FUS_BOVIN
ID FUS_BOVIN Reviewed; 513 AA.
AC Q28009; Q0P5J2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=RNA-binding protein FUS;
DE AltName: Full=Protein pigpen;
GN Name=FUS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=8631501; DOI=10.1006/dbio.1996.0074;
RA Alliegro M.C., Alliegro M.A.;
RT "A nuclear protein regulated during the transition from active to quiescent
RT phenotype in cultured endothelial cells.";
RL Dev. Biol. 174:288-297(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DOMAIN.
RX PubMed=10694442; DOI=10.1006/excr.1999.4776;
RA Alliegro M.C.;
RT "A C-terminal carbohydrate-binding domain in the endothelial cell
RT regulatory protein, pigpen: new function for an EWS family member.";
RL Exp. Cell Res. 255:270-277(2000).
CC -!- FUNCTION: DNA/RNA-binding protein that plays a role in various cellular
CC processes such as transcription regulation, RNA splicing, RNA
CC transport, DNA repair and damage response. Binds to nascent pre-mRNAs
CC and acts as a molecular mediator between RNA polymerase II and U1 small
CC nuclear ribonucleoprotein thereby coupling transcription and splicing.
CC Binds also its own pre-mRNA and autoregulates its expression; this
CC autoregulation mechanism is mediated by non-sense-mediated decay. Plays
CC a role in DNA repair mechanisms by promoting D-loop formation and
CC homologous recombination during DNA double-strand break repair (By
CC similarity). In neuronal cells, plays crucial roles in dendritic spine
CC formation and stability, RNA transport, mRNA stability and synaptic
CC homeostasis (By similarity). {ECO:0000250|UniProtKB:P35637,
CC ECO:0000250|UniProtKB:P56959}.
CC -!- SUBUNIT: Self-oligomerizes (via N-terminal region). Oligomerization is
CC essential for chromatin binding. Component of nuclear riboprotein
CC complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-
CC terminus with SFRS13A. Interacts with OTUB1 and SARNP. Interacts with
CC LRSAM1. Interacts with SAFB1 in a DNA-dependent manner; this
CC interaction tethers FUS to chromatin. Interacts with MATR3. Interacts
CC with SNRNP70 and POLR2A; these interactions couple RNA transcription
CC and splicing. Interacts (through its RNA-binding domain) with RALY
CC (through its RNA-binding domain); both are components of the same RNPs.
CC {ECO:0000250|UniProtKB:P35637}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35637}.
CC Note=Displays a punctate pattern inside the nucleus and is excluded
CC from nucleoli. {ECO:0000250|UniProtKB:P35637}.
CC -!- DOMAIN: The C-terminal domain binds carbohydrates.
CC {ECO:0000269|PubMed:10694442}.
CC -!- PTM: Phosphorylated in its N-terminal serine residues upon induced DNA
CC damage. ATM and DNA-PK are able to phosphorylate FUS N-terminal region.
CC {ECO:0000250|UniProtKB:P35637}.
CC -!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}.
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DR EMBL; U26024; AAC13543.1; -; mRNA.
DR EMBL; BC119965; AAI19966.1; -; mRNA.
DR RefSeq; NP_776337.1; NM_173912.2.
DR RefSeq; XP_005224884.1; XM_005224827.3.
DR AlphaFoldDB; Q28009; -.
DR BMRB; Q28009; -.
DR SMR; Q28009; -.
DR STRING; 9913.ENSBTAP00000007571; -.
DR PaxDb; Q28009; -.
DR PeptideAtlas; Q28009; -.
DR PRIDE; Q28009; -.
DR GeneID; 280796; -.
DR KEGG; bta:280796; -.
DR CTD; 2521; -.
DR eggNOG; KOG1995; Eukaryota.
DR HOGENOM; CLU_025609_2_0_1; -.
DR InParanoid; Q28009; -.
DR OrthoDB; 1539664at2759; -.
DR TreeFam; TF322599; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034459; FUS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034870; TET_fam.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23238; PTHR23238; 1.
DR PANTHER; PTHR23238:SF5; PTHR23238:SF5; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..513
FT /note="RNA-binding protein FUS"
FT /id="PRO_0000081590"
FT DOMAIN 272..358
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 409..440
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 211
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 213
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 213
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 229
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 231
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 235
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 238
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 246
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 364
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 370
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 373
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 375
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 381
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 394
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 394
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56959"
FT MOD_RES 460
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 463
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 468
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 472
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 474
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 478
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 482
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 485
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 490
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT MOD_RES 490
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35637"
FT CONFLICT 65..66
FT /note="TG -> S (in Ref. 1; AAC13543)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="S -> G (in Ref. 1; AAC13543)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> S (in Ref. 1; AAC13543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 52311 MW; 0B10277BCC454D30 CRC64;
MASNDYTQQA TQSYGAYPTQ PGQGYSQQSN QPYGQQSYGG YGQSTDTSGY GQSSYSGSYG
QTQNTGYSTQ SAPQGYSSAG GYGSSQSSQS SYGQQSSYPG YGQQPAPSGT SGSYGSSSQS
SGYGQPQGGG YGQQSGYGGQ QQSYGQQQSY NPPQGYGQQS QYNSSGGGGG GGGGSYGQDQ
PSMSSGGGGG GYGNQDQSGG YGGGQQDRGG RGRGGGGGYN RSSGGYEPRG RGGGRGGRGG
MGGSDRGGFN KFGGPRDQGS RHDSEQDNSD NNTIFVQGLG ENVTIESVAD YFKQIGIIKT
NKKTGQPMIN LYTDRETGKL KGEATVSFDD PPSAKAAIDW FDGKEFSGNP IKVSFATRRA
DFNRGGGNGR GGRGRGGPMG RGGYGGGGSG GGGRGGFPSG GGGGGGQQRA GDWKCPNPTC
ENMNFSWRNE CNQCKAPKPD GPGGGPGGSH MGGNYGDDRR GGRGGYDRGG YRGRGGDRGG
FRGGRGGGDR GGFGPGKMDS RGEHRQDRRE RPY
