UBP36_DROER
ID UBP36_DROER Reviewed; 1085 AA.
AC B3NC86;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-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=GG15285;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954178; EDV51044.1; -; Genomic_DNA.
DR RefSeq; XP_001972018.2; XM_001971982.2.
DR AlphaFoldDB; B3NC86; -.
DR SMR; B3NC86; -.
DR STRING; 7220.FBpp0133831; -.
DR EnsemblMetazoa; FBtr0410345; FBpp0368780; FBgn0107537.
DR GeneID; 6544695; -.
DR KEGG; der:6544695; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_006208_0_0_1; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B3NC86; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000008711; Unassembled WGS sequence.
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..1085
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378496"
FT DOMAIN 173..481
FT /note="USP"
FT REGION 23..47
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 489..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1085
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 489..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..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1005
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 660
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 664
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 784
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 825
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 846
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1085 AA; 118856 MW; 5C90048688306DA6 CRC64;
MPVSMAVCET ANVVNAALRE SLGGNSSAAG SSADQAKSGE ESNGSLQNHI VANAKRILMA
KIEYEEVPNY HESVLESLKS 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 DIRKADTLED AFEGHFSRER LEDMGYKCEG
CKKKVSATKQ FSLERAPITL CIQLKRFSMI GNKLTKQISF KPRIDLSKYA ARSPAAQAQP
LTYRLVSMVT HLGVSQHCGH YTAIGSTDTG SYYNFDDSYV RPIAMQSVCN TNAYIMFYEL
DLSQTASPAA NRPNGMRLTN GHSTTPVPAT TVSSPSPTRF IGPQLPPGGV NGYSNGNAQK
TAIQFKQHHQ QSQQNGFQLG TGKFQDTAKP PLVGAHAKGE ANPAPTANGN KSSSTSSNNS
SSSNHKSINQ QQYLPISSED EDSEDERTSR PSTVQLPSMP KMTDDHTEKP KSPVKIQAKT
PIKTPLKSLV PYESASEEEE APLPNPRKRR SGEDSSESDQ ESGQTNGHSK TNGSLTNGSA
SSSVHVNNSK LKTDAIDEIF KSLKKSADSD DDDDEEESSI QLTNGWHPQK QSQSQSKAPP
SPKTPPSPAV IKSKTGIWKV TRNDEVDDID DDDDEEEEAT VKIQTPSKTH RNPFSSSKPS
TDSPATPGAK RQKLLNGSPV KSHQQPRVGN GYQSEATSNG STINELLKQS HRGYGSSVLS
WNGKPAELEK ETFELVCAKR IAGHGSVDGS DIVESSVAVN ASSGSDSNDV VVIAVALLVD
AREQRQRDLD DDEENEMDRG RQRKVKSGSA KGNNASNSTP GYNPFQEYEG QKRWNKNGGG
GGGFPRFYNQ NFRQNFQQRN KFKFNRFGGP GGAKFQQQRA LQRHLAAGGG FSRRQPSAQQ
QQQQS
