UBX3_YEAST
ID UBX3_YEAST Reviewed; 455 AA.
AC Q12229; D6VRQ7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=UBX domain-containing protein 3;
GN Name=UBX3; OrderedLocusNames=YDL091C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP INTERACTION WITH CDC48.
RX PubMed=15258615; DOI=10.1038/sj.embor.7400203;
RA Schuberth C., Richly H., Rumpf S., Buchberger A.;
RT "Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent
RT protein degradation.";
RL EMBO Rep. 5:818-824(2004).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE DSC E3 UBIQUITIN LIGASE COMPLEX.
RX PubMed=25078903; DOI=10.1074/mcp.m114.040774;
RA Tong Z., Kim M.S., Pandey A., Espenshade P.J.;
RT "Identification of candidate substrates for the Golgi Tul1 E3 ligase using
RT quantitative diGly proteomics in yeast.";
RL Mol. Cell. Proteomics 13:2871-2882(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=29355480; DOI=10.7554/elife.33116;
RA Yang X., Arines F.M., Zhang W., Li M.;
RT "Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome
RT system.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Component of the DSC E3 ubiquitin ligase complexes that tag
CC proteins present in Golgi, endosome and vacuole membranes and function
CC in protein homeostasis under non-stress conditions and support a role
CC in protein quality control (PubMed:25078903, PubMed:29355480). Involved
CC in CDC48-dependent protein degradation through the ubiquitin/proteasome
CC pathway. Involved in delivery of substrates to the 26S proteasome. Also
CC required for membrane fusion (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:25078903, ECO:0000269|PubMed:29355480}.
CC -!- SUBUNIT: Component of the DSC E3 ligase complexes composed of at least
CC TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized
CC complex or GLD1 for the Golgi/endosome-localized complex
CC (PubMed:29355480). Interacts with CDC48 (PubMed:15258615).
CC {ECO:0000269|PubMed:15258615, ECO:0000269|PubMed:29355480}.
CC -!- INTERACTION:
CC Q12229; P25694: CDC48; NbExp=3; IntAct=EBI-35335, EBI-4308;
CC Q12229; Q08232: DSC2; NbExp=6; IntAct=EBI-35335, EBI-32978;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 233 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X95644; CAA64920.1; -; Genomic_DNA.
DR EMBL; Z74139; CAA98657.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11767.1; -; Genomic_DNA.
DR PIR; S67627; S67627.
DR RefSeq; NP_010192.1; NM_001180150.1.
DR AlphaFoldDB; Q12229; -.
DR SMR; Q12229; -.
DR BioGRID; 31969; 136.
DR ComplexPortal; CPX-1190; TUL1 E3 ubiquitin ligase complex.
DR DIP; DIP-5024N; -.
DR IntAct; Q12229; 6.
DR MINT; Q12229; -.
DR STRING; 4932.YDL091C; -.
DR iPTMnet; Q12229; -.
DR MaxQB; Q12229; -.
DR PaxDb; Q12229; -.
DR PRIDE; Q12229; -.
DR EnsemblFungi; YDL091C_mRNA; YDL091C; YDL091C.
DR GeneID; 851467; -.
DR KEGG; sce:YDL091C; -.
DR SGD; S000002249; UBX3.
DR VEuPathDB; FungiDB:YDL091C; -.
DR eggNOG; KOG1363; Eukaryota.
DR GeneTree; ENSGT00940000154831; -.
DR HOGENOM; CLU_020031_0_0_1; -.
DR InParanoid; Q12229; -.
DR OMA; FFQGSYT; -.
DR BioCyc; YEAST:G3O-29498-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR PRO; PR:Q12229; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12229; protein.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0030276; F:clathrin binding; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:SGD.
DR GO; GO:0033523; P:histone H2B ubiquitination; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..455
FT /note="UBX domain-containing protein 3"
FT /id="PRO_0000211000"
FT DOMAIN 356..455
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 25..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 52943 MW; 7C565528A9C9D33E CRC64;
MDIFRHTFGN NDDSFIRIPG AFREEPPADL NGRTEDQNSN TNEPTQSRDG RLKSILHFLF
QAPLIVLYYL LNFIVRSSRL LKPLLRLHGF YQRKHNRLLD HSSQLHRLLE NLENEAQAVT
CSEGNGNNDD GSNTDSTSNN ESSGVQFSFG SLYNPENGTF SKSIMQNSYT ELLDACSEQV
KFGVIYLHDP LLDNHMDYVN KILCSEAFVN MIRKYQVLLW YGDVTTSEGL QVSNALKIRQ
YPLLGIISLK AEKKIELIAR VEGSISNYKA QDLEAIFSKN YSRLIQLRQQ RQNIEMQRLI
RQQQDSRYQD SLRRDQQRES ERLEQTQREQ MEREHQRIEN QWLLWRKSQL KPEPSSDKDA
SKVAIRLENG QRLVRKFDAS LPTEEIYAFV ELQLHDMLNS ENDTLPVYQP ANYQHQYSFK
LITPVPRREL DLSTKISDVS GIYPSGNIVM ERLDE
