NFM_PIG
ID NFM_PIG Reviewed; 455 AA.
AC P08552;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Neurofilament medium polypeptide;
DE Short=NF-M;
DE AltName: Full=160 kDa neurofilament protein;
DE AltName: Full=Neurofilament 3;
DE AltName: Full=Neurofilament triplet M protein;
DE Flags: Fragment;
GN Name=NEFM; Synonyms=NEF3;
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 OF 2-455.
RC TISSUE=Spinal cord;
RX PubMed=6439558; DOI=10.1002/j.1460-2075.1984.tb02196.x;
RA Geisler N., Fischer S., Vandekerckhove J., Plessmann U., Weber K.;
RT "Hybrid character of a large neurofilament protein (NF-M): intermediate
RT filament type sequence followed by a long and acidic carboxy-terminal
RT extension.";
RL EMBO J. 3:2701-2706(1984).
CC -!- FUNCTION: Neurofilaments usually contain three intermediate filament
CC proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of
CC neuronal caliber. May additionally cooperate with the neuronal
CC intermediate filament proteins PRPH and INA to form neuronal
CC filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08553}.
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:P12839}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P08553}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P08553}.
CC -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFM is
CC phosphorylated on a number of the serines in this motif. It is thought
CC that phosphorylation of NFM 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; A05075; QFPGM.
DR AlphaFoldDB; P08552; -.
DR SMR; P08552; -.
DR STRING; 9823.ENSSSCP00000010300; -.
DR PeptideAtlas; P08552; -.
DR PRIDE; P08552; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P08552; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0005883; C:neurofilament; IEA:InterPro.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0033693; P:neurofilament bundle assembly; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR027697; NF-M.
DR PANTHER; PTHR45652:SF3; PTHR45652:SF3; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycoprotein; Intermediate filament;
KW Methylation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O77788,
FT ECO:0000269|PubMed:6439558"
FT CHAIN 2..>455
FT /note="Neurofilament medium polypeptide"
FT /id="PRO_0000063796"
FT DOMAIN 102..413
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..105
FT /note="Head"
FT REGION 80..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..137
FT /note="Coil 1A"
FT REGION 138..150
FT /note="Linker 1"
FT REGION 151..249
FT /note="Coil 1B"
FT REGION 250..266
FT /note="Linker 12"
FT REGION 267..288
FT /note="Coil 2A"
FT REGION 289..292
FT /note="Linker 2"
FT REGION 293..412
FT /note="Coil 2B"
FT REGION 414..>455
FT /note="Tail"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 321
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT CARBOHYD 48
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 433
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT NON_TER 455
SQ SEQUENCE 455 AA; 51985 MW; 55D5DF5556013723 CRC64;
MSYTLDSLGN PSSAYRRVTE TRSSFSRVSG SPSSGFRSQS WSRGSPSTVS SSYKRSALAP
RLTYSSAMLS SAESSLDFSQ SSSLLDGGSG PGGDYKLSRS NEKEQIQGLN DRFAGYIEKV
HYLEQQNKEI EAEIQALRQK QASHAQLGDA YDQEIRELRA TLELVNHEKA QVQLDSDHLE
EDIHRLKERF EEEARLRDDT EAAIRALRKD IEEASLVKVE LDKKVQSLQD EVAFLRSNHE
EEVADLLAQI QASHITVERK DYLKTDISSA LKEIRSQLEC HSDQNMAQAE EWFKCRYAKL
TEAAQENKEA IRSAKEEIAE YRRQLQSKSI ELESVRGTKE SLERQLSDIE ERHNHDLSSY
QDTIQQLENE LRGTKWEMAR HLREYQDLLN VKMALDIEIA AYRKLLEGEE TRFASTFAGS
IGPLYTHRQP SITISSKFVE EIIEETKVED EKSEM
