PKRI1_MOUSE
ID PKRI1_MOUSE Reviewed; 186 AA.
AC Q9CWV6; Q8BL85; Q9CXA5; Q9CY32;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=PRKR-interacting protein 1;
DE AltName: Full=Protein C114;
GN Name=Prkrip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY IL11, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH
RP EIF2AK2.
RX PubMed=12679338; DOI=10.1074/jbc.m212969200;
RA Yin Z., Haynie J., Williams B.R.G., Yang Y.-C.;
RT "C114 is a novel IL-11-inducible nuclear double-stranded RNA-binding
RT protein that inhibits protein kinase R.";
RL J. Biol. Chem. 278:22838-22845(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Liver, Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (By similarity). Binds double-stranded RNA. Inhibits
CC EIF2AK2 kinase activity. {ECO:0000250|UniProtKB:Q9H875,
CC ECO:0000269|PubMed:12679338}.
CC -!- SUBUNIT: Component of the pre-catalytic and post-catalytic spliceosome
CC complexes (By similarity). Interacts with EIF2AK2.
CC {ECO:0000250|UniProtKB:Q9H875, ECO:0000269|PubMed:12679338}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H875}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12679338}.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in liver,
CC kidney, brain and heart. {ECO:0000269|PubMed:12679338}.
CC -!- INDUCTION: By IL11. {ECO:0000269|PubMed:12679338}.
CC -!- SIMILARITY: Belongs to the PRKRIP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31212.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK010961; BAB27293.1; -; mRNA.
DR EMBL; AK088862; BAC40620.1; -; mRNA.
DR EMBL; AK018438; BAB31212.1; ALT_INIT; mRNA.
DR EMBL; AK046035; BAC32579.1; -; mRNA.
DR EMBL; AK010359; BAB26879.1; -; mRNA.
DR EMBL; BC027503; AAH27503.1; -; mRNA.
DR CCDS; CCDS19754.1; -.
DR RefSeq; NP_080050.1; NM_025774.3.
DR AlphaFoldDB; Q9CWV6; -.
DR SMR; Q9CWV6; -.
DR STRING; 10090.ENSMUSP00000120659; -.
DR PhosphoSitePlus; Q9CWV6; -.
DR EPD; Q9CWV6; -.
DR MaxQB; Q9CWV6; -.
DR PaxDb; Q9CWV6; -.
DR PeptideAtlas; Q9CWV6; -.
DR PRIDE; Q9CWV6; -.
DR ProteomicsDB; 289442; -.
DR Antibodypedia; 35198; 64 antibodies from 17 providers.
DR Ensembl; ENSMUST00000151786; ENSMUSP00000120659; ENSMUSG00000039737.
DR GeneID; 66801; -.
DR KEGG; mmu:66801; -.
DR UCSC; uc009aaf.1; mouse.
DR CTD; 79706; -.
DR MGI; MGI:1914051; Prkrip1.
DR VEuPathDB; HostDB:ENSMUSG00000039737; -.
DR eggNOG; KOG4055; Eukaryota.
DR GeneTree; ENSGT00390000005003; -.
DR HOGENOM; CLU_079129_2_0_1; -.
DR InParanoid; Q9CWV6; -.
DR OMA; EPSFIMG; -.
DR OrthoDB; 1545283at2759; -.
DR PhylomeDB; Q9CWV6; -.
DR TreeFam; TF314382; -.
DR BioGRID-ORCS; 66801; 18 hits in 71 CRISPR screens.
DR ChiTaRS; Prkrip1; mouse.
DR PRO; PR:Q9CWV6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CWV6; protein.
DR Bgee; ENSMUSG00000039737; Expressed in animal zygote and 243 other tissues.
DR ExpressionAtlas; Q9CWV6; baseline and differential.
DR Genevisible; Q9CWV6; MM.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IDA:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0003014; P:renal system process; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR009548; Prkrip1.
DR PANTHER; PTHR13507; PTHR13507; 1.
DR Pfam; PF06658; DUF1168; 1.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Spliceosome.
FT CHAIN 1..186
FT /note="PRKR-interacting protein 1"
FT /id="PRO_0000324788"
FT REGION 1..50
FT /note="Interaction with EIF2AK2"
FT /evidence="ECO:0000269|PubMed:12679338"
FT REGION 51..143
FT /note="Required for RNA-binding"
FT REGION 116..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..138
FT /note="Required for nuclear localization"
FT COILED 91..178
FT /evidence="ECO:0000255"
FT COMPBIAS 140..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1
FT /note="M -> L (in Ref. 2; BAB31212)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="A -> V (in Ref. 2; BAB31212)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="V -> L (in Ref. 2; BAB26879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 21492 MW; A37AD0B2D5834A2E CRC64;
MASPAAASVR PPRPKKEPQT LVIPKNAAEE QKLKLERLMK NPDKAVPIPE KMNEWAPRAP
PEFVRDVMGS SAGAGSGEFH VYRHLRRREY QRQDYMDAMA EKQKLDAEFQ KRLEKNKIAA
EEQTAKRRKK RQKLKEKKLL AKKMKLEQKK QKEEPSQCQE QHASSSDEAS ETEEEEEEPS
VVIMGR
