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Guanine nucleotide-binding protein subunit beta-like protein (Receptor of activated protein kinase C)

 GBLP_SCHPO              Reviewed;         314 AA.
Q10281; P78896;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
29-AUG-2001, sequence version 3.
20-JUN-2018, entry version 148.
RecName: Full=Guanine nucleotide-binding protein subunit beta-like protein;
AltName: Full=Receptor of activated protein kinase C;
Name=rkp1; Synonyms=cpc2; ORFNames=SPAC6B12.15;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ED616;
Park S.-K., Yoo H.-S.;
"Molecular cloning and nucleotide sequence of Schizosaccharomyces
pombe homologue of the receptor for activated protein kinase C gene.";
J. Microbiol. 33:128-131(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ED616;
PubMed=11263963; DOI=10.1006/bbrc.2001.4535;
Won M., Park S.-K., Hoe K.-L., Jang Y.-J., Chung K.-S., Kim D.-U.,
Kim H.-B., Yoo H.-S.;
"Rkp1/Cpc2, a fission yeast RACK1 homolog, is involved in actin
cytoskeleton organization through protein kinase C, Pck2, signaling.";
Biochem. Biophys. Res. Commun. 282:10-15(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-314.
STRAIN=PR745;
PubMed=9501991; DOI=10.1093/dnares/4.6.363;
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe
cDNAs.";
DNA Res. 4:363-369(1997).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; SER-39; TYR-52;
SER-148; SER-242 AND SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: May be a receptor for protein kinase C in the regulation
of actin cytoskeleton organization during cell wall synthesis and
morphogenesis. {ECO:0000269|PubMed:11263963}.
-!- SUBUNIT: Interacts with pck2.
-!- INTERACTION:
O13370:ded1; NbExp=3; IntAct=EBI-696304, EBI-2478405;
Q09702:nrd1; NbExp=4; IntAct=EBI-696304, EBI-696291;
P79015:rpl3202; NbExp=2; IntAct=EBI-696304, EBI-7169357;
Q09826:sds23; NbExp=3; IntAct=EBI-696304, EBI-7169035;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11263963}.
Note=Associated with particulate fractions.
-!- SIMILARITY: Belongs to the WD repeat G protein beta family.
Ribosomal protein RACK1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L37885; AAA56865.2; -; mRNA.
EMBL; AF320333; AAK38633.1; -; Genomic_DNA.
EMBL; CU329670; CAB11079.1; -; Genomic_DNA.
EMBL; D89247; BAA13908.1; -; mRNA.
PIR; T43158; T43158.
PIR; T43299; T43299.
RefSeq; NP_593770.1; NM_001019200.2.
ProteinModelPortal; Q10281; -.
SMR; Q10281; -.
BioGrid; 279723; 13.
IntAct; Q10281; 6.
MINT; Q10281; -.
STRING; 4896.SPAC6B12.15.1; -.
iPTMnet; Q10281; -.
MaxQB; Q10281; -.
PaxDb; Q10281; -.
PRIDE; Q10281; -.
EnsemblFungi; SPAC6B12.15.1; SPAC6B12.15.1:pep; SPAC6B12.15.
GeneID; 2543298; -.
KEGG; spo:SPAC6B12.15; -.
EuPathDB; FungiDB:SPAC6B12.15; -.
PomBase; SPAC6B12.15; -.
HOGENOM; HOG000091643; -.
InParanoid; Q10281; -.
KO; K14753; -.
OMA; QYGYPKR; -.
OrthoDB; EOG092C10HM; -.
PhylomeDB; Q10281; -.
PRO; PR:Q10281; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
GO; GO:0005080; F:protein kinase C binding; IPI:PomBase.
GO; GO:0043022; F:ribosome binding; IDA:PomBase.
GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISO:PomBase.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IMP:PomBase.
GO; GO:0060733; P:regulation of eIF2 alpha phosphorylation by amino acid starvation; IMP:PomBase.
GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IGI:PomBase.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
GO; GO:0023052; P:signaling; NAS:PomBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
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.
1: Evidence at protein level;
Complete proteome; Membrane; Phosphoprotein; Reference proteome;
Repeat; Ribonucleoprotein; Ribosomal protein; WD repeat.
CHAIN 1 314 Guanine nucleotide-binding protein
subunit beta-like protein.
/FTId=PRO_0000127757.
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 10 10 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 52 52 Phosphotyrosine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
CONFLICT 41 41 I -> L (in Ref. 1; AAA56865 and 2;
AAK38633). {ECO:0000305}.
SEQUENCE 314 AA; 34851 MW; 4E14707164E68ACD CRC64;
MPEQLVLRAT LEGHSGWVTS LSTAPENPDI LLSGSRDKSI ILWNLVRDDV NYGVAQRRLT
GHSHFVSDCA LSFDSHYALS ASWDKTIRLW DLEKGECTHQ FVGHTSDVLS VSISPDNRQV
VSGSRDKTIK IWNIIGNCKY TITDGGHSDW VSCVRFSPNP DNLTFVSAGW DKAVKVWDLE
TFSLRTSHYG HTGYVSAVTI SPDGSLCASG GRDGTLMLWD LNESTHLYSL EAKANINALV
FSPNRYWLCA ATGSSIRIFD LETQEKVDEL TVDFVGVGKK SSEPECISLT WSPDGQTLFS
GWTDNLIRVW QVTK


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