NFH_PIG
ID NFH_PIG Reviewed; 142 AA.
AC P12037;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Neurofilament heavy polypeptide;
DE Short=NF-H;
DE AltName: Full=200 kDa neurofilament protein;
DE AltName: Full=Neurofilament triplet H protein;
DE Flags: Fragment;
GN Name=NEFH;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=16453600; DOI=10.1002/j.1460-2075.1985.tb02317.x;
RA Geisler N., Fischer S., Vandekerckhove J., van Damme J., Plessmann U.,
RA Weber K.;
RT "Protein-chemical characterization of NF-H, the largest mammalian
RT neurofilament component; intermediate filament-type sequences followed by a
RT unique carboxy-terminal extension.";
RL EMBO J. 4:57-63(1985).
CC -!- FUNCTION: Neurofilaments usually contain three intermediate filament
CC proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of
CC neuronal caliber. NEFH has an important function in mature axons that
CC is not subserved by the two smaller NF proteins. May additionally
CC cooperate with the neuronal intermediate filament proteins PRPH and INA
CC to form neuronal filamentous networks (By similarity).
CC {ECO:0000250|UniProtKB:P19246}.
CC -!- SUBUNIT: Forms heterodimers with NEFL; which can further hetero-
CC oligomerize (in vitro) (By similarity). Forms heterodimers with INA (in
CC vitro) (By similarity). {ECO:0000250|UniProtKB:P16884}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P19246}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P19246}.
CC -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFH is
CC phosphorylated on a number of the serines in this motif. It is thought
CC that phosphorylation of NFH results in the formation of interfilament
CC cross bridges that are important in the maintenance of axonal caliber.
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.
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}.
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DR PIR; C22702; C22702.
DR AlphaFoldDB; P12037; -.
DR SMR; P12037; -.
DR PeptideAtlas; P12037; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005883; C:neurofilament; IDA:CAFA.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0061564; P:axon development; IBA:GO_Central.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IBA:GO_Central.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR033183; NF-H.
DR PANTHER; PTHR23214; PTHR23214; 1.
DR Pfam; PF00038; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Intermediate filament; Phosphoprotein;
KW Reference proteome.
FT CHAIN <1..>142
FT /note="Neurofilament heavy polypeptide"
FT /id="PRO_0000063802"
FT DOMAIN <1..>142
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT COILED 26..74
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 142
SQ SEQUENCE 142 AA; 16204 MW; F19117D0F2DCFD8E CRC64;
MRGAVLRLGA ARGQLRLEQE HLLEDIAHVR QRLDDEARQR QEAEAAARAL ARFAQEAEAA
RVELQKKAQA LQEECGYLRR HHQEEAQAEA RDALKCDVTS ALREIRAQLE GHAVQSTLQQ
EEWFRVRLDR LSEAAKVNTD AM