NFL_XENTR
ID NFL_XENTR Reviewed; 557 AA.
AC B4F721;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Neurofilament light polypeptide;
DE Short=NF-L;
DE AltName: Full=Neurofilament triplet L protein;
GN Name=nefl;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2008) 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 other neuronal
CC intermediate filament proteins to form neuronal filamentous networks
CC (By similarity). {ECO:0000250|UniProtKB:P08551}.
CC -!- SUBUNIT: Forms homodimers (in vitro). {ECO:0000250|UniProtKB:P19527}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P08551}.
CC -!- MISCELLANEOUS: NF-L is the most abundant of the three neurofilament
CC proteins and, as the other nonepithelial intermediate filament
CC proteins, it can form homomeric 10-nm filaments. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; BC168098; AAI68098.1; -; mRNA.
DR AlphaFoldDB; B4F721; -.
DR SMR; B4F721; -.
DR STRING; 8364.ENSXETP00000048761; -.
DR PaxDb; B4F721; -.
DR PRIDE; B4F721; -.
DR eggNOG; ENOG502QSXY; Eukaryota.
DR InParanoid; B4F721; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; 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:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR GO; GO:0061564; P:axon development; IEA:InterPro.
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; 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 Intermediate filament; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..557
FT /note="Neurofilament light polypeptide"
FT /id="PRO_0000373800"
FT DOMAIN 86..396
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..89
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 90..121
FT /note="Coil 1A"
FT /evidence="ECO:0000250"
FT REGION 122..134
FT /note="Linker 1"
FT /evidence="ECO:0000250"
FT REGION 135..230
FT /note="Coil 1B"
FT /evidence="ECO:0000250"
FT REGION 231..248
FT /note="Linker 12"
FT /evidence="ECO:0000250"
FT REGION 249..267
FT /note="Coil 2A"
FT /evidence="ECO:0000250"
FT REGION 268..276
FT /note="Linker 2"
FT /evidence="ECO:0000250"
FT REGION 277..392
FT /note="Coil 2B"
FT /evidence="ECO:0000250"
FT REGION 393..557
FT /note="Tail"
FT /evidence="ECO:0000250"
FT REGION 393..437
FT /note="Tail, subdomain A"
FT /evidence="ECO:0000250"
FT REGION 438..557
FT /note="Tail, subdomain B (acidic)"
FT /evidence="ECO:0000250"
FT REGION 452..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..541
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 63115 MW; BE35CD724D7ED59B CRC64;
MSSYSYDPYY TSYKRRVVES SPRVHIRSSY VSPSRTTYSP VVSSTMRRSY AASSSSSSSL
LHGVDTMDLS QVAAISSDLK IVRTQEKAQL QDLNDRFANF IERVHELEQR NKVLEAELLL
LRQKHNEPSR LRDLYEQEVR ELRLAQEEAT GDRQTMRNER ERLEDALRLL QGRYEEEALS
REDAEARLLD VRKEADMAAL ARVELEKRMD SLLDEIAFLK KVHEEELAQL QSQVQYAQIS
LEVEVAKPDL SSALRDIRAQ YEKLAAKNMQ SAEDWFKSRF TVLTQSAARN TDAVRAAKDE
VSESRRMLSA KGLEIEACRG VNDALERQIQ ELEEKQSGEI AGMQDAINKL EEELRNTKSE
MARYLKEYQD LLNVKMALDI EIAAYRKLLE GEETRLSFSG VGAITSGYTQ SAPVFGRSAY
SLQSSSYMTS RAFPTYYSSH VQEEQLDIEE TIESSRAEEA KAEAPEEEEE EAGEEEAEGG
EGDEGEGEEG EEAKEEEAEE EGEGEEKEEE EEGEGEAEGE AEGEGEAEGE GEEEEEGKGE
EPAEEESKKK KKKKKKK
