RACK1_MOUSE
ID RACK1_MOUSE Reviewed; 317 AA.
AC P68040; P25388; P99049; Q3THP0; Q3THY7; Q3TKQ0; Q3TW88; Q5NCC5; Q5NCC6;
AC Q9CSQ0; Q9ERM6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Receptor of activated protein C kinase 1;
DE AltName: Full=12-3;
DE AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1;
DE AltName: Full=Receptor for activated C kinase;
DE AltName: Full=Receptor of activated protein kinase C 1;
DE AltName: Full=p205;
DE Contains:
DE RecName: Full=Receptor of activated protein C kinase 1, N-terminally processed;
DE AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed;
GN Name=Rack1 {ECO:0000312|MGI:MGI:101849}; Synonyms=Gnb2-rs1, Gnb2l1;
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, AND TISSUE SPECIFICITY.
RX PubMed=7968370; DOI=10.1016/0169-328x(94)90144-9;
RA Imai Y., Suzuki Y., Tohyama M., Wanaka A., Takagi T.;
RT "Cloning and expression of a neural differentiation-associated gene, p205,
RT in the embryonal carcinoma cell line P19 and in the developing mouse.";
RL Brain Res. Mol. Brain Res. 24:313-319(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RA Raj N.B.K., Su Y., Au W.C., Pitha P.M.;
RT "Primary sequence of the mouse guanine nucleotide binding protein related
RT gene.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J;
RC TISSUE=Blastocyst, Embryo, Embryonic head, Embryonic spinal ganglion,
RC Embryonic stem cell, Head, Kidney, Mammary gland, and Osteoclast;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
RC STRAIN=129/SvJ;
RA Choi D., Messing R.O.;
RT "Genomic structure and expression of mouse receptor for activated C kinase
RT (RACK1).";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 2-11 AND 271-279, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA Kanor S., Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 226-317, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16414032; DOI=10.1016/j.brainres.2005.11.018;
RA Ashique A.M., Kharazia V., Yaka R., Phamluong K., Peterson A.S., Ron D.;
RT "Localization of the scaffolding protein RACK1 in the developing and adult
RT mouse brain.";
RL Brain Res. 1069:31-38(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH TRPM6.
RX PubMed=18258429; DOI=10.1016/j.cub.2007.12.058;
RA Cao G., Thebault S., van der Wijst J., van der Kemp A., Lasonder E.,
RA Bindels R.J., Hoenderop J.G.;
RT "RACK1 inhibits TRPM6 activity via phosphorylation of the fused alpha-
RT kinase domain.";
RL Curr. Biol. 18:168-176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, INTERACTION WITH BMAL1 AND PRKCA, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20093473; DOI=10.1126/science.1180067;
RA Robles M.S., Boyault C., Knutti D., Padmanabhan K., Weitz C.J.;
RT "Identification of RACK1 and protein kinase Calpha as integral components
RT of the mammalian circadian clock.";
RL Science 327:463-466(2010).
RN [14]
RP INTERACTION WITH VANGL2.
RX PubMed=21262816; DOI=10.1073/pnas.1013170108;
RA Li S., Esterberg R., Lachance V., Ren D., Radde-Gallwitz K., Chi F.,
RA Parent J.L., Fritz A., Chen P.;
RT "Rack1 is required for Vangl2 membrane localization and planar cell
RT polarity signaling while attenuating canonical Wnt activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2264-2269(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130 AND LYS-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Scaffolding protein involved in the recruitment, assembly
CC and/or regulation of a variety of signaling molecules. Interacts with a
CC wide variety of proteins and plays a role in many cellular processes.
CC Component of the 40S ribosomal subunit involved in translational
CC repression. Involved in the initiation of the ribosome quality control
CC (RQC), a pathway that takes place when a ribosome has stalled during
CC translation, by promoting ubiquitination of a subset of 40S ribosomal
CC subunits (By similarity). Binds to and stabilizes activated protein
CC kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit
CC activated PKC to the ribosome, leading to phosphorylation of EIF6.
CC Inhibits the activity of SRC kinases including SRC, LCK and YES1.
CC Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle.
CC Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional
CC activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent
CC nuclear translocation of AR following PKC activation, represses AR
CC transactivation activity and is required for phosphorylation of AR by
CC SRC. Modulates IGF1R-dependent integrin signaling and promotes cell
CC spreading and contact with the extracellular matrix. Involved in PKC-
CC dependent translocation of ADAM12 to the cell membrane. Promotes the
CC ubiquitination and proteasome-mediated degradation of proteins such as
CC CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits
CC Wnt signaling, and regulates cellular polarization and oriented cell
CC division during gastrulation. Required for PTK2/FAK1 phosphorylation
CC and dephosphorylation. Regulates internalization of the muscarinic
CC receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX
CC and disrupting the interaction of BAX with the anti-apoptotic factor
CC BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface
CC expression of some GPCRs such as TBXA2R. Plays a role in regulation of
CC FLT1-mediated cell migration. Involved in the transport of ABCB4 from
CC the Golgi to the apical bile canalicular membrane (By similarity).
