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   24-JAN-2024, entry version 111.
DE   RecName: Full=Ubiquitin hydrolase B;
DE            EC=3.4.19.12;
GN   Name=ubpB; ORFNames=DDB_G0275021;
OS   Dictyostelium discoideum (Social amoeba).
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.O96612; -.
DR   MEROPS; C19.A68; -.
DR   PaxDb; 44689-DDB0191402; -.
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   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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02257; Peptidase_C19; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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
//