PUF3_SCHPO
ID PUF3_SCHPO Reviewed; 732 AA.
AC O94462;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=mRNA-binding protein puf3;
DE AltName: Full=Pumilio homology domain family member 3;
GN Name=puf3; ORFNames=SPAC1687.22c;
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 INDUCTION.
RX PubMed=12529438; DOI=10.1091/mbc.e02-08-0499;
RA Chen D., Toone W.M., Mata J., Lyne R., Burns G., Kivinen K., Brazma A.,
RA Jones N., Baehler J.;
RT "Global transcriptional responses of fission yeast to environmental
RT stress.";
RL Mol. Biol. Cell 14:214-229(2003).
RN [3]
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).
CC -!- FUNCTION: RNA-binding protein involved in post-transcriptional
CC regulation. Predominantly binds to mRNAs encoding mitochondrial
CC proteins and localizes them to the vicinity of mitochondria for
CC translation. Regulates mitochondrial biogenesis, motility and
CC morphology (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes
CC to multiple discrete foci in the cytoplasm. {ECO:0000250}.
CC -!- INDUCTION: By stress. {ECO:0000269|PubMed:12529438}.
CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the PUF3 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22616.2; -; Genomic_DNA.
DR RefSeq; NP_593141.2; NM_001018537.3.
DR AlphaFoldDB; O94462; -.
DR SMR; O94462; -.
DR BioGRID; 278767; 48.
DR STRING; 4896.SPAC1687.22c.1; -.
DR iPTMnet; O94462; -.
DR MaxQB; O94462; -.
DR PaxDb; O94462; -.
DR PRIDE; O94462; -.
DR EnsemblFungi; SPAC1687.22c.1; SPAC1687.22c.1:pep; SPAC1687.22c.
DR GeneID; 2542300; -.
DR KEGG; spo:SPAC1687.22c; -.
DR PomBase; SPAC1687.22c; puf3.
DR VEuPathDB; FungiDB:SPAC1687.22c; -.
DR eggNOG; KOG1488; Eukaryota.
DR HOGENOM; CLU_386441_0_0_1; -.
DR InParanoid; O94462; -.
DR OMA; HLIMSVE; -.
DR PhylomeDB; O94462; -.
DR PRO; PR:O94462; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; EXP:PomBase.
DR GO; GO:1905762; F:CCR4-NOT complex binding; IDA:PomBase.
DR GO; GO:0044692; F:exoribonuclease activator activity; IDA:PomBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:PomBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IBA:GO_Central.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..732
FT /note="mRNA-binding protein puf3"
FT /id="PRO_0000372691"
FT DOMAIN 376..716
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 396..431
FT /note="Pumilio 1"
FT REPEAT 432..468
FT /note="Pumilio 2"
FT REPEAT 469..504
FT /note="Pumilio 3"
FT REPEAT 505..540
FT /note="Pumilio 4"
FT REPEAT 541..576
FT /note="Pumilio 5"
FT REPEAT 577..611
FT /note="Pumilio 6"
FT REPEAT 612..647
FT /note="Pumilio 7"
FT REPEAT 655..690
FT /note="Pumilio 8"
FT REGION 98..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 81069 MW; 51E5636807FEEC1F CRC64;
MFTAVNSNPN ASESISGNSA FNFPSAPVSS LDTNNYGQRR PSLLSGTSPT SSFFNSSMIS
SNYTFPHGSN KQASLESPVS YSNPIPSLTW LSLDGDSPDS LVSTPTAPSA NHHGNPFPNG
KQSIKAMPSL VNLQEDSVIS KFPNSLEVPF RKRSESTSSS LSGLHSDLRP LKTELYGQLN
SECGARFPQT LKSPLTPIGG DSARTVSAST ARTSDKFFPR HTRAHSDFWI PATSKPSRHA
SHSSIGDLTT ITQSSISSGS GSFKPSWDGS FDSSLMAHQS YGTSPAFANG NSPTLKNDSS
FFGSASVRPT VSPIGTSFRQ SLPDISAFGI PKTETNPSEV VAPGTIPISV LPTSNFSAAT
PANPSLINQN GQEFLQQSRV LYLFHANKQR HFELSDILGN VVLFSTDQHG SRFIQQKLAT
ATEEEREAVF QEIASTSCLQ LMMDIFGNYV VQKYFEFGNE KQKQILLSQI KGHVFSLSLQ
MYGCRVVQKA IEYISPEHQV QLIQELDGHV LDCVCDQNGN HVIQKAIECI DTGHLQFILR
ALRPQIHVLS AHPYGCRVIQ RAIEHCHSER KLIIEELLPH ILKLTQDQYG NYVVQHILRT
GSESDKKYIF DLMIDHLLFL SCHKFASNVV ERCISYISDV DRRRILNKII SEKAENCSIL
MLMMKDKYAN YVIQKLLDAS PEEERDLLIS YIYPHISVLK KFTYGKHLIM SVERFRQKSI
SAVPKLASKE CK
