NFM_RAT
ID NFM_RAT Reviewed; 846 AA.
AC P12839; Q63370;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
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 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].
RX PubMed=2441012;
RA Napolitano E.W., Chin S.S.M., Colman D.R., Liem R.K.H.;
RT "Complete amino acid sequence and in vitro expression of rat NF-M, the
RT middle molecular weight neurofilament protein.";
RL J. Neurosci. 7:2590-2599(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=1321159; DOI=10.1083/jcb.118.2.397;
RA Kelly B.M., Gillespie C.S., Sherman D.L., Brophy P.J.;
RT "Schwann cells of the myelin-forming phenotype express neurofilament
RT protein NF-M.";
RL J. Cell Biol. 118:397-410(1992).
RN [3]
RP PROTEIN SEQUENCE OF 102-117; 139-154; 168-183; 207-216; 223-258; 352-371;
RP 391-410; 412-427; 452-461 AND 686-693, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION AT SER-503; SER-507; SER-537; SER-604; SER-609 AND SER-667,
RP AND SEQUENCE REVISION TO 500.
RX PubMed=1537832; DOI=10.1016/s0021-9258(18)42856-6;
RA Xu Z.-S., Liu W.-S., Willard M.B.;
RT "Identification of six phosphorylation sites in the COOH-terminal tail
RT region of the rat neurofilament protein M.";
RL J. Biol. Chem. 267:4467-4471(1992).
RN [5]
RP GLYCOSYLATION AT THR-48 AND THR-431.
RX PubMed=8344946; DOI=10.1016/s0021-9258(19)85471-6;
RA Dong D.L.-Y., Xu Z.-S., Chevrier M.R., Cotter R.J., Cleveland D.W.,
RA Hart G.W.;
RT "Glycosylation of mammalian neurofilaments. Localization of multiple O-
RT linked N-acetylglucosamine moieties on neurofilament polypeptides L and
RT M.";
RL J. Biol. Chem. 268:16679-16687(1993).
RN [6]
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 [7]
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-345; SER-417;
RP SER-429; SER-467; SER-483; SER-503; SER-507; SER-537; SER-545; SER-550;
RP SER-551; THR-564; SER-604; SER-609; SER-643; SER-667; SER-713; SER-721;
RP SER-751 AND SER-767, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
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:P08553}.
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:P08553}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P08553}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglion neurons (at
CC protein level). {ECO:0000269|PubMed:9388258}.
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 {ECO:0000269|PubMed:1537832}.
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:1537832}.
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; M18628; AAA41696.1; -; mRNA.
DR EMBL; Z12152; CAA78136.1; -; mRNA.
DR PIR; A45669; A45669.
DR RefSeq; NP_058725.1; NM_017029.2.
DR AlphaFoldDB; P12839; -.
DR SMR; P12839; -.
DR BioGRID; 246731; 6.
DR DIP; DIP-208N; -.
DR IntAct; P12839; 2.
DR MINT; P12839; -.
DR STRING; 10116.ENSRNOP00000065853; -.
DR GlyConnect; 432; 1 O-Linked glycan (2 sites).
DR GlyGen; P12839; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P12839; -.
DR PhosphoSitePlus; P12839; -.
DR World-2DPAGE; 0004:P12839; -.
DR jPOST; P12839; -.
DR PaxDb; P12839; -.
DR PRIDE; P12839; -.
DR GeneID; 24588; -.
DR KEGG; rno:24588; -.
DR UCSC; RGD:3160; rat.
DR CTD; 4741; -.
DR RGD; 3160; Nefm.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P12839; -.
DR OrthoDB; 898483at2759; -.
DR PhylomeDB; P12839; -.
DR PRO; PR:P12839; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:RGD.
DR GO; GO:0097418; C:neurofibrillary tangle; ISO:RGD.
DR GO; GO:0005883; C:neurofilament; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO: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:0099182; C:presynaptic intermediate filament cytoskeleton; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0015643; F:toxic substance binding; IDA:RGD.
DR GO; GO:0008088; P:axo-dendritic transport; ISO:RGD.
DR GO; GO:0031103; P:axon regeneration; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP: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; ISO:RGD.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0045105; P:intermediate filament polymerization or depolymerization; IDA:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0033693; P:neurofilament bundle assembly; IDA:RGD.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; ISO:RGD.
DR GO; GO:0031133; P:regulation of axon diameter; ISO:RGD.
DR GO; GO:1903937; P:response to acrylamide; IEP:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR027697; NF-M.
DR PANTHER; PTHR45652:SF3; PTHR45652:SF3; 2.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
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; 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:0000269|Ref.7"
FT CHAIN 2..846
FT /note="Neurofilament medium polypeptide"
FT /id="PRO_0000063798"
FT DOMAIN 100..411
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..104
FT /note="Head"
FT REGION 104..135
FT /note="Coil 1A"
FT REGION 136..148
FT /note="Linker 1"
FT REGION 149..247
FT /note="Coil 1B"
FT REGION 248..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..845
FT /note="Tail"
FT REGION 483..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..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..572
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 319
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 345
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 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1537832,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1537832,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1537832,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1537832,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1537832,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:1537832,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 48
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:8344946"
FT /id="CAR_000130"
FT CARBOHYD 431
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:8344946"
FT /id="CAR_000131"
FT CONFLICT 18
FT /note="Missing (in Ref. 2; CAA78136)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="R -> P (in Ref. 2; CAA78136)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> L (in Ref. 2; CAA78136)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="Missing (in Ref. 1; AAA41696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 95791 MW; 14DE91A1D1F68EC8 CRC64;
MSYTLDSLGN PSAYRRVPTE TRSSFSRVSG SPSSGFRSQS WSRGSPSTVS SSYKRSALAP
RLAYSSAMLS SAESSLDFSQ SSSLLNGGSG GDYKLSRSNE KEQLQGLNDR FAGYIEKVHY
LEQQNKEIEA EIHALRQKQA SHAQLGDAYD QEIRELRATL EMVNHEKAQV QLDSDHLEED
IHRLKERFEE EARLRDDTEA AIRAVRKDIE ESSMVKVELD KKVQSLQDEV AFLRSNHEEE
VADLLAQIQA SHITVERKDY LKTDISTALK EIRSQLECHS DQNMHQAEEW FKCRYAKLTE
AAEQNKEAIR SAKEEIAEYR RQLQSKSIEL ESVRGTKESL ERQLSDIEER HNHDLSSYQD
TIQQLENELR GTKWEMARHL REYQDLLNVK MALDIEIAAY RKLLEGEETR FSTFSGSITG
PLYTHRQPSV TISSKIQKTK VEAPKLKVQH KFVEEIIEET KVEDEKSEME DALTVIAEEL
AASAKEEKEE AEEKEEEPEV EKSPVKSPEA KEEEEGEKEE EEEGQEEEEE EDEGVKSDQA
EEGGSEKEGS SEKDEGEQEE EGETEAEGEG EEAEAKEEKK TEGKVEEMAI KEEIKVEKPE
KAKSPVPKSP VEEVKPKPEA KAGKDEQKEE EKVEEKKEVA KESPKEEKVE KKEEKPKDVP
DKKKAESPVK EKAVEEMITI TKSVKVSLEK DTKEEKPQQQ EKVKEKAEEE GGSEEEVGDK
SPQESKKEDI AINGEVEGKE EEEQETQEKG SGQEEEKGVV TNGLDVSPAE EKKGEDRSDD
KVVVTKKVEK ITSEGGDGAT KYITKSVTVT QKVEEHEETF EEKLVSTKKV EKVTSHAIVK
EVTQGD
