NFM_BOVIN
ID NFM_BOVIN Reviewed; 926 AA.
AC O77788;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 25-MAY-2022, entry version 131.
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;
GN Name=NEFM; Synonyms=NEF3, NFM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE OF 2-116, ACETYLATION AT SER-2, PHOSPHORYLATION AT
RP SER-513; SER-547; SER-555; SER-561; THR-628; SER-630; SER-635; SER-640;
RP THR-647; SER-650; SER-655; SER-665; SER-670; THR-677; SER-680; SER-685;
RP SER-695; SER-727; SER-751; SER-757; SER-771 AND SER-847, AND MASS
RP SPECTROMETRY.
RX PubMed=14967049; DOI=10.1021/bi030196q;
RA Trimpin S., Mixon A.E., Stapels M.D., Kim M.Y., Spencer P.S., Deinzer M.L.;
RT "Identification of endogenous phosphorylation sites of bovine medium and
RT low molecular weight neurofilament proteins by tandem mass spectrometry.";
RL Biochemistry 43:2091-2105(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-926.
RA Hill W.D., Zhang L., Balin B.J., Sprinkle T.J., Spicer K., Gearhart D.A.;
RT "The bovine neurofilament M subunit has a novel set of KSP repeats normally
RT restricted to NF-H.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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: Phosphorylated on a number of serine residues in the repeated K-S-
CC P tripeptide motif. Phosphorylation of NFH may result in the formation
CC of interfilament cross-links that are important in the maintenance of
CC axonal caliber (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC leading to the inhibition of polymerization. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=105044; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14967049};
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AF091342; AAC36357.1; -; mRNA.
DR AlphaFoldDB; O77788; -.
DR SMR; O77788; -.
DR IntAct; O77788; 1.
DR STRING; 9913.ENSBTAP00000036438; -.
DR iPTMnet; O77788; -.
DR PaxDb; O77788; -.
DR PeptideAtlas; O77788; -.
DR PRIDE; O77788; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; O77788; -.
DR OrthoDB; 898483at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005883; C:neurofilament; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; 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; 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; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14967049"
FT CHAIN 2..926
FT /note="Neurofilament medium polypeptide"
FT /id="PRO_0000063793"
FT DOMAIN 101..412
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REPEAT 512..516
FT /note="1"
FT REPEAT 619..623
FT /note="2"
FT REPEAT 624..628
FT /note="3"
FT REPEAT 629..633
FT /note="4"
FT REPEAT 634..638
FT /note="5"
FT REPEAT 639..643
FT /note="6"
FT REPEAT 644..648
FT /note="7"
FT REPEAT 649..653
FT /note="8"
FT REPEAT 654..658
FT /note="9"
FT REPEAT 659..663
FT /note="10"
FT REPEAT 664..668
FT /note="11"
FT REPEAT 669..673
FT /note="12"
FT REPEAT 674..678
FT /note="13"
FT REPEAT 679..683
FT /note="14"
FT REPEAT 684..688
FT /note="15"
FT REPEAT 689..693
FT /note="16"
FT REPEAT 694..698
FT /note="17"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..104
FT /note="Head"
FT REGION 79..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..136
FT /note="Coil 1A"
FT REGION 137..149
FT /note="Linker 1"
FT REGION 150..248
FT /note="Coil 1B"
FT REGION 249..265
FT /note="Linker 12"
FT REGION 266..287
FT /note="Coil 2A"
FT REGION 288..291
FT /note="Linker 2"
FT REGION 292..412
FT /note="Coil 2B"
FT REGION 413..926
FT /note="Tail"
FT REGION 487..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..698
FT /note="17 X 5 AA approximate tandem repeats of K-S-P-
FT [TVEA]-[AKETP]"
FT COMPBIAS 504..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 42
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 320
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 628
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 647
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 677
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08553"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12839"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14967049"
FT CARBOHYD 47
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 926 AA; 103210 MW; B1C2FA96E31793C0 CRC64;
MSYTLDSLGN PSAYRRVTET RSSFSRISGS PSSGFRSQSW SRGSPSTVSS SYKRSALAPR
LTYSSAMLSS AESSLDFSQS SSLLDGGSGP GGDYKLSRSN EKEQIQGLND RFAGYIEKVH
YLEQQNKEIE AEIQALRQKQ ASHAQLGDAY DQEIRELRAT LEMVNHEKAQ VQLDSDHLEE
DIHRLKERFE EEARLRDDTE AAIRALRKDI EESSLVKVEL DKKVQSLQDE VAFLRSNHEE
EVADLLAQIQ ASHITVERKD YLKTDISTAL KEIRSQLESH SDQNMHQAEE WFKCRYAKLT
EAAEQNKEAI RSAKEEIAEY RRQLQSKSIE LESVRGTKES LERQLSDIEE RHNHDLSSYQ
DTIQQLENEL RGTKWEMARH LREYQDLLNV KMALDIEIAA YRKLLEGEET RFSTFAGSIT
GPLYTHRQPS IAISSKIQKT KVEAPKLKVQ HKFVEEIIEE TKVEDEKSEM EEALTAITEE
LAVSVKEEVK EEEAEEKEEK EEAEEEVVAA KKSPVKATAP ELKEEEGEKE EEEGQEEEEE
EEEAAKSDQA EEGGSEKEGS SEKEEGEQEE EGETEAEGEG EEAAAEAKEE KKMEEKAEEV
APKEELAAEA KVEKPEKAKS PVAKSPTTKS PTAKSPEAKS PEAKSPTAKS PTAKSPVAKS
PTAKSPEAKS PEAKSPTAKS PTAKSPAAKS PAPKSPVEEV KPKAEAGAEK GEQKEKVEEE
KKEAKESPKE EKAEKKEEKP KDVPEKKKAE SPVKAESPVK EEVPAKPVKV SPEKEAKEEE
KPQEKEKEKE KVEEVGGKEE GGLKESRKED IAINGEVEGK EEEQETKEKG SGGEEEKGVV
TNGLDVSPGD EKKGGDKSEE KVVVTKMVEK ITSEGGDGAT KYITKSVTVT QKVEEHEETF
EEKLVSTKKV EKVTSHAIVK EVTQSD
