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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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000637932 – 926Neurofilament medium polypeptideAdd BLAST925

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei30PhosphoserineBy similarity1
Modified residuei42Omega-N-methylarginineBy similarity1
Glycosylationi47O-linked (GlcNAc)By similarity1
Modified residuei99PhosphoserineBy similarity1
Modified residuei226PhosphoserineBy similarity1
Modified residuei320PhosphotyrosineBy similarity1
Modified residuei346PhosphoserineBy similarity1
Modified residuei418PhosphoserineBy similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei468PhosphoserineBy similarity1
Modified residuei484PhosphoserineBy similarity1
Modified residuei513Phosphoserine1 Publication1
Modified residuei547Phosphoserine1 Publication1
Modified residuei555Phosphoserine1 Publication1
Modified residuei560PhosphoserineBy similarity1
Modified residuei561Phosphoserine1 Publication1
Modified residuei574PhosphothreonineBy similarity1
Modified residuei628Phosphothreonine1 Publication1
Modified residuei630Phosphoserine1 Publication1
Modified residuei635Phosphoserine1 Publication1
Modified residuei640Phosphoserine1 Publication1
Modified residuei647Phosphothreonine1 Publication1
Modified residuei650Phosphoserine1 Publication1
Modified residuei655Phosphoserine1 Publication1
Modified residuei665Phosphoserine1 Publication1
Modified residuei670Phosphoserine1 Publication1
Modified residuei677Phosphothreonine1 Publication1
Modified residuei680Phosphoserine1 Publication1
Modified residuei685Phosphoserine1 Publication1
Modified residuei690PhosphoserineBy similarity1
Modified residuei695Phosphoserine1 Publication1
Modified residuei727Phosphoserine1 Publication1
Modified residuei751Phosphoserine1 Publication1
Modified residuei757Phosphoserine1 Publication1
Modified residuei771Phosphoserine1 Publication1
Modified residuei831PhosphoserineBy similarity1
Modified residuei847Phosphoserine1 Publication1

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, Methylation, Phosphoprotein

Proteomic databases

PaxDbiO77788.
PeptideAtlasiO77788.
PRIDEiO77788.

PTM databases

iPTMnetiO77788.

Interactioni

Protein-protein interaction databases

IntActiO77788. 1 interactor.
STRINGi9913.ENSBTAP00000036438.

Structurei

3D structure databases

ProteinModelPortaliO77788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati512 – 51615
Repeati619 – 62325
Repeati624 – 62835
Repeati629 – 63345
Repeati634 – 63855
Repeati639 – 64365
Repeati644 – 64875
Repeati649 – 65385
Repeati654 – 65895
Repeati659 – 663105
Repeati664 – 668115
Repeati669 – 673125
Repeati674 – 678135
Repeati679 – 683145
Repeati684 – 688155
Repeati689 – 693165
Repeati694 – 698175

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 104HeadAdd BLAST103
Regioni105 – 412RodAdd BLAST308
Regioni105 – 136Coil 1AAdd BLAST32
Regioni137 – 149Linker 1Add BLAST13
Regioni150 – 248Coil 1BAdd BLAST99
Regioni249 – 265Linker 12Add BLAST17
Regioni266 – 287Coil 2AAdd BLAST22
Regioni288 – 291Linker 24
Regioni292 – 412Coil 2BAdd BLAST121
Regioni413 – 926TailAdd BLAST514
Regioni512 – 69817 X 5 AA approximate tandem repeats of K-S-P-[TVEA]-[AKETP]Add BLAST187

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO77788. 1 interactor.
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...

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: November 2, 2016
This is version 113 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.