UBPB_DICDI
ID UBPB_DICDI Reviewed; 451 AA.
AC O96612; Q554A4; Q869X4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ubiquitin hydrolase B;
DE EC=3.4.19.12;
GN Name=ubpB; ORFNames=DDB_G0275021;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MKKA, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX3;
RX PubMed=9832508; DOI=10.1101/gad.12.22.3564;
RA Chung C.Y., Reddy T.B.K., Zhou K., Firtel R.A.;
RT "A novel, putative MEK kinase controls developmental timing and spatial
RT patterning in Dictyostelium and is regulated by ubiquitin-mediated protein
RT degradation.";
RL Genes Dev. 12:3564-3578(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Required for proper prespore cell patterning. Plays a role in
CC stabilizing mkkA by preventing it from being targeted for degradation.
CC ubcB and ubpB differentially control ubiquitination/deubiquitination
CC and degradation of mkkA in a cell-type-specific and temporally
CC regulated manner. {ECO:0000269|PubMed:9832508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SUBUNIT: Interacts with mkkA (via F-box/WD40 domains).
CC {ECO:0000269|PubMed:9832508}.
CC -!- DEVELOPMENTAL STAGE: Found at low levels in vegetative cells and at
CC higher levels during aggregation and mound formation (4 and 8 hours of
CC development). {ECO:0000269|PubMed:9832508}.
CC -!- DISRUPTION PHENOTYPE: Null cells differentiate into prestalk cells
CC preferentially. They develop precociously and exhibit abnormal cell-
CC type patterning with an increase in the prestalk domain and reduction
CC in the prespore domain in the slug, and spore domain in a fruiting
CC body. Null cells do not form the normal spherical sori seen in mature
CC wild-type fruiting bodies. Instead, the sori remain elongated, similar
CC to those seen in wild-type fruiting bodies that are not fully mature.
CC The upper and lower cups of the fruiting body, which are derived from
CC prestalk cells and anterior-like cells, are enlarged. The spore-
CC containing region is reduced. Null cells form fruiting bodies at
CC approximately 17 hours and exhibit precocious expression of the spore
CC marker. The expression levels of the prespore/spore markers are lower
CC in null cells compared to wild-type cells, whereas expression of the
CC prestalk/stalk marker is elevated slightly. The loss of gene function,
CC might lead to increased mkkA ubiquitination and a more rapid turnover
CC of mkkA. This should result in a reduced level of mkkA activity,
CC producing the above mentioned mkkA null cell type phenotype.
CC {ECO:0000269|PubMed:9832508}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF093690; AAC97115.1; -; mRNA.
DR EMBL; AAFI02000013; EAL69791.1; ALT_TERM; Genomic_DNA.
DR RefSeq; XP_643807.1; XM_638715.1.
DR AlphaFoldDB; O96612; -.
DR SMR; O96612; -.
DR STRING; 44689.DDB0191402; -.
DR MEROPS; C19.A68; -.
DR PaxDb; O96612; -.
DR PRIDE; O96612; -.
DR EnsemblProtists; EAL69791; EAL69791; DDB_G0275021.
DR GeneID; 8619853; -.
DR KEGG; ddi:DDB_G0275021; -.
DR dictyBase; DDB_G0275021; ubpB.
DR eggNOG; KOG1871; Eukaryota.
DR HOGENOM; CLU_008279_7_0_1; -.
DR InParanoid; O96612; -.
DR OMA; INTSNTC; -.
DR PhylomeDB; O96612; -.
DR Reactome; R-DDI-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR PRO; PR:O96612; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IDA:dictyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..451
FT /note="Ubiquitin hydrolase B"
FT /id="PRO_0000389021"
FT DOMAIN 19..450
FT /note="USP"
FT REGION 83..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 408
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 451 AA; 51134 MW; DADCD2CD07AFBFD7 CRC64;
MKNIEEMPSK SQLVAHRSRG LINTSNTCFM NVILQSLTGC QLFLRVIKNL SDLEDLGKYP
TLHSFNQFYT EYFSNPTSNI LNNNSNSTTT TSSSSTTATT TSTSNNNKSQ TPTSPIQQHH
QSQTNGLSNQ PSVATQSQQQ QQPQPPINPK HFNDLVKSFN SKVSPVPQTT VSPHSMVQVS
KKKLKLQLYN NSLPQTICQQ DAQEFLVFLL DLIHEEFLTL IKDIDIPKED DKSTPTSTSI
VDDNWEVVGK KGKTAIITNS QQELPKTPIS QIFSGVLRSS FNRTGSKESI TVEPFYCLHL
DIRPEEINSL EDALKFFMKP EIIEGYTCST KKIEISASKS WSFESLPRIL IVHFKRFAFE
SDTSKKLDKL IRFPTQLSLS TASNHQTQKK YSLFSVVSHH GRGLSQGHYT CDIYQPQQAQ
WIRYDDSTFT EVKEQDVLNR EAYLLLYQLV N
