QKIA_DANRE
ID QKIA_DANRE Reviewed; 341 AA.
AC Q6P0D0; O42476; Q6PHD0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein quaking-A;
DE Short=zqk;
GN Name=qkia; Synonyms=qk;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DEVELOPMENTAL STAGE.
RX PubMed=9486543; DOI=10.1016/s0925-4773(97)00164-0;
RA Tanaka H., Abe K., Kim C.-H.;
RT "Cloning and expression of the quaking gene in the zebrafish embryo.";
RL Mech. Dev. 69:209-213(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 which promotes oligodendrocyte differentiation.
CC Participates in mRNA transport by regulating the nuclear export of MBP
CC mRNA. Also involved in regulation of mRNA splicing of some pre-mRNA.
CC Acts as a translational repressor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Does not require RNA to homodimerize (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P0D0-1; Sequence=Displayed;
CC Name=2; Synonyms=ZD;
CC IsoId=Q6P0D0-2; Sequence=VSP_019204;
CC -!- DEVELOPMENTAL STAGE: Maternally and zygotically expressed. Ubiquitously
CC expressed during cleavage and blastula periods, and then it accumulates
CC in the dorsal midline of the body trunk during gastrulation. During
CC segmentation and pharyngula periods it is expressed in the neural
CC tissue of the head region, and in the paraxial mesoderm of the body
CC trunk. Subsequently expression diminishes until the hatching period,
CC when it is expressed only in the cardiac sac and pectoral finbuds.
CC Isoform 2 localizes in neural tissue in the head region, but not in the
CC paraxial mesoderm in the body trunk. {ECO:0000269|PubMed:9486543}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U62134; AAB70454.1; ALT_INIT; mRNA.
DR EMBL; BC056599; AAH56599.1; -; mRNA.
DR EMBL; BC065667; AAH65667.1; -; mRNA.
DR RefSeq; NP_571299.1; NM_131224.1.
DR AlphaFoldDB; Q6P0D0; -.
DR SMR; Q6P0D0; -.
DR GeneID; 30471; -.
DR KEGG; dre:30471; -.
DR CTD; 30471; -.
DR ZFIN; ZDB-GENE-990415-230; qkia.
DR InParanoid; Q6P0D0; -.
DR OrthoDB; 1565749at2759; -.
DR ChiTaRS; qkia; zebrafish.
DR PRO; PR:Q6P0D0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IGI:ZFIN.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:ZFIN.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:ZFIN.
DR GO; GO:0014866; P:skeletal myofibril assembly; IGI:ZFIN.
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 Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Reference proteome; RNA-binding; SH3-binding; Translation regulation;
KW Transport.
FT CHAIN 1..341
FT /note="Protein quaking-A"
FT /id="PRO_0000239378"
FT DOMAIN 87..153
FT /note="KH"
FT MOTIF 276..279
FT /note="SH3-binding"
FT VAR_SEQ 311
FT /note="L -> LGKRAWGLGTSPFGVPQEGTPGVFYGGILDGASPSPVQDSLK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9486543, ECO:0000303|Ref.2"
FT /id="VSP_019204"
SQ SEQUENCE 341 AA; 37934 MW; 8960AA37B4C07DE7 CRC64;
MVGEMEVKER PRPSPDYLMQ LLNEKKLMTS LPNLCGIFTH LERLLDEEIN RVRKDMYNDS
VNGLVDKHPL ELPEPVGPIV HLQEKLFVPV KEYPDYNFVG RILGPRGLTA KQLEAETGCK
IMVRGRSSMR DKKKEEQNRG KPNWEHLNED LHVLITVEDT QTRAEIKMRR AVEEVKKLLV
PAAEGEDNLK KMQLMELAIL NGTYRDTNIK APTLAFSLAA AAAAAQGPRL IAAPPGQVLP
PATLRPPTPA GTPIMNIIRP TQMATVLPNG TPTLVPPTPD AGIIYTTPYD YPYALAPTSL
LEYPIEHSGV LGAMATKVRR HDSRVHPYQR IVTADRAATG N
