RACK1_PIG
ID RACK1_PIG Reviewed; 317 AA.
AC P63246; P25388; P99049;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Receptor of activated protein C kinase 1;
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 Contains:
DE RecName: Full=Receptor of activated protein C kinase 1, N-terminally processed;
GN Name=RACK1; Synonyms=GNB2L1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=10673032; DOI=10.1016/s0167-4781(99)00213-4;
RA Chou Y.-C., Chou C.-C., Chen Y.-K., Tsai S., Hsieh F.M.J., Liu H.J.,
RA Hseu T.-H.;
RT "Structure and genomic organization of porcine RACK1 gene.";
RL Biochim. Biophys. Acta 1489:315-322(1999).
RN [2]
RP FUNCTION, AND INTERACTION WITH CHRM2.
RX PubMed=20976005; DOI=10.1371/journal.pone.0013517;
RA Reiner C.L., McCullar J.S., Kow R.L., Le J.H., Goodlett D.R.,
RA Nathanson N.M.;
RT "RACK1 associates with muscarinic receptors and regulates M(2) receptor
RT trafficking.";
RL PLoS ONE 5:E13517-E13517(2010).
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 (By similarity). Involved in the initiation of the ribosome
CC quality control (RQC), a pathway that takes place when a ribosome has
CC stalled during translation, by promoting ubiquitination of a subset of
CC 40S ribosomal subunits (By similarity). Binds to and stabilizes
CC activated protein kinase C (PKC), increasing PKC-mediated
CC phosphorylation. May recruit activated PKC to the ribosome, leading to
CC phosphorylation of EIF6. Inhibits the activity of SRC kinases including
CC SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase
CC of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and
CC inhibits transcriptional activity of the BMAL1-CLOCK heterodimer.
CC Facilitates ligand-independent nuclear translocation of AR following
CC PKC activation, represses AR transactivation activity and is required
CC for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin
CC signaling and promotes cell spreading and contact with the
CC extracellular matrix. Involved in PKC-dependent translocation of ADAM12
CC to the cell membrane. Promotes the ubiquitination and proteasome-
CC mediated degradation of proteins such as CLEC1B and HIF1A. Required for
CC VANGL2 membrane localization, inhibits Wnt signaling, and regulates
CC cellular polarization and oriented cell division during gastrulation.
CC Required for PTK2/FAK1 phosphorylation and dephosphorylation. Promotes
CC apoptosis by increasing oligomerization of BAX and disrupting the
CC interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6
CC channel activity. Regulates cell surface expression of some GPCRs such
CC as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration
CC (By similarity). Regulates internalization of the muscarinic receptor
CC CHRM2 (PubMed:20976005). Involved in the transport of ABCB4 from the
CC Golgi to the apical bile canalicular membrane (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P63244,
CC ECO:0000269|PubMed:20976005}.
CC -!- SUBUNIT: Monomer; also forms homodimers and homooligomersInteracts with
CC CPNE3 (By similarity). May interact with ABCB4 (By similarity).
CC Component of the small (40S) ribosomal subunit. Binds SLC9A3R1. Forms a
CC ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and
CC OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced
CC by tyrosine phosphorylation of RACK1. Recruited in a circadian manner
CC into a nuclear complex which also includes BMAL1 and PRKCA. Interacts
CC with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12.
CC Interacts with CLEC1B (via N-terminal region) and with HIF1A; the
CC interaction promotes their degradation. Interacts with RHOA; this
CC enhances RHOA activation and promotes cell migration. Interacts with
CC TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for
CC PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1.
CC Interacts with HRAS. Interacts with LARP4B. Interacts with PKD2L1 (By
CC similarity). Interacts with CHRM2; the interaction regulates CHRM2
CC internalization. {ECO:0000250, ECO:0000250|UniProtKB:P63244,
CC ECO:0000269|PubMed:20976005}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}.
