NFM_RABIT
ID NFM_RABIT Reviewed; 644 AA.
AC P54938;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 109.
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, NFM;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8899542; DOI=10.1006/jmcc.1996.0176;
RA Vitadello M., Vettore S., Lamar E., Chien K.R., Gorza L.;
RT "Neurofilament M mRNA is expressed in conduction system myocytes of the
RT developing and adult rabbit heart.";
RL J. Mol. Cell. Cardiol. 28:1833-1844(1996).
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 EMBL; Z47378; CAA87454.1; -; mRNA.
DR PIR; S55395; S55395.
DR AlphaFoldDB; P54938; -.
DR SMR; P54938; -.
DR PRIDE; P54938; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P54938; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005883; C:neurofilament; IEA:InterPro.
DR GO; GO:0033693; P:neurofilament bundle assembly; IEA:InterPro.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR027697; NF-M.
DR PANTHER; PTHR45652:SF3; PTHR45652:SF3; 2.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Intermediate filament; Phosphoprotein; Reference proteome.
FT CHAIN <1..644
FT /note="Neurofilament medium polypeptide"
FT /id="PRO_0000063797"
FT DOMAIN <1..197
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION <1..33
FT /note="Coil 1B"
FT REGION 34..50
FT /note="Linker 12"
FT REGION 51..72
FT /note="Coil 2A"
FT REGION 73..76
FT /note="Linker 2"
FT REGION 77..197
FT /note="Coil 2B"
FT REGION 198..643
FT /note="Tail"
FT REGION 270..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 105
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O77788"
FT CARBOHYD 217
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 644 AA; 72451 MW; 030FDAA622889678 CRC64;
VKVELDKKVQ SLQDEVAFLR TNHEEEVADL LAQIQASHIT VERKDYLKTD ISSALKEIRS
QLECHSDQNM HQAEEWFKCR YAKLTEAAEQ NKEAIRSAKE EIAEYRRQLQ SKSIELESVA
WHKESLERHV SDIEERHNHD LSSYQDTIQQ LENELRGTKW EMARHLREYQ DLLNVKMALD
IEIAAYRKLL EGEETRFSTF SGSITGPLYT HRQPSVTISS KIQKTKVEAP KLKVQHKFVE
EIIEETKVED EKSEMEDALT AIAEELAVSV KEEEKEEEAE GKEEEQEAEE EVAAAKKSPV
KATTPEIKEE EGEKEEEGQE EEEEEEDEGV KSDQAEEGGS EKEGSSKNEG EQEEGETEAE
GEVEEAEAKE EKKTEEKSEE VAAKEEPVTE AKVGKPEKAK SPVPKSPVEE VKPKAEATAG
KGEQKEEEEK VEEEKKKAAK ESPKEEKVEK KEEKPKDVPK KKAESPVKEE AAEEAATITK
PTKVGLEKET KEGEKPLQQE KEKEKAGEEG GSEEEGSDQG SKRAKKEDIA VNGEGEGKEE
EEPETKEKGS GREEEKGVVT NGLDLSPADE KKGGDRSEEK VVVTKKVEKI TTEGGDGATK
YITKSVTAQK VEEHEETFEE KLVSTKKVEK VTSHAIVKEV TQSD
