UBX3_SCHPO
ID UBX3_SCHPO Reviewed; 410 AA.
AC Q9UT81;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=UBX domain-containing protein 3;
DE AltName: Full=Meiotically up-regulated gene 39 protein;
GN Name=ubx3; Synonyms=mug39; ORFNames=SPAC343.09;
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 FUNCTION, AND INTERACTION WITH CDC48.
RX PubMed=15120077; DOI=10.1016/j.cub.2004.04.029;
RA Hartmann-Petersen R., Wallace M., Hofmann K., Koch G., Johnsen A.H.,
RA Hendil K.B., Gordon C.;
RT "The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and
RT nonproteolytic ubiquitin-dependent processes.";
RL Curr. Biol. 14:824-828(2004).
RN [3]
RP FUNCTION IN SPORULATION.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-167; SER-186 AND
RP THR-190, 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: Involved in CDC48-dependent protein degradation through the
CC ubiquitin/proteasome pathway. Involved in delivery of substrates to the
CC 26S proteasome. Also required for membrane fusion and sporulation.
CC {ECO:0000269|PubMed:15120077, ECO:0000269|PubMed:16303567}.
CC -!- SUBUNIT: Interacts with cdc48. {ECO:0000269|PubMed:15120077}.
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DR EMBL; CU329670; CAB52272.1; -; Genomic_DNA.
DR PIR; T38658; T38658.
DR RefSeq; NP_593429.1; NM_001018862.2.
DR AlphaFoldDB; Q9UT81; -.
DR SMR; Q9UT81; -.
DR BioGRID; 279601; 6.
DR IntAct; Q9UT81; 5.
DR STRING; 4896.SPAC343.09.1; -.
DR iPTMnet; Q9UT81; -.
DR MaxQB; Q9UT81; -.
DR PaxDb; Q9UT81; -.
DR PRIDE; Q9UT81; -.
DR EnsemblFungi; SPAC343.09.1; SPAC343.09.1:pep; SPAC343.09.
DR GeneID; 2543170; -.
DR KEGG; spo:SPAC343.09; -.
DR PomBase; SPAC343.09; ubx3.
DR VEuPathDB; FungiDB:SPAC343.09; -.
DR eggNOG; KOG2086; Eukaryota.
DR HOGENOM; CLU_029402_4_1_1; -.
DR InParanoid; Q9UT81; -.
DR OMA; EHQAFYA; -.
DR PhylomeDB; Q9UT81; -.
DR PRO; PR:Q9UT81; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0043130; F:ubiquitin binding; IDA:PomBase.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.210; -; 1.
DR InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00553; SEP; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF102848; SSF102848; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Meiosis; Phosphoprotein; Reference proteome; Sporulation;
KW Ubl conjugation pathway.
FT CHAIN 1..410
FT /note="UBX domain-containing protein 3"
FT /id="PRO_0000211006"
FT DOMAIN 211..276
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 334..410
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 46..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 410 AA; 44897 MW; FBA48696039DBDA0 CRC64;
MDREDILKEF CNRNNIDVSQ GRFFLESTNW NYELATALLH EVIPPEEDHG LQPSSDVSKV
PEVTGSSSGI SGGDQQPPRP LQRQQNTQGQ GMKSGTASKK FATLRDLEGN DESAEEKSHL
FTGGEKSGLS VEDGDPDPKK QLVRDILEKA RQHTISPLDE QDSGPSSLAS SWASVGQRLG
TENEASGSTT PVTQSGPPRE NPPTESQPEK PLRRTLYFWR NGFSVDDGPI YTYDDPANQE
MLRYINSGRA PLHLLGVSMN QPIDVVVQHR MDEDYVAPFK PFSGKGQRLG STYMQPRMSQ
MPGGLYTDTS TSSSVPINVK PNSTTPHASL QIDENKPTTR IQVRLSNGGR TVLTVNLSHT
LHDIYEAVRA VSPGNFILSV PFPAKTLEDD PSVTVEAASL KNASLVQKSL
