note="AAP -> GST (in Ref. 6; AAA41692)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="T -> L (in Ref. 4 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="P -> R (in Ref. 1; AAA41693/CAA32038)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="E -> Q (in Ref. 2; AAB87068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1072 AA; 115378 MW; 89BDFD7E2164D78B CRC64;
MMSFGSADAL LGAPFAPLHG GGSLHYALSR KAGAGGTRSA AGSSSGFHSW ARTSVSSVSA
SPSRFRGAAS STDSLDTLSN GPEGCVAAVA ARSEKEQLQA LNDRFAGYID KVRQLEAHNR
TLEGEAAALR QQKGRAAMGE LYEREVREMR GAVLRLGAAR GHVRLEQEHL LEDIAHVRQR
LDEEARQREE AEAAARALAR FAQEAEAARV ELQKKAQALQ EECGYLRRHH QEEVGELLGQ
IQGCGAAQAQ AQAEARDALK CDVTSALREI RAQLEGHTVQ STLQSEEWFR VRLDRLSEAA
KVNTDAMRSA QEEITEYRRQ LQARTTELEA LKSTKESLER QRSELEDRHQ VDMASYQDAI
QQLDNELRNT KWEMAAQLRE YQDLLNVKMA LDIEIAAYRK LLEGEECRIG FGPSPFSLTE
GLPKIPSMST HIKVKSEEKI KVVEKSEKET VIVEEQTEEI QVTEEVTEEE DKEAQGEEEE
EAEEGGEEAA TTSPPAEEAA SPEKETKSPV KEEAKSPAEA KSPAEAKSPA EAKSPAEVKS
PAEVKSPAEA KSPAEAKSPA EVKSPAEVKS PAEAKSPAEA KSPAEVKSPA TVKSPGEAKS
PAEAKSPAEV KSPVEAKSPA EAKSPASVKS PGEAKSPAEA KSPAEVKSPA TVKSPVEAKS
PAEVKSPVTV KSPAEAKSPV EVKSPASVKS PSEAKSPAGA KSPAEAKSPV VAKSPAEAKS
PAEAKPPAEA KSPAEAKSPA EAKSPAEAKS PAEAKSPVEV KSPEKAKSPV KEGAKSLAEA
KSPEKAKSPV KEEIKPPAEV KSPEKAKSPM KEEAKSPEKA KTLDVKSPEA KTPAKEEAKR
PADIRSPEQV KSPAKEEAKS PEKEETRTEK VAPKKEEVKS PVEEVKAKEP PKKVEEEKTP
ATPKTEVKES KKDEAPKEAQ KPKAEEKEPL TEKPKDSPGE AKKEEAKEKK AAAPEEETPA
KLGVKEEAKP KEKAEDAKAK EPSKPSEKEK PKKEEVPAAP EKKDTKEEKT TESKKPEEKP
KMEAKAKEED KGLPQEPSKP KTEKAEKSSS TDQKDSQPSE KAPEDKAAKG DK
