QKI_RAT
ID QKI_RAT Reviewed; 341 AA.
AC Q91XU1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein quaking;
DE Short=RqkI;
GN Name=Qki; Synonyms=Qk;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 98-302.
RC TISSUE=Brain;
RA Leng S., Tsutsumi M., Takase S., Abe S., Yamamoto Y., Fukunaga T.,
RA Saijoh K.;
RT "Differentially expressed genes.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11178867; DOI=10.1006/mcne.2000.0941;
RA Wu H.Y., Dawson M.R.L., Reynolds R., Hardy R.J.;
RT "Expression of QKI proteins and MAP1B identifies actively myelinating
RT oligodendrocytes in adult rat brain.";
RL Mol. Cell. Neurosci. 17:292-302(2001).
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
CC {ECO:0000269|PubMed:11178867}.
CC -!- TISSUE SPECIFICITY: Present in myelinating oligodendrocytes (at protein
CC level). {ECO:0000269|PubMed:11178867}.
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; AABR03000138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB054997; BAB62175.1; -; mRNA.
DR AlphaFoldDB; Q91XU1; -.
DR SMR; Q91XU1; -.
DR STRING; 10116.ENSRNOP00000034413; -.
DR iPTMnet; Q91XU1; -.
DR PhosphoSitePlus; Q91XU1; -.
DR jPOST; Q91XU1; -.
DR PaxDb; Q91XU1; -.
DR PRIDE; Q91XU1; -.
DR ABCD; Q91XU1; 4 sequenced antibodies.
DR RGD; 1584886; Qk.
DR eggNOG; KOG1588; Eukaryota.
DR InParanoid; Q91XU1; -.
DR PhylomeDB; Q91XU1; -.
DR PRO; PR:Q91XU1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008366; P:axon ensheathment; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IMP:RGD.
DR GO; GO:0048255; P:mRNA stabilization; IMP:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0042692; P:muscle cell differentiation; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
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 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_0000239376"
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; 37643 MW; 41B066F1711771C4 CRC64;
MVGEMETKEN PNPTPDYLMQ 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
