NFL_PONAB
ID NFL_PONAB Reviewed; 543 AA.
AC Q5R408; Q5R689; Q5R6Q8; Q5R6U5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Neurofilament light polypeptide;
DE Short=NF-L;
DE AltName: Full=Neurofilament triplet L protein;
GN Name=NEFL;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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:P08551}.
CC -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Forms
CC heterodimers with NEFH or NEFM; which can further hetero-oligomerize
CC (in vitro) (By similarity). Forms heterodimers with INA (in vitro) (By
CC similarity). Interacts with ARHGEF28. Interacts with TRIM2.
CC {ECO:0000250, ECO:0000250|UniProtKB:P19527}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P08551}.
CC -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1,
CC leading to the inhibition of polymerization. {ECO:0000250}.
CC -!- PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}.
CC -!- MISCELLANEOUS: NF-L is the most abundant of the three neurofilament
CC proteins and, like the other nonepithelial intermediate filament
CC proteins, it can form homomeric 10-nm filaments.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH92515.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR860389; CAH92515.1; ALT_FRAME; mRNA.
DR EMBL; CR860427; CAH92552.1; -; mRNA.
DR EMBL; CR860605; CAH92727.1; -; mRNA.
DR EMBL; CR861452; CAH93508.1; -; mRNA.
DR RefSeq; NP_001126494.1; NM_001133022.2.
DR AlphaFoldDB; Q5R408; -.
DR SMR; Q5R408; -.
DR STRING; 9601.ENSPPYP00000020675; -.
DR PRIDE; Q5R408; -.
DR Ensembl; ENSPPYT00000021504; ENSPPYP00000020675; ENSPPYG00000018449.
DR GeneID; 100173482; -.
DR KEGG; pon:100173482; -.
DR CTD; 4747; -.
DR eggNOG; ENOG502QSXY; Eukaryota.
DR GeneTree; ENSGT00940000156208; -.
DR HOGENOM; CLU_012560_7_3_1; -.
DR InParanoid; Q5R408; -.
DR OMA; YEPYYAT; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0005883; C:neurofilament; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0099182; C:presynaptic intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0040011; P:locomotion; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0033693; P:neurofilament bundle assembly; IEA:Ensembl.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
DR GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR027692; NF-L.
DR PANTHER; PTHR45652:SF8; PTHR45652:SF8; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 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 Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Glycoprotein; Intermediate filament; Methylation; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT CHAIN 2..543
FT /note="Neurofilament light polypeptide"
FT /id="PRO_0000373799"
FT DOMAIN 90..400
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..92
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 93..124
FT /note="Coil 1A"
FT /evidence="ECO:0000250"
FT REGION 125..137
FT /note="Linker 1"
FT /evidence="ECO:0000250"
FT REGION 138..234
FT /note="Coil 1B"
FT /evidence="ECO:0000250"
FT REGION 235..252
FT /note="Linker 12"
FT /evidence="ECO:0000250"
FT REGION 253..271
FT /note="Coil 2A"
FT /evidence="ECO:0000250"
FT REGION 272..280
FT /note="Linker 2"
FT /evidence="ECO:0000250"
FT REGION 281..396
FT /note="Coil 2B"
FT /evidence="ECO:0000250"
FT REGION 397..543
FT /note="Tail"
FT /evidence="ECO:0000250"
FT REGION 397..443
FT /note="Tail, subdomain A"
FT /evidence="ECO:0000250"
FT REGION 444..543
FT /note="Tail, subdomain B (acidic)"
FT /evidence="ECO:0000250"
FT REGION 462..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..543
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|UniProtKB:P02548"
FT MOD_RES 23
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 23
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 30
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08551"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19527"
FT CARBOHYD 21
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="Y -> H (in Ref. 1; CAH92552)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="S -> R (in Ref. 1; CAH92515)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="L -> V (in Ref. 1; CAH92515)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> T (in Ref. 1; CAH93508)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="R -> H (in Ref. 1; CAH93508)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="Y -> C (in Ref. 1; CAH93508)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="K -> R (in Ref. 1; CAH92552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 61517 MW; 98C1712D8ACFF33A CRC64;
MSSFSYEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA
ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE
EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI SFLKKVHEEE IAELQAQIQY
AQISVEMDVT KPDLSAALKD IRAQYEKLAA KNMQNAEEWF KSRFTVLTES AAKNTDAVRA
AKDEVSESRR LLKAKTLEIE ACRGMNEALE KQLQELEDKQ NADISAMQDT INKLENELRT
TKSEMARYLK EYQDLLNVKM ALDIEIAAYR KLLEGEETRL SFTSVGSITS GYSQSSQVFG
RSAYGGLQTS SYLMSTRSFP SYYTSHVQEE QIEVEETIEA AKAEEAKDEP PSEGEAEEEE
KDKEEAEEEE AAEEEEAAKE ESEEAKEEEE GGEGEEGEET KEAEEEEKKV EGAGEEQAAK
KKD
