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Protein

Neurofilament medium polypeptide

Gene

NEFM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neurofilaments usually contain three intermediate filament proteins: L, M, and H which are involved in the maintenance of neuronal caliber.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofilament medium polypeptide
Short name:
NF-M
Alternative name(s):
160 kDa neurofilament protein
Neurofilament 3
Neurofilament triplet M protein
Gene namesi
Name:NEFM
Synonyms:NEF3, NFM
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 926925Neurofilament medium polypeptidePRO_0000063793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei30 – 301PhosphoserineBy similarity
Glycosylationi47 – 471O-linked (GlcNAc)By similarity
Modified residuei99 – 991PhosphoserineBy similarity
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei320 – 3201PhosphotyrosineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei418 – 4181PhosphoserineBy similarity
Modified residuei430 – 4301PhosphoserineBy similarity
Modified residuei468 – 4681PhosphoserineBy similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei513 – 5131Phosphoserine1 Publication
Modified residuei547 – 5471Phosphoserine1 Publication
Modified residuei555 – 5551Phosphoserine1 Publication
Modified residuei560 – 5601PhosphoserineBy similarity
Modified residuei561 – 5611Phosphoserine1 Publication
Modified residuei574 – 5741PhosphothreonineBy similarity
Modified residuei628 – 6281Phosphothreonine1 Publication
Modified residuei630 – 6301Phosphoserine1 Publication
Modified residuei635 – 6351Phosphoserine1 Publication
Modified residuei640 – 6401Phosphoserine1 Publication
Modified residuei647 – 6471Phosphothreonine1 Publication
Modified residuei650 – 6501Phosphoserine1 Publication
Modified residuei655 – 6551Phosphoserine1 Publication
Modified residuei665 – 6651Phosphoserine1 Publication
Modified residuei670 – 6701Phosphoserine1 Publication
Modified residuei677 – 6771Phosphothreonine1 Publication
Modified residuei680 – 6801Phosphoserine1 Publication
Modified residuei685 – 6851Phosphoserine1 Publication
Modified residuei690 – 6901PhosphoserineBy similarity
Modified residuei695 – 6951Phosphoserine1 Publication
Modified residuei727 – 7271Phosphoserine1 Publication
Modified residuei751 – 7511Phosphoserine1 Publication
Modified residuei757 – 7571Phosphoserine1 Publication
Modified residuei771 – 7711Phosphoserine1 Publication
Modified residuei831 – 8311PhosphoserineBy similarity
Modified residuei847 – 8471Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on a number of serine residues in the repeated K-S-P tripeptide motif. Phosphorylation of NFH may result in the formation of interfilament cross-links that are important in the maintenance of axonal caliber (By similarity).By similarity
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.By similarity
Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO77788.
PeptideAtlasiO77788.
PRIDEiO77788.

PTM databases

iPTMnetiO77788.

Interactioni

Protein-protein interaction databases

IntActiO77788. 1 interaction.
STRINGi9913.ENSBTAP00000036438.

Structurei

3D structure databases

ProteinModelPortaliO77788.
SMRiO77788. Positions 99-136, 330-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati512 – 51651
Repeati619 – 62352
Repeati624 – 62853
Repeati629 – 63354
Repeati634 – 63855
Repeati639 – 64356
Repeati644 – 64857
Repeati649 – 65358
Repeati654 – 65859
Repeati659 – 663510
Repeati664 – 668511
Repeati669 – 673512
Repeati674 – 678513
Repeati679 – 683514
Repeati684 – 688515
Repeati689 – 693516
Repeati694 – 698517

