ID QKI_FELCA Reviewed; 341 AA.
AC Q7JJZ8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=KH domain-containing RNA-binding protein QKI {ECO:0000250|UniProtKB:Q9QYS9};
DE AltName: Full=Protein quaking {ECO:0000250|UniProtKB:Q9QYS9};
DE Short=FqkI {ECO:0000305};
GN Name=QKI {ECO:0000250|UniProtKB:Q9QYS9};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Murata T., Yamashiro Y., Kondo T., Une S., Nakaichi M.;
RT "Nucleotide sequence of cDNA encoding for canine and feline quaking
RT protein.";
RL J. Jpn. Vet. Med. Assoc. 55:505-508(2002).
CC -!- FUNCTION: RNA reader protein, which recognizes and binds specific RNAs,
CC thereby regulating RNA metabolic processes, such as pre-mRNA splicing,
CC circular RNA (circRNA) formation, mRNA export, mRNA stability and/or
CC translation. Involved in various cellular processes, such as mRNA
CC storage into stress granules, apoptosis, lipid deposition, interferon
CC response, glial cell fate and development. Binds to the 5'-NACUAAY-
CC N(1,20)-UAAY-3' RNA core sequence. Acts as a mRNA modification reader
CC that specifically recognizes and binds mRNA transcripts modified by
CC internal N(7)-methylguanine (m7G). Promotes the formation of circular
CC RNAs (circRNAs) during the epithelial to mesenchymal transition and in
CC cardiomyocytes: acts by binding to sites flanking circRNA-forming
CC exons. CircRNAs are produced by back-splicing circularization of pre-
CC mRNAs. Plays a central role in myelinization via 3 distinct mechanisms
CC (By similarity). First, acts by protecting and promoting stability of
CC target mRNAs such as MBP, SIRT2 and CDKN1B, which promotes
CC oligodendrocyte differentiation. Second, participates in mRNA transport
CC by regulating the nuclear export of MBP mRNA. Finally, indirectly
CC regulates mRNA splicing of MAG pre-mRNA during oligodendrocyte
CC differentiation by acting as a negative regulator of MAG exon 12
CC alternative splicing: acts by binding to HNRNPA1 mRNA splicing factor,
CC preventing its translation. Involved in microglia differentiation and
CC remyelination by regulating microexon alternative splicing of the Rho
CC GTPase pathway (By similarity). Involved in macrophage differentiation:
CC promotes monocyte differentiation by regulating pre-mRNA splicing in
CC naive peripheral blood monocytes (By similarity). Acts as an important
CC regulator of muscle development: required for the contractile function
CC of cardiomyocytes by regulating alternative splicing of cardiomyocyte
CC transcripts. Acts as a negative regulator of thermogenesis by
CC decreasing stability, nuclear export and translation of mRNAs encoding
CC PPARGC1A and UCP1. Also required for visceral endoderm function and
CC blood vessel development (By similarity). May also play a role in
CC smooth muscle development (By similarity). In addition to its RNA-
CC binding activity, also acts as a nuclear transcription coactivator for
CC SREBF2/SREBP2 (By similarity). {ECO:0000250|UniProtKB:Q96PU8,
CC ECO:0000250|UniProtKB:Q9QYS9}.
CC -!- SUBUNIT: Homodimer; does not require RNA to homodimerize (By
CC similarity). Able to heterodimerize with BICC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PU8, ECO:0000250|UniProtKB:Q9QYS9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PU8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96PU8}.
CC -!- DOMAIN: The KH domain and the Qua2 region are involved in RNA binding.
CC {ECO:0000250|UniProtKB:Q96PU8}.
CC -!- PTM: Methylated by PRMT1. {ECO:0000250|UniProtKB:Q9QYS9}.
CC -!- PTM: Tyrosine phosphorylated at its C-terminus, probably by FYN.
CC Phosphorylation leads to decreased mRNA-binding affinity, affecting
CC transport and/or stabilization of MBP mRNA (By similarity).
CC {ECO:0000250|UniProtKB:Q9QYS9}.
CC -!- PTM: Ubiquitinated by RNF6 in macrophages, leading to its degradation.
CC {ECO:0000250|UniProtKB:Q9QYS9}.
CC -!- SIMILARITY: Belongs to the quaking family. {ECO:0000305}.
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DR EMBL; AB061272; BAB47360.1; -; mRNA.
DR RefSeq; NP_001009232.1; NM_001009232.1.
DR AlphaFoldDB; Q7JJZ8; -.
DR SMR; Q7JJZ8; -.
DR STRING; 9685.ENSFCAP00000037791; -.
DR PaxDb; 9685-ENSFCAP00000015539; -.
DR GeneID; 493723; -.
DR KEGG; fca:493723; -.
DR eggNOG; KOG1588; Eukaryota.
DR InParanoid; Q7JJZ8; -.
DR OrthoDB; 1397at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0014004; P:microglia differentiation; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1905869; P:negative regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:UniProtKB.
DR GO; GO:0045650; P:negative regulation of macrophage differentiation; ISS:UniProtKB.
DR GO; GO:2000626; P:negative regulation of miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0048710; P:regulation of astrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; ISS:UniProtKB.
DR CDD; cd22465; KH-I_Hqk; 1.
DR Gene3D; 1.20.5.4010; -; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032367; Quaking_NLS.
DR InterPro; IPR032377; STAR_dimer.
DR PANTHER; PTHR11208:SF125; PROTEIN QUAKING; 1.
DR PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16551; Quaking_NLS; 1.
DR Pfam; PF16544; STAR_dimer; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Methylation; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; SH3-binding;
KW Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..341
FT /note="KH domain-containing RNA-binding protein QKI"
FT /id="PRO_0000239371"
FT DOMAIN 87..153
FT /note="KH"
FT REGION 11..82
FT /note="Qua1 domain; involved in homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT REGION 182..213
FT /note="Qua2 domain; involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOTIF 276..279
FT /note="SH3-binding"
FT MOTIF 324..330
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9QYS9"
FT SITE 97
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 120
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 124
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 130
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 190
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT SITE 193
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOD_RES 227
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOD_RES 242
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOD_RES 242
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96PU8"
FT MOD_RES 256
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYS9"
SQ SEQUENCE 341 AA; 37671 MW; 43E7F3A426A494C4 CRC64;
MVGEMETKEK PKPTPDYLMQ LMNDKKLMSS LPNFCGIFNH LERLLDEEIS RVRKDMYNDT
LNGSTEKRSA ELPDAVGPIV QLQEKLYVPV KEYPDFNFVG RILGPRGLTA KQLEAETGCK
IMVRGKGSMR DKKKEEQNRG KPNWEHLNED LHVLITVEDA QNRAEIKLKR AVEEVKKLLV
PAAEGEDSLK KMQLMELAIL NGTYRDANIK SPALAFSLAA TAQAAPRIIT GPAPVLPPAA
LRTPTPAGPT IMPLIRQIQT AVMPNGTPHP TAAIVPPGPE AGLIYTPYEY PYTLAPATSI
LEYPIEPSGV LGAVATKVRR HDMRVHPYQR IVTADRAATG N
//
