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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
 
 
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