UBP36_DROSI
ID UBP36_DROSI Reviewed; 988 AA.
AC B4QIS3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 36;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 36;
DE AltName: Full=Protein scrawny;
DE AltName: Full=Ubiquitin thioesterase 36;
DE AltName: Full=Ubiquitin-specific-processing protease 36;
GN Name=Usp36; Synonyms=scny; ORFNames=GD13899;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Required for maintaining multiple types of adult stem cells,
CC including male and female germline, epithelial follicle cell and
CC intestinal stem cells. May function as a transcriptional repressor by
CC continually deubiquiting histone H2B at the promoters of genes critical
CC for cellular differentiation, thereby preventing histone H3 'Lys-4'
CC trimethylation (H3K4). Controls selective autophagy activation by
CC ubiquitinated proteins. {ECO:0000250|UniProtKB:Q9VRP5}.
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 atms/PAF1, but not with CycT. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; CM000363; EDX09348.1; -; Genomic_DNA.
DR AlphaFoldDB; B4QIS3; -.
DR SMR; B4QIS3; -.
DR STRING; 7240.B4QIS3; -.
DR EnsemblMetazoa; FBtr0356385; FBpp0320570; FBgn0185595.
DR HOGENOM; CLU_006208_0_0_1; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B4QIS3; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000000304; Chromosome 3l.
DR Bgee; FBgn0185595; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
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; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..988
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378502"
FT DOMAIN 78..386
FT /note="USP"
FT REGION 16..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 561
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 685
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 728
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 749
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 988 AA; 108676 MW; 2E0027E8315CE4CB CRC64;
MLHSLVPRYN KCVPFPTLRT DNNGARKQAE HPNNQSHHNH PHPTSNPNEL PKPKRVLYPR
ENIRIGWKQS ERKWQVGTGM INVGNTCYLN STLQALLHIP ALANWLVSEQ AHLADCNVAE
PGSGCIICAM AKTLLATQSN QSAVRPFLIY SKLKQICKHM VVGRQEDAHE FLRFLVEAME
RAYLMRFRNY KELDQLVKET TPLGQIFGGY LRSEVRCLSC NHVSITFQHF QDLLLDIRKA
DSLEDAFEGH FSRERLEDMG YKCEGCKKKV SATKQFSLER APITLCIQLK RFSMIGNKLT
KQISFKPRID LSKYAARSPA AQAQPLTYRL VSMVTHLGAS QHCGHYTAIG STDTGSFYNF
DDSYVRPITM QNVCNTNAYI MFFELDLSQA ASPPANRPNG VRLTNGHSTT PVPAATVSSP
SPTRFIGPQL PPVGANGYTN GNAQKTAIQF KQQNQQNGLQ LGTGKFQDTA KPPLVGAYAK
GEATSAPTAN GNKSSSPSSN SSSNHKSINQ QQYLPISSDD EDIDDEMKPG PTTAQLPSMP
NMTEDSTEPK AKSPVKIHLK TPVKTPLKSL VPYESASEEE EAPLPNPRQS TEGEDFSESD
QESGQTNGHS KTNGSLTNGS ASSSVHVNNS KQKTDAIDEI FKSLKKSADS EEDDDEEEPS
IQLTNGWHPQ KQSQSQSKAP PSPKTPPSPA VIKSKTGIWK VTRNDEVDAI DDDDDAVVVE
GAPVKIPTPN KTHRNPFSSS KPSTDSPATP GAKRQKLLNG SALKSHQQPR VGNGYQSNVT
SNGSTVNELL KQSYRGYGAS VLSWNGKPAE LEKEPFELVC AKRIAGHGSV EGSDIVEGSV
AVDAAVTSSS DSNDVVVIAV ALLVDAREQR QRDLDDDEEN EMDRGRQRKV KSGSAKGNNA
SNSTPGYNPF QEYEGQKRWN KNGGGGGFSR FHNQNYRQNF QQRNKFKFNR FGGQGSAKFQ
QQRALQRHLS AGGGFSRRQP SAQQQQQT
