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-APR-2013, entry version 89.
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;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC 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;
RA Geisler N., Kaufmann E., Fischer S., Plessmann U., Weber K.;
RT "Neurofilament architecture combines structural principles of
RT intermediate filaments with carboxy-terminal extensions increasing in
RT size between triplet proteins.";
RL EMBO J. 2:1295-1302(1983).
CC -!- FUNCTION: Neurofilaments usually contain three intermediate
CC filament proteins: L, M, and H which are involved in the
CC maintenance of neuronal caliber.
CC -!- SUBUNIT: Interacts with ARHGEF28 (By similarity). Interacts with
CC TRIM2 (By similarity).
CC -!- DOMAIN: The extra mass and high charge density that distinguish
CC the neurofilament proteins from all other intermediate filament
CC proteins are due to the tailpiece extensions. This region may form
CC a charged scaffolding structure suitable for interaction with
CC other neuronal components or ions.
CC -!- PTM: O-glycosylated (By similarity).
CC -!- PTM: Phosphorylated in the head and rod regions by the PKC kinase
CC PKN1, leading to the inhibition of polymerization (By similarity).
CC -!- PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1 (By
CC similarity).
CC -!- MISCELLANEOUS: NF-L is the most abundant of the three
CC neurofilament proteins and, like the other nonepithelial
CC intermediate filament proteins, it can form homopolymeric 10-nm
CC filaments.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
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DR PIR; A91337; QFPGL.
DR DisProt; DP00151; -.
DR ProteinModelPortal; P02547; -.
DR SMR; P02547; 87-123, 323-395.
DR STRING; 9823.ENSSSCP00000010302; -.
DR PaxDb; P02547; -.
DR eggNOG; NOG145720; -.
DR HOGENOM; HOG000230977; -.
DR HOVERGEN; HBG013015; -.
DR OrthoDB; EOG42Z4QC; -.
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 axon cargo transport; ISS:UniProtKB.
DR GO; GO:0019896; P:axon transport of mitochondrion; ISS:UniProtKB.
DR GO; GO:0033693; P:neurofilament bundle assembly; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axon cargo transport; ISS:UniProtKB.
DR InterPro; IPR016044; F.
DR InterPro; IPR001664; IF.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR018039; Intermediate_filament_CS.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PROSITE; PS00226; IF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Complete proteome;
KW Direct protein sequencing; Glycoprotein; Intermediate filament;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 549 Neurofilament light polypeptide.
FT /FTId=PRO_0000063789.
FT REGION 2 92 Head.
FT REGION 93 396 Rod.
FT REGION 93 124 Coil 1A.
FT REGION 125 137 Linker 1.
FT REGION 138 233 Coil 1B.
FT REGION 234 252 Linker 12.
FT REGION 253 271 Coil 2A.
FT REGION 272 280 Linker 2.
FT REGION 281 396 Coil 2B.
FT REGION 381 391 Epitope; recognized by IF-specific
FT monoclonal antibody.
FT REGION 397 549 Tail.
FT REGION 397 443 Tail, subdomain A.
FT REGION 444 549 Tail, subdomain B (acidic).
FT MOD_RES 2 2 N-acetylserine (By similarity).
FT MOD_RES 43 43 Phosphotyrosine (By similarity).
FT MOD_RES 56 56 Phosphoserine (By similarity).
FT MOD_RES 66 66 Phosphoserine (By similarity).
FT MOD_RES 424 424 Phosphotyrosine (By similarity).
FT MOD_RES 432 432 Phosphotyrosine (By similarity).
FT MOD_RES 472 472 Phosphoserine (By similarity).
FT CARBOHYD 21 21 O-linked (GlcNAc) (By similarity).
FT CARBOHYD 27 27 O-linked (GlcNAc) (By similarity).
FT UNSURE 323 323 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
//
