NFL_COTJA
ID NFL_COTJA Reviewed; 556 AA.
AC Q02916;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Neurofilament light polypeptide;
DE Short=NF-L;
DE AltName: Full=Neurofilament triplet L protein;
GN Name=NEFL;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=8468353; DOI=10.1083/jcb.121.2.387;
RA Ohara O., Gahara Y., Miyake T., Teraoka H., Kitamura T.;
RT "Neurofilament deficiency in quail caused by nonsense mutation in
RT neurofilament-L gene.";
RL J. Cell Biol. 121:387-395(1993).
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 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 -!- 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 -!- DISEASE: Note=NF-L deficiency causes the disorder quiver.
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.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; D13223; BAA02504.1; -; Genomic_DNA.
DR EMBL; D13222; BAA02503.1; ALT_TERM; Genomic_DNA.
DR PIR; A46024; A46024.
DR AlphaFoldDB; Q02916; -.
DR SMR; Q02916; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005883; C:neurofilament; ISS:UniProtKB.
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: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 InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR027692; NF-L.
DR PANTHER; PTHR45652:SF8; PTHR45652:SF8; 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 3: Inferred from homology;
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..556
FT /note="Neurofilament light polypeptide"
FT /id="PRO_0000063791"
FT DOMAIN 91..402
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..94
FT /note="Head"
FT /evidence="ECO:0000250"
FT REGION 95..126
FT /note="Coil 1A"
FT REGION 127..139
FT /note="Linker 1"
FT REGION 140..235
FT /note="Coil 1B"
FT REGION 236..254
FT /note="Linker 12"
FT REGION 255..273
FT /note="Coil 2A"
FT REGION 274..282
FT /note="Linker 2"
FT REGION 283..398
FT /note="Coil 2B"
FT REGION 399..556
FT /note="Tail"
FT /evidence="ECO:0000250"
FT REGION 399..445
FT /note="Tail, subdomain A"
FT REGION 446..556
FT /note="Tail, subdomain B (acidic)"
FT REGION 464..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..556
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"
SQ SEQUENCE 556 AA; 62413 MW; 23A57AA7ECF945D2 CRC64;
MSSYGYDPFF PSYKRRYADS PRLHVSAMRS GGYSSARSAY SSLSAPVSSV SVRRSYATSS
ASGSLLHSVD SLDLSQVAAI SNDLKSIRSQ ERAQLQDLND RFACFIERVH ELEQQNKVLE
AELLVLRQKH AEPSRFRALY EQEIRELRLA AEEATSEKQA LQGERESLEE TLRGLQARYE
EEVLSREDAE ARLLEVRKGA DEAGLARAEL EKRVDSLLDE LAFLKKVHEE ELAELQAQIQ
YAHLSVEMDV SAKPDLSAAL RDIRAQYEKL AARNMQNAEE WFRSRFTVLS ESAAKNTDAV
RAAKDEVSES RRLLKAKTLE IEATRGMNEA LEKQLQELEE KQSADISALQ DTINKLENEL
RTTKSEMARY LKEYQDLLNV KMALDIEIAA YRKLLEGEET RLSFTSVGSI TSGYTQTAPT
FGRSAYSGLQ STSYLMTTRS FPTYYSSHVQ EEQIEIEETI EAAKAGEAKA APAEEGEEEE
KEEGEEEEAG GEEAEEEEEG AKEESEEGKE GEEEEGEETA AEDGEESQET AEETGEEEKE
EKEAAGKEET EVKKKA
