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Neurofilament medium polypeptide (NF-M) (160 kDa neurofilament protein) (Neurofilament 3) (Neurofilament triplet M protein)

 NFM_RAT                 Reviewed;         846 AA.
P12839; Q63370;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
10-MAY-2017, entry version 145.
RecName: Full=Neurofilament medium polypeptide;
Short=NF-M;
AltName: Full=160 kDa neurofilament protein;
AltName: Full=Neurofilament 3;
AltName: Full=Neurofilament triplet M protein;
Name=Nefm; Synonyms=Nef3, Nfm;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2441012;
Napolitano E.W., Chin S.S.M., Colman D.R., Liem R.K.H.;
"Complete amino acid sequence and in vitro expression of rat NF-M, the
middle molecular weight neurofilament protein.";
J. Neurosci. 7:2590-2599(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
PubMed=1321159; DOI=10.1083/jcb.118.2.397;
Kelly B.M., Gillespie C.S., Sherman D.L., Brophy P.J.;
"Schwann cells of the myelin-forming phenotype express neurofilament
protein NF-M.";
J. Cell Biol. 118:397-410(1992).
[3]
PROTEIN SEQUENCE OF 102-117; 139-154; 168-183; 207-216; 223-258;
352-371; 391-410; 412-427; 452-461 AND 686-693, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[4]
PHOSPHORYLATION AT SER-503; SER-507; SER-537; SER-604; SER-609 AND
SER-667, AND SEQUENCE REVISION TO 500.
PubMed=1537832;
Xu Z.-S., Liu W.-S., Willard M.B.;
"Identification of six phosphorylation sites in the COOH-terminal tail
region of the rat neurofilament protein M.";
J. Biol. Chem. 267:4467-4471(1992).
[5]
GLYCOSYLATION AT THR-48 AND THR-431.
PubMed=8344946;
Dong D.L.-Y., Xu Z.-S., Chevrier M.R., Cotter R.J., Cleveland D.W.,
Hart G.W.;
"Glycosylation of mammalian neurofilaments. Localization of multiple
O-linked N-acetylglucosamine moieties on neurofilament polypeptides L
and M.";
J. Biol. Chem. 268:16679-16687(1993).
[6]
ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (FEB-2007) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-345; SER-417;
SER-429; SER-467; SER-483; SER-503; SER-507; SER-537; SER-545;
SER-550; SER-551; THR-564; SER-604; SER-609; SER-643; SER-667;
SER-713; SER-721; SER-751 AND SER-767, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Neurofilaments usually contain three intermediate
filament proteins: L, M, and H which are involved in the
maintenance of neuronal caliber.
-!- PTM: There are a number of repeats of the tripeptide K-S-P, NFM is
phosphorylated on a number of the serines in this motif. It is
thought that phosphorylation of NFM results in the formation of
interfilament cross bridges that are important in the maintenance
of axonal caliber. {ECO:0000269|PubMed:1537832}.
-!- PTM: Phosphorylation seems to play a major role in the functioning
of the larger neurofilament polypeptides (NF-M and NF-H), the
levels of phosphorylation being altered developmentally and
coincidentally with a change in the neurofilament function.
{ECO:0000269|PubMed:1537832}.
-!- PTM: Phosphorylated in the head and rod regions by the PKC kinase
PKN1, leading to the inhibition of polymerization. {ECO:0000250}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M18628; AAA41696.1; -; mRNA.
EMBL; Z12152; CAA78136.1; -; mRNA.
PIR; A45669; A45669.
RefSeq; NP_058725.1; NM_017029.2.
UniGene; Rn.10971; -.
ProteinModelPortal; P12839; -.
SMR; P12839; -.
BioGrid; 246731; 3.
DIP; DIP-208N; -.
STRING; 10116.ENSRNOP00000065853; -.
iPTMnet; P12839; -.
PhosphoSitePlus; P12839; -.
UniCarbKB; P12839; -.
World-2DPAGE; 0004:P12839; -.
PaxDb; P12839; -.
PRIDE; P12839; -.
GeneID; 24588; -.
KEGG; rno:24588; -.
UCSC; RGD:3160; rat.
CTD; 4741; -.
RGD; 3160; Nefm.
eggNOG; ENOG410IGME; Eukaryota.
eggNOG; ENOG410XPTM; LUCA.
HOGENOM; HOG000230977; -.
HOVERGEN; HBG013015; -.
InParanoid; P12839; -.
KO; K04573; -.
PhylomeDB; P12839; -.
PRO; PR:P12839; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:RGD.
GO; GO:0005883; C:neurofilament; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0015643; F:toxic substance binding; IDA:RGD.
GO; GO:0031103; P:axon regeneration; IEP:RGD.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0045105; P:intermediate filament polymerization or depolymerization; IDA:RGD.
GO; GO:0033693; P:neurofilament bundle assembly; IDA:RGD.
GO; GO:1903937; P:response to acrylamide; IEP:RGD.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
InterPro; IPR001664; IF.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR002957; Keratin_I.
InterPro; IPR027697; NF-M.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF257; PTHR23239:SF257; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome;
Direct protein sequencing; Glycoprotein; Intermediate filament;
Methylation; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 846 Neurofilament medium polypeptide.
/FTId=PRO_0000063798.
REGION 2 104 Head.
REGION 104 411 Rod.
REGION 104 135 Coil 1A.
REGION 136 148 Linker 1.
REGION 149 247 Coil 1B.
REGION 248 264 Linker 12.
REGION 265 286 Coil 2A.
REGION 287 290 Linker 2.
REGION 291 411 Coil 2B.
REGION 412 845 Tail.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.6}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 43 43 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P08553}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000250|UniProtKB:P08553}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:P08553}.
MOD_RES 319 319 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08553}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1537832}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1537832}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1537832}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 564 564 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1537832}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1537832}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:1537832}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000250|UniProtKB:O77788}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 721 721 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 751 751 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 48 48 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:8344946}.
/FTId=CAR_000130.
CARBOHYD 431 431 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:8344946}.
/FTId=CAR_000131.
CONFLICT 18 18 Missing (in Ref. 2; CAA78136).
{ECO:0000305}.
CONFLICT 22 22 R -> P (in Ref. 2; CAA78136).
{ECO:0000305}.
CONFLICT 205 205 V -> L (in Ref. 2; CAA78136).
{ECO:0000305}.
CONFLICT 501 501 Missing (in Ref. 1; AAA41696).
{ECO:0000305}.
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


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