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Protein

Neurofilament heavy polypeptide

Gene

NEFH

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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. NF-H has an important function in mature axons that is not subserved by the two smaller NF proteins.

GO - Molecular functioni

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
Neurofilament heavy polypeptide
Short name:
NF-H
Alternative name(s):
200 kDa neurofilament protein
Neurofilament triplet H protein
Gene namesi
Name:NEFH
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000063802‹1 – ›142Neurofilament heavy polypeptideAdd BLAST›142

Post-translational modificationi

There are a number of repeats of the tripeptide K-S-P, NFH is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFH results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.
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.
Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PeptideAtlasiP12037
PRIDEiP12037

Structurei

3D structure databases

SMRiP12037
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini‹1 – ›142IF rodPROSITE-ProRule annotationAdd BLAST›142

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili26 – 74Sequence analysisAdd BLAST49

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000230977

Family and domain databases

InterProiView protein in InterPro
IPR039008 IF_rod_dom
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PROSITEiView protein in PROSITE
PS51842 IF_ROD_2, 1 hit

Sequencei

Sequence statusi: Fragment.

P12037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGAVLRLGA ARGQLRLEQE HLLEDIAHVR QRLDDEARQR QEAEAAARAL
60 70 80 90 100
ARFAQEAEAA RVELQKKAQA LQEECGYLRR HHQEEAQAEA RDALKCDVTS
110 120 130 140
ALREIRAQLE GHAVQSTLQQ EEWFRVRLDR LSEAAKVNTD AM
Length:142
Mass (Da):16,204
Last modified:October 1, 1989 - v1
Checksum:iF19117D0F2DCFD8E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei1421

Sequence databases

PIRiC22702

Similar proteinsi

Entry informationi

Entry nameiNFH_PIG
AccessioniPrimary (citable) accession number: P12037
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: May 23, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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