ID   QKI_CANLF               Reviewed;         341 AA.
AC   Q9GMY1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein quaking;
DE            Short=CqkI;
GN   Name=QKI;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; 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-binding protein that plays a central role in
CC       myelinization. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core
CC       sequence. Acts by regulating pre-mRNA splicing, mRNA export, mRNA
CC       stability and protein translation. Required to protect and promote
CC       stability of mRNAs such as MBP and CDKN1B which promotes
CC       oligodendrocyte differentiation. Participates in mRNA transport by
CC       regulating the nuclear export of MBP mRNA. Also involved in regulation
CC       of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Does not require RNA to homodimerize. Able to
CC       heterodimerize with BICC1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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}.
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}.
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DR   EMBL; AB047312; BAB11981.1; -; mRNA.
DR   RefSeq; NP_001003021.1; NM_001003021.2.
DR   AlphaFoldDB; Q9GMY1; -.
DR   SMR; Q9GMY1; -.
DR   STRING; 9612.ENSCAFP00000030367; -.
DR   PaxDb; Q9GMY1; -.
DR   PRIDE; Q9GMY1; -.
DR   Ensembl; ENSCAFT00030019710; ENSCAFP00030017189; ENSCAFG00030010469.
DR   Ensembl; ENSCAFT00040001984; ENSCAFP00040001698; ENSCAFG00040001027.
DR   GeneID; 606754; -.
DR   KEGG; cfa:606754; -.
DR   CTD; 9444; -.
DR   eggNOG; KOG1588; Eukaryota.
DR   InParanoid; Q9GMY1; -.
DR   OrthoDB; 1565749at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0042552; P:myelination; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR   GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   Gene3D; 3.30.1370.10; -; 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; PTHR11208; 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; SSF54791; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; Methylation;
KW   mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; SH3-binding; Translation regulation;
KW   Transport.
FT   CHAIN           1..341
FT                   /note="Protein quaking"
FT                   /id="PRO_0000239370"
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"
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