PLP1_SCHPO
ID PLP1_SCHPO Reviewed; 279 AA.
AC O14095; Q8NIQ0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Thioredoxin domain-containing protein plp1;
DE AltName: Full=Phosducin-like protein 1;
GN Name=plp1; ORFNames=SPAC2F3.12c;
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 [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 [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-275, AND
RP 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: Inhibits early G-protein signaling events following pheromone
CC stimulation. May help create heterodimerizable beta-tubulin by
CC facilitating the efficient transfer of nascent beta-tubulin
CC polypeptides to the folding apparatus (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; CU329670; CAD43412.1; -; Genomic_DNA.
DR RefSeq; NP_001018268.1; NM_001019813.2.
DR AlphaFoldDB; O14095; -.
DR SMR; O14095; -.
DR BioGRID; 280506; 6.
DR STRING; 4896.SPAC2F3.12c.1; -.
DR iPTMnet; O14095; -.
DR MaxQB; O14095; -.
DR PaxDb; O14095; -.
DR PRIDE; O14095; -.
DR EnsemblFungi; SPAC2F3.12c.1; SPAC2F3.12c.1:pep; SPAC2F3.12c.
DR GeneID; 2541749; -.
DR PomBase; SPAC2F3.12c; plp1.
DR VEuPathDB; FungiDB:SPAC2F3.12c; -.
DR eggNOG; KOG1672; Eukaryota.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_072378_0_1_1; -.
DR InParanoid; O14095; -.
DR OMA; CHFFHRE; -.
DR PhylomeDB; O14095; -.
DR PRO; PR:O14095; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; ISO:PomBase.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Nucleus; Pheromone response; Phosphoprotein;
KW Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..279
FT /note="Thioredoxin domain-containing protein plp1"
FT /id="PRO_0000120171"
FT DOMAIN 137..248
FT /note="Thioredoxin"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 279 AA; 32190 MW; 6662C05898B5DB28 CRC64;
MTSFPASHGF GPRKRGYQMD LTNVQPVENK PAWISMKSPL EKEIANEYEA LKVTERKEDT
QDYNEPELHN SNDPTVDLYA DTYATQAATE SDSELEDALF SQLDEFDDTA YREQRLEMLK
KEFARVEAAK EKGHMQFLTV ENEREVMDFT LSSKKVVIHF YHPDFIRCKI IDSHLEKIAK
VHWETKFIRI EAANAPFLVV KLGLKVLPAV LCYVNSQLVD KIIGFADLGN KDDFETSLLE
FRLLKSSAID RLKEESSSNK SIYHDELQNN QSDDSDFFE
