NFM_CHICK
ID NFM_CHICK Reviewed; 858 AA.
AC P16053;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Neurofilament medium polypeptide;
DE Short=NF-M;
DE AltName: Full=160 kDa neurofilament protein;
DE AltName: Full=Neurofilament triplet M protein;
GN Name=NEFM;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2106668; DOI=10.1093/nar/18.3.521;
RA Zopf D., Dineva B., Betz H., Gundelfinger E.D.;
RT "Isolation of the chicken middle-molecular weight neurofilament (NF-M) gene
RT and characterization of its promoter.";
RL Nucleic Acids Res. 18:521-529(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 260-858.
RX PubMed=3123320; DOI=10.1101/gad.1.7.699;
RA Zopf D., Hermans-Borgmeyer I., Gundelfinger E.D., Betz H.;
RT "Identification of gene products expressed in the developing chick visual
RT system: characterization of a middle-molecular-weight neurofilament cDNA.";
RL Genes Dev. 1:699-708(1987).
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 other neuronal
CC intermediate filament proteins to form neuronal filamentous networks
CC (By similarity). {ECO:0000250|UniProtKB:P08553}.
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 coincident with a
CC change in the neurofilament function.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17102; CAA34958.1; -; Genomic_DNA.
DR EMBL; X05558; CAA29073.1; -; mRNA.
DR PIR; S15762; S15762.
DR RefSeq; NP_001095200.1; NM_001101730.1.
DR AlphaFoldDB; P16053; -.
DR SMR; P16053; -.
DR BioGRID; 676466; 1.
DR IntAct; P16053; 1.
DR STRING; 9031.ENSGALP00000000422; -.
DR iPTMnet; P16053; -.
DR PaxDb; P16053; -.
DR PRIDE; P16053; -.
DR GeneID; 396206; -.
DR KEGG; gga:396206; -.
DR CTD; 4741; -.
DR VEuPathDB; HostDB:geneid_396206; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; P16053; -.
DR OrthoDB; 898483at2759; -.
DR PhylomeDB; P16053; -.
DR PRO; PR:P16053; -.
DR Proteomes; UP000000539; 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 2: Evidence at transcript level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Glycoprotein; Intermediate filament; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..858
FT /note="Neurofilament medium polypeptide"
FT /id="PRO_0000063799"
FT DOMAIN 96..407
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..99
FT /note="Head"
FT REGION 22..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..131
FT /note="Coil 1A"
FT REGION 132..144
FT /note="Linker 1"
FT REGION 145..243
FT /note="Coil 1B"
FT REGION 244..260
FT /note="Linker 12"
FT REGION 261..282
FT /note="Coil 2A"
FT REGION 283..286
FT /note="Linker 2"
FT REGION 287..407
FT /note="Coil 2B"
FT REGION 408..858
FT /note="Tail"
FT REGION 478..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 427
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 547
FT /note="G -> R (in Ref. 2; CAA29073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 95835 MW; 50D10457BCE2B839 CRC64;
MSYTMEPLGN PSYRRVMTET RATYSRASAS PSSGFRSQSW SRGSGSTVSS SYKRTNLGAP
RTAYGSTVLS SAESLDVSQS SLLNGAAELK LSRSNEKEQL QGLNDRFAGY IEKVHYLEQQ
NKEIEAELAA LRQKHAGRAQ LGDAYEQELR ELRGALEQVS HEKAQIQLDS EHIEEDIQRL
RERFEDEARL RDETEATIAA LRKEMEEASL MRAELDKKVQ SLQDEVAFLR GNHEEEVAEL
LAQLQASHAT VERKDYLKTD LTTALKEIRA QLECQSDHNM HQAEEWFKCR YAKLTEAAEQ
NKEAIRSAKE EIAEYRRQLQ SKSIELESVR GTKESLERQL SDIEERHNND LTTYQDTIHQ
LENELRGTKW EMARHLREYQ DLLNVKMALD IEIAAYRKLL EGEETRFSAF SGSITGPIFT
HRQPSVTIAS TKIQKTKIEP PKLKVQHKFV EEIIEETKVE DEKSEMEDAL SAIAEEMAAK
AQEEEQEEEK AEEEAVEEEA VSEKAAEQAA EEEEKEEEEA EEEEAAKSDA AEEGGSKKEE
IEEKEEGEEA EEEEAEAKGK AEEAGAKVEK VKSPPAKSPP KSPPKSPVTE QAKAVQKAAA
EVGKDQKAEK AAEKAAKEEK AASPEKPATP KVTSPEKPAT PEKPPTPEKA ITPEKVRSPE
KPTTPEKVVS PEKPASPEKP RTPEKPASPE KPATPEKPRT PEKPATPEKP RSPEKPSSPL
KDEKAVVEES ITVTKVTKVT AEVEVSKEAR KEDIAVNGEV EEKKDEAKEK EAEEEEKGVV
TNGLDVSPVD EKGEKVVVTK KAEKITSEGG DSTTTYITKS VTVTQKVEEH EESFEEKLVS
TKKVEKVTSH AVVKEIKE
