RACK1_BOVIN
ID RACK1_BOVIN Reviewed; 317 AA.
AC P63243; P25388; P99049; Q3T0R8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11099474; DOI=10.1096/fj.99-1038com;
RA Berns H., Humar R., Hengerer B., Kiefer F.N., Battegay E.J.;
RT "RACK1 is up-regulated in angiogenesis and human carcinomas.";
RL FASEB J. 14:2549-2558(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Regulates
CC internalization of the muscarinic receptor CHRM2. Promotes apoptosis by
CC increasing oligomerization of BAX and disrupting the interaction of BAX
CC with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity.
CC Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a
CC role in regulation of FLT1-mediated cell migration (By similarity).
CC Involved in the transport of ABCB4 from the Golgi to the apical bile
CC canalicular membrane (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P63244}.
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 Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE.
CC Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2
CC 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. Interacts with LARP4B. Interacts with LARP4. Interacts with
CC PKD2L1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63244}.
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: Expressed in aortic endothelial cells (EC) and the
CC endothelium of tumor neovascularizations. Differential gene expression
CC is displayed in the corpora lutea of the early, mid, and late stages of
CC the ovarian cycle that are associated with progressive, active, and
CC regressive stages of angiogenesis. {ECO:0000269|PubMed:11099474}.
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}.
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DR EMBL; AJ132860; CAB64792.1; -; mRNA.
DR EMBL; BC102286; AAI02287.2; -; mRNA.
DR RefSeq; NP_786996.1; NM_175802.3.
DR AlphaFoldDB; P63243; -.
DR SMR; P63243; -.
DR STRING; 9913.ENSBTAP00000026183; -.
DR PaxDb; P63243; -.
DR PeptideAtlas; P63243; -.
DR PRIDE; P63243; -.
DR Ensembl; ENSBTAT00000026183; ENSBTAP00000026183; ENSBTAG00000019648.
DR GeneID; 327682; -.
DR KEGG; bta:327682; -.
DR CTD; 10399; -.
DR VEuPathDB; HostDB:ENSBTAG00000019648; -.
DR VGNC; VGNC:33676; RACK1.
DR eggNOG; KOG0279; Eukaryota.
DR GeneTree; ENSGT00940000154461; -.
DR HOGENOM; CLU_000288_57_7_1; -.
DR InParanoid; P63243; -.
DR OMA; CKAMLWD; -.
DR OrthoDB; 805365at2759; -.
DR TreeFam; TF300600; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000019648; Expressed in theca cell and 106 other tissues.
DR ExpressionAtlas; P63243; 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 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Biological rhythms; Cell cycle; Cell membrane;
KW Cell projection; Cytoplasm; Developmental protein; Gastrulation;
KW Growth regulation; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; Ribosomal protein; Translation regulation;
KW WD repeat.
FT CHAIN 1..317
FT /note="Receptor of activated protein C kinase 1"
FT /id="PRO_0000127730"
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_0000424479"
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"
FT CONFLICT 91
FT /note="D -> E (in Ref. 2; AAI02287)"
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
