NFL_PIG
ID NFL_PIG Reviewed; 549 AA.
AC P02547;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Neurofilament light polypeptide;
DE Short=NF-L;
DE AltName: Full=68 kDa neurofilament protein;
DE AltName: Full=Neurofilament triplet L protein;
GN Name=NEFL;
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 2-549.
RX PubMed=3920075; DOI=10.1016/0014-5793(85)80357-4;
RA Geisler N., Plessmann U., Weber K.;
RT "The complete amino acid sequence of the major mammalian neurofilament
RT protein (NF-L).";
RL FEBS Lett. 182:475-478(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-83 AND 279-549.
RX PubMed=10872323; DOI=10.1002/j.1460-2075.1983.tb01584.x;
RA Geisler N., Kaufmann E., Fischer S., Plessmann U., Weber K.;
RT "Neurofilament architecture combines structural principles of intermediate
RT filaments with carboxy-terminal extensions increasing in size between
RT triplet proteins.";
RL EMBO J. 2:1295-1302(1983).
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 -!- DOMAIN: The extra mass and high charge density that distinguish the
CC neurofilament proteins from all other intermediate filament proteins
CC are due to the tailpiece extensions. This region may form a charged
CC scaffolding structure suitable for interaction with other neuronal
CC components or ions.
CC -!- PTM: O-glycosylated. {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 -!- 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}.
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DR PIR; A91337; QFPGL.
DR AlphaFoldDB; P02547; -.
DR SMR; P02547; -.
DR STRING; 9823.ENSSSCP00000010302; -.
DR iPTMnet; P02547; -.
DR PaxDb; P02547; -.
DR PeptideAtlas; P02547; -.
DR PRIDE; P02547; -.
DR eggNOG; ENOG502QSXY; Eukaryota.
DR InParanoid; P02547; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
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; IDA:CAFA.
DR GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0061564; P:axon development; IEA:InterPro.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISS:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0033693; P:neurofilament bundle assembly; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
DR DisProt; DP00151; -.
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 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; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02548,
FT ECO:0000269|PubMed:10872323, ECO:0000269|PubMed:3920075"
FT CHAIN 2..549
FT /note="Neurofilament light polypeptide"
FT /id="PRO_0000063789"
FT DOMAIN 89..400
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..92
FT /note="Head"
FT REGION 93..124
FT /note="Coil 1A"
FT REGION 125..137
FT /note="Linker 1"
FT REGION 138..233
FT /note="Coil 1B"
FT REGION 234..252
FT /note="Linker 12"
FT REGION 253..271
FT /note="Coil 2A"
FT REGION 272..280
FT /note="Linker 2"
FT REGION 281..396
FT /note="Coil 2B"
FT REGION 381..391
FT /note="Epitope; recognized by IF-specific monoclonal
FT antibody"
FT REGION 397..549
FT /note="Tail"
FT REGION 397..443
FT /note="Tail, subdomain A"
FT REGION 444..549
FT /note="Tail, subdomain B (acidic)"
FT REGION 462..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..549
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 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02548"
FT MOD_RES 102
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 526
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 UNSURE 323
FT /note="R or K"
SQ SEQUENCE 549 AA; 62072 MW; 23CD481372F7024B CRC64;
MSSFYSEPYY STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
SGLMPSLENL DLSQVAAISN DLKSIRTQEK AQLQDLNDRF ASFIERVHEL EQQNKVLEAQ
LLVLRQKHSE PSRFRALYEQ EIRDLRLAAE DATNEKQALQ GEREGLEETL RNLQARYEEE
VLSREDAEGR LMEARKGADE AALARAELEK RIDSLMDEIA FLKKVHEEEI AELQAQIQYA
QISVEMDVSS KPDLSAALKD IRAQYEKLAA KNMQNAEEWF KSRFTVLTES AAKNTDAVRA
AKDEVSESRR LLKAKTLEIE ACRGMNEALE KQLQELEDKQ NADISAMQDT INKLENELRT
TKSEMARYLK EYQDLLNVKM ALDIEIAAYR KLLEGEETRL SFTSVGSLTT GYSQSSQVFG
RSAYGGLQTS SYLMSTRSFP SYYTSHVQEE QIEVEETIEA AKAEEAKDEP PSEGEAEEEG
KEKEEAEAEA EAEEEGAQEE EEAAEKEESE EAKEEEGGEG EQGEETKEAE EEEKKDEGAG
EEQATKKKD
