UBP36_DROYA
ID UBP36_DROYA Reviewed; 1082 AA.
AC B4PIW8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=GE21508;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000159; EDW93538.1; -; Genomic_DNA.
DR RefSeq; XP_002093826.2; XM_002093790.2.
DR AlphaFoldDB; B4PIW8; -.
DR SMR; B4PIW8; -.
DR STRING; 7245.FBpp0266518; -.
DR GeneID; 6533100; -.
DR KEGG; dya:Dyak_GE21508; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_006208_0_0_1; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B4PIW8; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000002282; Chromosome 3L.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:EnsemblMetazoa.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; IEA:EnsemblMetazoa.
DR GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IEA:EnsemblMetazoa.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:EnsemblMetazoa.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISS:UniProtKB.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:EnsemblMetazoa.
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; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1082
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378505"
FT DOMAIN 173..481
FT /note="USP"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 662
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 823
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1082 AA; 118583 MW; 047FCB6AD4F1BD81 CRC64;
MPVSMAVCET ANVVNAALRE SLGGNSSAAG SSIDQAKSGE DSNGSLQNHI VANAKRILMA
KIEYEEVPNY HESVLENLKS KYIVIKPGNP GAINGFGGKN NTGKVVGANG HDNNGARKQA
EHPNNQSHHN NHNNHPHPTS NPNELPKPKR VLYPRENIRI GWKQSERKWQ VGTGMINVGN
TCYLNSTLQA LLHIPALANW LVSEQAHLEN CNVAESGGGC IVCAMAKTLL ATQSNQSAVR
PFLIYSKLKQ ICKHMVVGRQ EDAHEFLRFL VEAMERAYLM RFRNYKELDQ LVKETTPLGQ
IFGGYLRSEV RCLSCNHVSI TFQHFQDLLL DIRKADSLED AFEGHFSRER LEDMGYKCEG
CKKKVSATKQ FSLERAPITL CIQLKRFSMI GNKLTKQISL KPRIDLSKYA ARSPAAQAQP
LTYRLVSMVT HLGVSQHCGH YTAIGSTDTG SYYNFDDSYV RPIAMQSVCN TNAYIMFYEL
DLSQAASPAA NRPNGVRLTN GHSTTPVPAA TVSSPSPTRF IGPQLPPGGV NGYSNGNAQK
TAIQFKQHHQ QSQQNGFQLG TGKFQDTAKP PLVGAHAKGD ANPVPTANGN KSSSTSSNSS
SNHKSINQQQ YLPISSEDED SEDEMTPRPT TAQLPSMPKM TDDHTEKPKS PVKIQVKTPV
KTPLKSLVPY ESASEEEEAP QPNPRKRRSE EDSSESDQES GQTNGHSKTN GSLTNGSASS
SVHVNNSKQK TDAIDEIFKS LKKSADSDDD DDEEESSIQL TNGWHPQKQS QSQSKAPPSP
KTPPSPAVIK SKTGIWKVTR NDEVDDIDDD DDEEDEAPAK IQTPSKTHRN PFSSTKPSTE
SPATPGAKRQ KLLNGSAVKS HQQPRVGNGY QSEATSNGST INELLKQSHR GYGSSVLSWN
GKPAELEKEP FELVCAKRIA GHGSVDGSDI VESSVAVNAS SGSDSNDVVV IALLVDAREQ
RQRDLDDDEE NEMDRGRQRK VKSSGSAKAN NASNSTPGYN PFQEYEGQKR WNKNGGGGGG
FPRFYNQNFR QNFQQRNKFK FNRFGGPGSA KFQQQRALQR HLAAGGGFSR RQPSAQQQQQ
QS