CC Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane
CC through interaction with KRT1 which binds to membrane-bound ITGB1. Also
CC associated with the membrane in oncogene-transformed cells. 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 (By similarity). {ECO:0000250|UniProtKB:P63244,
CC ECO:0000250|UniProtKB:P68040}.
CC -!- TISSUE SPECIFICITY: Differentially expressed in various tissues, with
CC highest expression observed in thymus, pituitary, spleen and liver,
CC whereas there was no detectable expression in muscle.
CC {ECO:0000269|PubMed:10673032}.
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 ---------------------------------------------------------------------------
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; Z33879; CAA83944.1; -; mRNA.
DR EMBL; AF146043; AAD37978.1; -; Genomic_DNA.
DR PIR; S45054; S45054.
DR RefSeq; NP_999497.1; NM_214332.1.
DR PDB; 3J7P; EM; 3.50 A; Sg=1-317.
DR PDB; 3J7R; EM; 3.90 A; Sg=1-317.
DR PDBsum; 3J7P; -.
DR PDBsum; 3J7R; -.
DR AlphaFoldDB; P63246; -.
DR SMR; P63246; -.
DR IntAct; P63246; 2.
DR STRING; 9823.ENSSSCP00000023723; -.
DR PaxDb; P63246; -.
DR PeptideAtlas; P63246; -.
DR PRIDE; P63246; -.
DR Ensembl; ENSSSCT00000022602; ENSSSCP00000023723; ENSSSCG00000029724.
DR Ensembl; ENSSSCT00005065854; ENSSSCP00005040753; ENSSSCG00005041028.
DR Ensembl; ENSSSCT00015092717; ENSSSCP00015037908; ENSSSCG00015067931.
DR Ensembl; ENSSSCT00025084487; ENSSSCP00025036753; ENSSSCG00025061587.
DR Ensembl; ENSSSCT00030045369; ENSSSCP00030020404; ENSSSCG00030032752.
DR Ensembl; ENSSSCT00035105457; ENSSSCP00035045285; ENSSSCG00035076782.
DR Ensembl; ENSSSCT00040062588; ENSSSCP00040026390; ENSSSCG00040046413.
DR Ensembl; ENSSSCT00045009969; ENSSSCP00045006795; ENSSSCG00045005934.
DR Ensembl; ENSSSCT00050096955; ENSSSCP00050041781; ENSSSCG00050071078.
DR Ensembl; ENSSSCT00055043778; ENSSSCP00055034861; ENSSSCG00055022149.
DR Ensembl; ENSSSCT00060006171; ENSSSCP00060002097; ENSSSCG00060004937.
DR Ensembl; ENSSSCT00065082735; ENSSSCP00065036048; ENSSSCG00065060348.
DR Ensembl; ENSSSCT00070026581; ENSSSCP00070022091; ENSSSCG00070013602.
DR GeneID; 397605; -.
DR KEGG; ssc:397605; -.
DR CTD; 10399; -.
DR VGNC; VGNC:100848; RACK1.
DR eggNOG; KOG0279; Eukaryota.
DR GeneTree; ENSGT00940000154461; -.
DR InParanoid; P63246; -.
DR OMA; CKAMLWD; -.
DR OrthoDB; 805365at2759; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000029724; Expressed in blood and 46 other tissues.
DR ExpressionAtlas; P63246; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:1990630; C:IRE1-RACK1-PP2A complex; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IEA:InterPro.
DR GO; GO:0051434; F:BH3 domain binding; IEA:Ensembl.
DR GO; GO:0030332; F:cyclin binding; IEA:Ensembl.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
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:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
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: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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 Gastrulation; Growth regulation; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Translation regulation; WD repeat.
FT CHAIN 1..317
FT /note="Receptor of activated protein C kinase 1"
FT /id="PRO_0000127733"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT CHAIN 2..317
FT /note="Receptor of activated protein C kinase 1, N-
FT terminally processed"
FT /id="PRO_0000424483"
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:0000250|UniProtKB:P63244"
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:0000250|UniProtKB:P63244"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68040"
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:0000250|UniProtKB:P68040"
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
