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Receptor of activated protein C kinase 1 (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed]

 RACK1_BOVIN             Reviewed;         317 AA.
P63243; P25388; P99049; Q3T0R8;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 112.
RecName: Full=Receptor of activated protein C kinase 1;
AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1;
AltName: Full=Receptor for activated C kinase;
AltName: Full=Receptor of activated protein kinase C 1;
Contains:
RecName: Full=Receptor of activated protein C kinase 1, N-terminally processed;
Name=RACK1; Synonyms=GNB2L1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11099474; DOI=10.1096/fj.99-1038com;
Berns H., Humar R., Hengerer B., Kiefer F.N., Battegay E.J.;
"RACK1 is up-regulated in angiogenesis and human carcinomas.";
FASEB J. 14:2549-2558(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in the recruitment, assembly and/or regulation
of a variety of signaling molecules. Interacts with a wide variety
of proteins and plays a role in many cellular processes. Component
of the 40S ribosomal subunit involved in translational repression
(By similarity). Involved in the initiation of the ribosome
quality control (RQC), a pathway that takes place when a ribosome
has stalled during translation, by promoting ubiquitination of a
subset of 40S ribosomal subunits (By similarity). Binds to and
stabilizes activated protein kinase C (PKC), increasing PKC-
mediated phosphorylation. May recruit activated PKC to the
ribosome, leading to phosphorylation of EIF6. Inhibits the
activity of SRC kinases including SRC, LCK and YES1. Inhibits cell
growth by prolonging the G0/G1 phase of the cell cycle. Enhances
phosphorylation of BMAL1 by PRKCA and inhibits transcriptional
activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-
independent nuclear translocation of AR following PKC activation,
represses AR transactivation activity and is required for
phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin
signaling and promotes cell spreading and contact with the
extracellular matrix. Involved in PKC-dependent translocation of
ADAM12 to the cell membrane. Promotes the ubiquitination and
proteasome-mediated degradation of proteins such as CLEC1B and
HIF1A. Required for VANGL2 membrane localization, inhibits Wnt
signaling, and regulates cellular polarization and oriented cell
division during gastrulation. Required for PTK2/FAK1
phosphorylation and dephosphorylation. Regulates internalization
of the muscarinic receptor CHRM2. Promotes apoptosis by increasing
oligomerization of BAX and disrupting the interaction of BAX with
the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity.
Regulates cell surface expression of some GPCRs such as TBXA2R.
Plays a role in regulation of FLT1-mediated cell migration (By
similarity). Involved in the transport of ABCB4 from the Golgi to
the apical bile canalicular membrane (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P63244}.
-!- SUBUNIT: Interacts with CPNE3 (By similarity). May interact with
ABCB4 (By similarity). Component of the small (40S) ribosomal
subunit. Exists as a monomer and also forms oligomers. Binds
SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts
with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain);
the interaction is enhanced by tyrosine phosphorylation of RACK1.
Recruited in a circadian manner into a nuclear complex which also
includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R
but not with INSR. Interacts with ADAM12. Interacts with CLEC1B
(via N-terminal region) and with HIF1A; the interaction promotes
their degradation. Interacts with RHOA; this enhances RHOA
activation and promotes cell migration. Interacts with CHRM2; the
interaction regulates CHRM2 internalization. Interacts with TRPM6
(via kinase domain). Interacts with PTK2/FAK1; required for
PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with
FLT1. Interacts with HRAS. Interacts with LARP4B. Interacts with
LARP4. Interacts with PKD2L1 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P63244}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P63244}. Cytoplasm
{ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P63244}. Nucleus
{ECO:0000250|UniProtKB:P63244}. Perikaryon
{ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma
membrane through interaction with KRT1 which binds to membrane-
bound ITGB1. Also associated with the membrane in oncogene-
transformed cells. PKC activation induces translocation from the
perinuclear region to the cell periphery (By similarity). In the
brain, detected mainly in cell bodies and dendrites with little
expression in axonal fibers or nuclei (By similarity).
{ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}.
-!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells (EC) and
the endothelium of tumor neovascularizations. Differential gene
expression is displayed in the corpora lutea of the early, mid,
and late stages of the ovarian cycle that are associated with
progressive, active, and regressive stages of angiogenesis.
{ECO:0000269|PubMed:11099474}.
-!- PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is
required for binding to SRC (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the WD repeat G protein beta family.
Ribosomal protein RACK1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ132860; CAB64792.1; -; mRNA.
EMBL; BC102286; AAI02287.2; -; mRNA.
RefSeq; NP_786996.1; NM_175802.3.
UniGene; Bt.2981; -.
ProteinModelPortal; P63243; -.
SMR; P63243; -.
STRING; 9913.ENSBTAP00000026183; -.
PaxDb; P63243; -.
PeptideAtlas; P63243; -.
PRIDE; P63243; -.
Ensembl; ENSBTAT00000026183; ENSBTAP00000026183; ENSBTAG00000019648.
GeneID; 327682; -.
KEGG; bta:327682; -.
CTD; 10399; -.
eggNOG; KOG0279; Eukaryota.
eggNOG; ENOG410XQGZ; LUCA.
GeneTree; ENSGT00890000139419; -.
HOGENOM; HOG000091643; -.
HOVERGEN; HBG000277; -.
InParanoid; P63243; -.
KO; K14753; -.
OMA; QYGYPKR; -.
OrthoDB; EOG091G0KZQ; -.
TreeFam; TF300600; -.
Reactome; R-BTA-5357905; Regulation of TNFR1 signaling.
Reactome; R-BTA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-BTA-5626978; TNFR1-mediated ceramide production.
Proteomes; UP000009136; Chromosome 7.
Bgee; ENSBTAG00000019648; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:1990630; C:IRE1-RACK1-PP2A complex; IEA:Ensembl.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISS:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IEA:Ensembl.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0043473; P:pigmentation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030822; P:positive regulation of cAMP catabolic process; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0032464; P:positive regulation of protein homooligomerization; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
2: Evidence at transcript level;
Acetylation; Apoptosis; Biological rhythms; Cell cycle; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Developmental protein;
Gastrulation; Growth regulation; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
Translation regulation; WD repeat.
CHAIN 1 317 Receptor of activated protein C kinase 1.
/FTId=PRO_0000127730.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P63244}.
CHAIN 2 317 Receptor of activated protein C kinase 1,
N-terminally processed.
/FTId=PRO_0000424479.
REPEAT 13 44 WD 1.
REPEAT 61 91 WD 2.
REPEAT 103 133 WD 3.
REPEAT 146 178 WD 4.
REPEAT 190 220 WD 5.
REPEAT 231 260 WD 6.
REPEAT 281 311 WD 7.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 2 2 N-acetylthreonine; in Guanine nucleotide-
binding protein subunit beta-2-like 1, N-
terminally processed.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 52 52 Phosphotyrosine; by ABL1. {ECO:0000250}.
MOD_RES 96 96 Phosphothreonine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 130 130 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 183 183 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68040}.
MOD_RES 228 228 Phosphotyrosine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000250|UniProtKB:P63244}.
MOD_RES 316 316 Phosphothreonine.
{ECO:0000250|UniProtKB:P68040}.
CONFLICT 91 91 D -> E (in Ref. 2; AAI02287).
{ECO:0000305}.
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


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