GBLP_SCHPO
ID GBLP_SCHPO Reviewed; 314 AA.
AC Q10281; P78896;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-like protein;
DE AltName: Full=Receptor of activated protein kinase C;
GN Name=rkp1; Synonyms=cpc2; ORFNames=SPAC6B12.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ED616;
RA Park S.-K., Yoo H.-S.;
RT "Molecular cloning and nucleotide sequence of Schizosaccharomyces pombe
RT homologue of the receptor for activated protein kinase C gene.";
RL J. Microbiol. 33:128-131(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ED616;
RX PubMed=11263963; DOI=10.1006/bbrc.2001.4535;
RA Won M., Park S.-K., Hoe K.-L., Jang Y.-J., Chung K.-S., Kim D.-U.,
RA Kim H.-B., Yoo H.-S.;
RT "Rkp1/Cpc2, a fission yeast RACK1 homolog, is involved in actin
RT cytoskeleton organization through protein kinase C, Pck2, signaling.";
RL Biochem. Biophys. Res. Commun. 282:10-15(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-314.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; SER-39; TYR-52; SER-148;
RP SER-242 AND SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May be a receptor for protein kinase C in the regulation of
CC actin cytoskeleton organization during cell wall synthesis and
CC morphogenesis. {ECO:0000269|PubMed:11263963}.
CC -!- SUBUNIT: Interacts with pck2.
CC -!- INTERACTION:
CC Q10281; O13370: ded1; NbExp=3; IntAct=EBI-696304, EBI-2478405;
CC Q10281; Q09702: nrd1; NbExp=4; IntAct=EBI-696304, EBI-696291;
CC Q10281; P79015: rpl3202; NbExp=2; IntAct=EBI-696304, EBI-7169357;
CC Q10281; Q09826: sds23; NbExp=3; IntAct=EBI-696304, EBI-7169035;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11263963}.
CC Note=Associated with particulate fractions.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000305}.
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DR EMBL; L37885; AAA56865.2; -; mRNA.
DR EMBL; AF320333; AAK38633.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11079.1; -; Genomic_DNA.
DR EMBL; D89247; BAA13908.1; -; mRNA.
DR PIR; T43158; T43158.
DR PIR; T43299; T43299.
DR RefSeq; NP_593770.1; NM_001019200.2.
DR AlphaFoldDB; Q10281; -.
DR SMR; Q10281; -.
DR BioGRID; 279723; 19.
DR IntAct; Q10281; 6.
DR MINT; Q10281; -.
DR STRING; 4896.SPAC6B12.15.1; -.
DR iPTMnet; Q10281; -.
DR MaxQB; Q10281; -.
DR PaxDb; Q10281; -.
DR PRIDE; Q10281; -.
DR EnsemblFungi; SPAC6B12.15.1; SPAC6B12.15.1:pep; SPAC6B12.15.
DR GeneID; 2543298; -.
DR KEGG; spo:SPAC6B12.15; -.
DR PomBase; SPAC6B12.15; -.
DR VEuPathDB; FungiDB:SPAC6B12.15; -.
DR eggNOG; KOG0279; Eukaryota.
DR HOGENOM; CLU_000288_57_7_1; -.
DR InParanoid; Q10281; -.
DR OMA; CKAMLWD; -.
DR PhylomeDB; Q10281; -.
DR PRO; PR:Q10281; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:PomBase.
DR GO; GO:0008494; F:translation activator activity; EXP:PomBase.
DR GO; GO:0140469; P:GCN2-mediated signaling; IMP:PomBase.
DR GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; IMP:PomBase.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISO:PomBase.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:PomBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:PomBase.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; IMP:PomBase.
DR GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IGI:PomBase.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
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 Membrane; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; WD repeat.
FT CHAIN 1..314
FT /note="Guanine nucleotide-binding protein subunit beta-like
FT protein"
FT /id="PRO_0000127757"
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 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 41
FT /note="I -> L (in Ref. 1; AAA56865 and 2; AAK38633)"
FT /evidence="ECO:0000305"
SQ 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
