LRRF1_RAT
ID LRRF1_RAT Reviewed; 738 AA.
AC Q66HF9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Leucine-rich repeat flightless-interacting protein 1;
DE Short=LRR FLII-interacting protein 1;
GN Name=Lrrfip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=10364563; DOI=10.1161/01.res.84.11.1258;
RA Khachigian L.M., Santiago F.S., Rafty L.A., Chan O.L.-W., Delbridge G.J.,
RA Bobik A., Collins T., Johnson A.C.;
RT "GC factor 2 represses platelet-derived growth factor A-chain gene
RT transcription and is itself induced by arterial injury.";
RL Circ. Res. 84:1258-1267(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-560 AND SER-675, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional repressor which preferentially binds to the
CC GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate
CC expression of TNF, EGFR and PDGFA. May control smooth muscle cells
CC proliferation following artery injury through PDGFA repression. May
CC also bind double-stranded RNA. Positively regulates Toll-like receptor
CC (TLR) signaling in response to agonist probably by competing with the
CC negative FLII regulator for MYD88-binding (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10364563}.
CC -!- SUBUNIT: Homodimer. May also form higher oligomers. Interacts with FLII
CC (By similarity). Interacts with MYD88 (By similarity). Competes with
CC FLII for MyD88-binding, even in the absence of LPS (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Up-regulated after artery wall injury (at protein level).
CC {ECO:0000269|PubMed:10364563}.
CC -!- DOMAIN: The DNA-binding domain is intrinsically unstructured.
CC {ECO:0000250}.
CC -!- DOMAIN: The coiled coil mediates dimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
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DR EMBL; BC081883; AAH81883.1; -; mRNA.
DR RefSeq; NP_001014291.1; NM_001014269.1.
DR AlphaFoldDB; Q66HF9; -.
DR SMR; Q66HF9; -.
DR STRING; 10116.ENSRNOP00000045021; -.
DR iPTMnet; Q66HF9; -.
DR PhosphoSitePlus; Q66HF9; -.
DR jPOST; Q66HF9; -.
DR PaxDb; Q66HF9; -.
DR PRIDE; Q66HF9; -.
DR GeneID; 367314; -.
DR KEGG; rno:367314; -.
DR UCSC; RGD:1359548; rat.
DR CTD; 9208; -.
DR RGD; 1359548; Lrrfip1.
DR VEuPathDB; HostDB:ENSRNOG00000019892; -.
DR eggNOG; KOG2010; Eukaryota.
DR HOGENOM; CLU_018924_0_0_1; -.
DR InParanoid; Q66HF9; -.
DR OMA; KGYGFQC; -.
DR OrthoDB; 1434475at2759; -.
DR PhylomeDB; Q66HF9; -.
DR TreeFam; TF314109; -.
DR PRO; PR:Q66HF9; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019892; Expressed in lung and 19 other tissues.
DR Genevisible; Q66HF9; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR019139; LRRFIP1/2.
DR PANTHER; PTHR19212; PTHR19212; 2.
DR Pfam; PF09738; LRRFIP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT CHAIN 2..738
FT /note="Leucine-rich repeat flightless-interacting protein
FT 1"
FT /id="PRO_0000248394"
FT REGION 40..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..580
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT COILED 94..194
FT /evidence="ECO:0000250"
FT COMPBIAS 40..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ39"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ39"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UZ39"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q32MZ4"
SQ SEQUENCE 738 AA; 80019 MW; 10D6F003160948B7 CRC64;
MTSPEGAQNK EIDCLSPEAQ RLAEARLAAK RAARAEAREI RMKELERQQK EVEERPDKDF
AEKGSRNMPS LSAATLASLG GTSSRRGSGD TSISMDTEAS IREIKDSLAE VEEKYKKAMV
SNAQLDNEKT NFMYQVDTLK DMLLELEEQL AESQRQYEEK NKEFEREKHA HSILQFQFAE
VKEALRQREE MLEKHGIILN SEIATNGETS DTVNDVGYQA PTKITKEELN ALKAAGEGTL
GKAKEVEVKK EIVEKVGQRE TLQDSEQEQP KLNTGKDCVD RGVLHPGEKA ENQRPVEDSA
LSPGPLAGAK CEQEVQSQDQ ENTSILKSPE QIESHEVTNK SDSRDSNSPE PSSCRGGLDS
EVSGPTALGI KNQSENSMDS QGKENQEDLG KGSFEPRPDH VLGQTPEIDK VSCTDSRGTG
GNHLEDVVQA GDTIVEDQVG TMASAEQSKS MENHIGRSLN DGLGQSSERE LAHEAAELEE
ALTQSSQAGG ENTVTEAEDA AVRDEKPLQA DVQATPAAPT VQSGHQDTTG PGSTDTKHTS
PHAKERNKAK SEQQAEALDS PQKKTKNKKK KNKKKKAAAP METCKDANEE SSCQDPDVGD
GEEEERVQAT DKKWAAETPE LKEDPQSRPS GKQNDAEEDS GPAEGPTDVL DQNSLQCADG
DISPVGRKGP QRDASQIGGE EGLVPSQHPG QADEKGIEGH SVDNSDLSGE LGGFNSESGE
QAREEVGNSK SKEDCTMS