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 104103HeadAdd
BLAST
Regioni105 – 412308RodAdd
BLAST
Regioni105 – 13632Coil 1AAdd
BLAST
Regioni137 – 14913Linker 1Add
BLAST
Regioni150 – 24899Coil 1BAdd
BLAST
Regioni249 – 26517Linker 12Add
BLAST
Regioni266 – 28722Coil 2AAdd
BLAST
Regioni288 – 2914Linker 2
Regioni292 – 412121Coil 2BAdd
BLAST
Regioni413 – 926514TailAdd
BLAST
Regioni512 – 69818717 X 5 AA approximate tandem repeats of K-S-P-[TVEA]-[AKETP]Add
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiO77788.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR027697. NF-M.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 3 hits.
PTHR23239:SF19. PTHR23239:SF19. 3 hits.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O77788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYTLDSLGN PSAYRRVTET RSSFSRISGS PSSGFRSQSW SRGSPSTVSS
60 70 80 90 100
SYKRSALAPR LTYSSAMLSS AESSLDFSQS SSLLDGGSGP GGDYKLSRSN
110 120 130 140 150
EKEQIQGLND RFAGYIEKVH YLEQQNKEIE AEIQALRQKQ ASHAQLGDAY
160 170 180 190 200
DQEIRELRAT LEMVNHEKAQ VQLDSDHLEE DIHRLKERFE EEARLRDDTE
210 220 230 240 250
AAIRALRKDI EESSLVKVEL DKKVQSLQDE VAFLRSNHEE EVADLLAQIQ
260 270 280 290 300
ASHITVERKD YLKTDISTAL KEIRSQLESH SDQNMHQAEE WFKCRYAKLT
310 320 330 340 350
EAAEQNKEAI RSAKEEIAEY RRQLQSKSIE LESVRGTKES LERQLSDIEE
360 370 380 390 400
RHNHDLSSYQ DTIQQLENEL RGTKWEMARH LREYQDLLNV KMALDIEIAA
410 420 430 440 450
YRKLLEGEET RFSTFAGSIT GPLYTHRQPS IAISSKIQKT KVEAPKLKVQ
460 470 480 490 500
HKFVEEIIEE TKVEDEKSEM EEALTAITEE LAVSVKEEVK EEEAEEKEEK
510 520 530 540 550
EEAEEEVVAA KKSPVKATAP ELKEEEGEKE EEEGQEEEEE EEEAAKSDQA
560 570 580 590 600
EEGGSEKEGS SEKEEGEQEE EGETEAEGEG EEAAAEAKEE KKMEEKAEEV
610 620 630 640 650
APKEELAAEA KVEKPEKAKS PVAKSPTTKS PTAKSPEAKS PEAKSPTAKS
660 670 680 690 700
PTAKSPVAKS PTAKSPEAKS PEAKSPTAKS PTAKSPAAKS PAPKSPVEEV
710 720 730 740 750
KPKAEAGAEK GEQKEKVEEE KKEAKESPKE EKAEKKEEKP KDVPEKKKAE
760 770 780 790 800
SPVKAESPVK EEVPAKPVKV SPEKEAKEEE KPQEKEKEKE KVEEVGGKEE
810 820 830 840 850
GGLKESRKED IAINGEVEGK EEEQETKEKG SGGEEEKGVV TNGLDVSPGD
860 870 880 890 900
EKKGGDKSEE KVVVTKMVEK ITSEGGDGAT KYITKSVTVT QKVEEHEETF
910 920
EEKLVSTKKV EKVTSHAIVK EVTQSD
Length:926
Mass (Da):103,210
Last modified:April 3, 2007 - v3
Checksum:iB1C2FA96E31793C0
GO

Mass spectrometryi

Molecular mass is 105044 Da from positions 2 - 926. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091342 mRNA. Translation: AAC36357.1.
UniGeneiBt.51690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091342 mRNA. Translation: AAC36357.1.
UniGeneiBt.51690.

3D structure databases

ProteinModelPortaliO77788.
SMRiO77788. Positions 99-136, 330-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO77788. 1 interaction.
STRINGi9913.ENSBTAP00000036438.

PTM databases

iPTMnetiO77788.

Proteomic databases

PaxDbiO77788.
PeptideAtlasiO77788.
PRIDEiO77788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IGME. Eukaryota.
ENOG410XPTM. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiO77788.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR027697. NF-M.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 3 hits.
PTHR23239:SF19. PTHR23239:SF19. 3 hits.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of endogenous phosphorylation sites of bovine medium and low molecular weight neurofilament proteins by tandem mass spectrometry."
    Trimpin S., Mixon A.E., Stapels M.D., Kim M.Y., Spencer P.S., Deinzer M.L.
    Biochemistry 43:2091-2105(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-116, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-513; SER-547; SER-555; SER-561; THR-628; SER-630; SER-635; SER-640; THR-647; SER-650; SER-655; SER-665; SER-670; THR-677; SER-680; SER-685; SER-695; SER-727; SER-751; SER-757; SER-771 AND SER-847, MASS SPECTROMETRY.
  2. "The bovine neurofilament M subunit has a novel set of KSP repeats normally restricted to NF-H."
    Hill W.D., Zhang L., Balin B.J., Sprinkle T.J., Spicer K., Gearhart D.A.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 117-926.

Entry informationi

Entry nameiNFM_BOVIN
AccessioniPrimary (citable) accession number: O77788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 3, 2007
Last modified: July 6, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.