CC {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:18258429,
CC ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:7968370}.
CC -!- SUBUNIT: Monomer; also forms homodimers and homooligomers (By
CC similarity). Interacts with CPNE3 (By similarity). May interact with
CC ABCB4 (By similarity). Component of the small (40S) ribosomal subunit.
CC Interacts with LARP4B. Interacts with LARP4. Interacts with PKD2L1 (By
CC similarity). Binds SLC9A3R1. Forms a ternary complex with TRIM63 and
CC PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via
CC SH2 domain); the interaction is enhanced by tyrosine phosphorylation of
CC RACK1. Recruited in a circadian manner into a nuclear complex which
CC also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R
CC but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-
CC terminal region) and with HIF1A; the interaction promotes their
CC degradation. Interacts with RHOA; this enhances RHOA activation and
CC promotes cell migration. Interacts with CHRM2; the interaction
CC regulates CHRM2 internalization. Interacts with TRPM6 (via kinase
CC domain). Interacts with PTK2/FAK1; required for PTK2/FAK1
CC phosphorylation and dephosphorylation. Interacts with FLT1. Interacts
CC with HRAS. {ECO:0000250, ECO:0000250|UniProtKB:P63244,
CC ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:20093473,
CC ECO:0000269|PubMed:21262816}.
CC -!- INTERACTION:
CC P68040; O88351: Ikbkb; NbExp=4; IntAct=EBI-296749, EBI-447960;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm
CC {ECO:0000269|PubMed:20093473}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000269|PubMed:20093473}.
CC Perikaryon {ECO:0000269|PubMed:16414032}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16414032}. Note=Recruited to the plasma membrane
CC through interaction with KRT1 which binds to membrane-bound ITGB1. PKC
CC activation induces translocation from the perinuclear region to the
CC cell periphery (By similarity). In the brain, detected mainly in cell
CC bodies and dendrites with little expression in axonal fibers or nuclei
CC (PubMed:16414032). {ECO:0000250|UniProtKB:P63244,
CC ECO:0000269|PubMed:16414032}.
CC -!- TISSUE SPECIFICITY: Strongly and ubiquitously expressed in the
CC embryonic and early postnatal brain. At 11.5 dpc, expressed in a high-
CC dorsal to low-ventral gradient throughout the brain. At 13.5 dpc, most
CC abundant in the telecephalon. At 18.5 dpc, expressed most abundantly in
CC layers 1-4 of the cortex, striatum, hippocampus, dentate gyrus, and
CC specific thalamic nuclei. This expression decreases during postnatal
CC development and is localized in the dentate gyrus, habenula, piriform
CC cortex, paraventricular nucleus of the hypothalamus and supraoptic
CC nucleus of the adult brain. {ECO:0000269|PubMed:16414032,
CC ECO:0000269|PubMed:7968370}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic brain development
CC with high levels detected at 11.5 dpc, 13.5 dpc and 18.5 dpc. Also
CC detected at high levels in the adult brain.
CC {ECO:0000269|PubMed:16414032}.
CC -!- DOMAIN: The 7 WD repeats mediate protein-protein interactions with
CC binding partners. {ECO:0000250|UniProtKB:P63244}.
CC -!- PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required
CC for binding to SRC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29506.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D29802; BAA06185.1; -; mRNA.
DR EMBL; X75313; CAA53062.1; -; mRNA.
DR EMBL; AK002493; BAB22141.1; -; mRNA.
DR EMBL; AK012242; BAB28114.1; -; mRNA.
DR EMBL; AK017772; BAB30920.1; -; mRNA.
DR EMBL; AK051226; BAC34564.1; -; mRNA.
DR EMBL; AK159797; BAE35378.1; -; mRNA.
DR EMBL; AK160528; BAE35846.1; -; mRNA.
DR EMBL; AK160739; BAE35980.1; -; mRNA.
DR EMBL; AK161234; BAE36257.1; -; mRNA.
DR EMBL; AK166417; BAE38762.1; -; mRNA.
DR EMBL; AK166786; BAE39017.1; -; mRNA.
DR EMBL; AK166800; BAE39028.1; -; mRNA.
DR EMBL; AK166889; BAE39095.1; -; mRNA.
DR EMBL; AK166945; BAE39133.1; -; mRNA.
DR EMBL; AK168086; BAE40059.1; -; mRNA.
