QKIA_XENLA
ID QKIA_XENLA Reviewed; 341 AA.
AC Q32NN2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein quaking-A;
DE Short=Xqua;
GN Name=qki-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), RNA-BINDING, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9133592; DOI=10.1016/s0378-1119(96)00795-0;
RA Zorn A.M., Grow M., Patterson K.D., Ebersole T.A., Chen Q., Artzt K.,
RA Krieg P.A.;
RT "Remarkable sequence conservation of transcripts encoding amphibian and
RT mammalian homologues of quaking, a KH domain RNA-binding protein.";
RL Gene 188:199-206(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR LOCATION,
RP RNA-BINDING, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=9303534; DOI=10.1101/gad.11.17.2176;
RA Zorn A.M., Krieg P.A.;
RT "The KH domain protein encoded by quaking functions as a dimer and is
RT essential for notochord development in Xenopus embryos.";
RL Genes Dev. 11:2176-2190(1997).
RN [4]
RP STRUCTURE BY NMR OF 82-215.
RX PubMed=15811367; DOI=10.1016/j.jmb.2005.02.058;
RA Maguire M.L., Guler-Gane G., Nietlispach D., Raine A.R.C., Zorn A.M.,
RA Standart N., Broadhurst R.W.;
RT "Solution structure and backbone dynamics of the KH-QUA2 region of the
RT Xenopus STAR/GSG quaking protein.";
RL J. Mol. Biol. 348:265-279(2005).
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). Essential for
CC notochord development. {ECO:0000250, ECO:0000269|PubMed:9303534}.
CC -!- SUBUNIT: Homodimer. Does not require RNA to homodimerize.
CC {ECO:0000269|PubMed:9303534}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9303534}. Cytoplasm
CC {ECO:0000269|PubMed:9303534}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q32NN2-1; Sequence=Displayed;
CC Name=2; Synonyms=Xqua365;
CC IsoId=Q32NN2-2; Sequence=VSP_019206;
CC Name=3; Synonyms=Xqua357;
CC IsoId=Q32NN2-3; Sequence=VSP_019206, VSP_019207;
CC Name=4;
CC IsoId=Q32NN2-4; Sequence=VSP_019207;
CC -!- DEVELOPMENTAL STAGE: First detected in the chordamesoderm of the dorsal
CC blastopore lip of the mid-gastrula embryo (stage 11). This tissue,
CC which differentiates into the notochord. In late gastrula embryos
CC (stage 13), it is highly expressed in the notochord, and the original
CC expression domain expands to include the tissue surrounding the
CC blastopore. In neurula embryos, it is maintained in the notochord and
CC the circumblastoporal region and now also extends to the paraxial
CC mesoderm and the neuroectoderm. By the tailbud stage, it is expressed
CC in various mesodermal and neural tissues. Highly expressed in the brain
CC and the neural tube. Maintained throughout development to the tadpole
CC stage (stage 35). {ECO:0000269|PubMed:9133592,
CC ECO:0000269|PubMed:9303534}.
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DR EMBL; BC108554; AAI08555.1; -; mRNA.
DR RefSeq; NP_001089857.1; NM_001096388.1. [Q32NN2-4]
DR PDB; 2BL5; NMR; -; A=82-215.
DR PDB; 2YMJ; NMR; -; A/B=8-57.
DR PDBsum; 2BL5; -.
DR PDBsum; 2YMJ; -.
DR AlphaFoldDB; Q32NN2; -.
DR BMRB; Q32NN2; -.
DR SMR; Q32NN2; -.
DR DNASU; 734923; -.
DR GeneID; 734923; -.
DR KEGG; xla:734923; -.
DR CTD; 734923; -.
DR Xenbase; XB-GENE-6254729; qki.S.
DR OMA; GHTIMPL; -.
DR OrthoDB; 1565749at2759; -.
DR EvolutionaryTrace; Q32NN2; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 734923; Expressed in blastula and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IMP:CAFA.
DR GO; GO:0005634; C:nucleus; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0008266; F:poly(U) RNA binding; IMP:CAFA.
DR GO; GO:0003727; F:single-stranded RNA binding; IMP:CAFA.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0060034; P:notochord cell differentiation; IMP:CAFA.
DR GO; GO:0030903; P:notochord development; IMP:CAFA.
DR GO; GO:0014028; P:notochord formation; IMP:CAFA.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR DisProt; DP00286; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Reference proteome; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..341
FT /note="Protein quaking-A"
FT /id="PRO_0000239380"
FT DOMAIN 88..154
FT /note="KH"
FT VAR_SEQ 1
FT /note="M -> MFFGHAGCDIRNSAAPAFGLFDWNM (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:9133592"
FT /id="VSP_019206"
FT VAR_SEQ 214..221
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019207"
FT CONFLICT 194
FT /note="Q -> K (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:2YMJ"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2YMJ"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2YMJ"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2BL5"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2BL5"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2BL5"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2BL5"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2BL5"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2BL5"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:2BL5"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2BL5"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2BL5"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2BL5"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2BL5"
SQ SEQUENCE 341 AA; 37879 MW; F39F36CB80DE77A1 CRC64;
MVGEMETKEK PKPTPDYLMQ LMNDKKLMSS LPNFCGIFTH LERLLDEEIS RVRKDMYNDT
MNSSSNEKRT SELPDGIGPI VQLQEKLYVP VKEYPDFNFV GRILGPRGLT AKQLEAETGC
KIMVRGKGSM RDKKKEEQNR GKPNWEHLNE DLHVLITVED AQNRAELKLK RAVEEVKKLL
VPAAEGEDSL KKMQLMELAI LNGTYRDANL KSPALAFSLA ATGQAPRIIT GPAPVLSPAA
LRTPTPAGHT LMPLIRQIQT AVMPNGTPHP TATLMQQAPE GGLIYTPYEY PYTLAPATSI
LEYPIEASGV LGAVATKVRR HDMRVHPYQR IVTADRAATG N