DR EMBL; AK168096; BAE40068.1; -; mRNA.
DR EMBL; AK168196; BAE40156.1; -; mRNA.
DR EMBL; AK168349; BAE40286.1; -; mRNA.
DR EMBL; AL645849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466575; EDL33791.1; -; Genomic_DNA.
DR EMBL; BC046760; AAH46760.1; -; mRNA.
DR EMBL; AF295529; AAG29506.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS24585.1; -.
DR PIR; S38398; S38398.
DR RefSeq; NP_032169.1; NM_008143.3.
DR PDB; 7CPU; EM; 2.82 A; Sg=1-317.
DR PDB; 7CPV; EM; 3.03 A; Sg=1-317.
DR PDB; 7LS1; EM; 3.30 A; I3=1-317.
DR PDB; 7LS2; EM; 3.10 A; I3=1-317.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P68040; -.
DR SMR; P68040; -.
DR BioGRID; 199978; 102.
DR CORUM; P68040; -.
DR IntAct; P68040; 22.
DR MINT; P68040; -.
DR STRING; 10090.ENSMUSP00000020640; -.
DR iPTMnet; P68040; -.
DR PhosphoSitePlus; P68040; -.
DR SwissPalm; P68040; -.
DR REPRODUCTION-2DPAGE; P68040; -.
DR SWISS-2DPAGE; P68040; -.
DR EPD; P68040; -.
DR jPOST; P68040; -.
DR MaxQB; P68040; -.
DR PaxDb; P68040; -.
DR PeptideAtlas; P68040; -.
DR PRIDE; P68040; -.
DR ProteomicsDB; 300295; -.
DR TopDownProteomics; P68040; -.
DR Antibodypedia; 3802; 463 antibodies from 44 providers.
DR DNASU; 14694; -.
DR Ensembl; ENSMUST00000020640; ENSMUSP00000020640; ENSMUSG00000020372.
DR GeneID; 14694; -.
DR KEGG; mmu:14694; -.
DR UCSC; uc007ipa.1; mouse.
DR CTD; 10399; -.
DR MGI; MGI:101849; Rack1.
DR VEuPathDB; HostDB:ENSMUSG00000020372; -.
DR eggNOG; KOG0279; Eukaryota.
DR GeneTree; ENSGT00940000154461; -.
DR HOGENOM; CLU_000288_57_7_1; -.
DR InParanoid; P68040; -.
DR OMA; CKAMLWD; -.
DR OrthoDB; 805365at2759; -.
DR PhylomeDB; P68040; -.
DR TreeFam; TF300600; -.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5626978; TNFR1-mediated ceramide production.
DR BioGRID-ORCS; 14694; 31 hits in 71 CRISPR screens.
DR ChiTaRS; Rack1; mouse.
DR PRO; PR:P68040; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P68040; protein.
DR Bgee; ENSMUSG00000020372; Expressed in epiblast (generic) and 70 other tissues.
DR Genevisible; P68040; MM.
DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:1990630; C:IRE1-RACK1-PP2A complex; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; ISO:MGI.
DR GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008200; F:ion channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
DR GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045223; Asc1/RACK1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19868; PTHR19868; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Biological rhythms; Cell cycle;
KW Cell membrane; Cell projection; Cytoplasm; Developmental protein;
KW Direct protein sequencing; Gastrulation; Growth regulation; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; Translation regulation; WD repeat.
FT CHAIN 1..317
FT /note="Receptor of activated protein C kinase 1"
FT /id="PRO_0000424482"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..317
FT /note="Receptor of activated protein C kinase 1, N-
FT terminally processed"
FT /id="PRO_0000127732"
FT REPEAT 13..44
FT /note="WD 1"
FT REPEAT 61..91
FT /note="WD 2"
FT REPEAT 103..133
FT /note="WD 3"
FT REPEAT 146..178
FT /note="WD 4"
FT REPEAT 190..220
FT /note="WD 5"
FT REPEAT 231..260
FT /note="WD 6"
FT REPEAT 281..311
FT /note="WD 7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Guanine nucleotide-binding
FT protein subunit beta-2-like 1, N-terminally processed"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 52
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 9
FT /note="G -> R (in Ref. 3; BAE40068/BAE40156)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="R -> Q (in Ref. 3; BAE40059/BAE40068/BAE40156)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="L -> P (in Ref. 3; BAE35378)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="I -> M (in Ref. 6; AAG29506)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="E -> A (in Ref. 1; BAA06185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35077 MW; 257F91E369ED2044 CRC64;
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR
GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI
VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA
NCKLKTNHIG HTGYLNTVTV SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC
FSPNRYWLCA ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA
GYTDNLVRVW QVTIGTR
