UBP36_DROAN
ID UBP36_DROAN Reviewed; 1091 AA.
AC B3M3M6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GF23992;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902618; EDV40319.1; -; Genomic_DNA.
DR RefSeq; XP_001957513.2; XM_001957477.2.
DR AlphaFoldDB; B3M3M6; -.
DR SMR; B3M3M6; -.
DR STRING; 7217.FBpp0127184; -.
DR MEROPS; C19.097; -.
DR PRIDE; B3M3M6; -.
DR GeneID; 6506628; -.
DR KEGG; dan:6506628; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_006208_0_0_1; -.
DR InParanoid; B3M3M6; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B3M3M6; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000007801; 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; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1091
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378495"
FT DOMAIN 176..484
FT /note="USP"
FT REGION 115..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..821
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 443
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 663
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 786
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 829
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 850
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1091 AA; 119512 MW; E146651907DF1A24 CRC64;
MPVSVAVCET TNVVNAALRE SLGVGIGSGG ASSDDKSAGE DTNSLQNHIV ANAKRILMTK
IEYEEVPNYQ EAVLENLKSK YIVIKPTNPT NGCNLNGNTA NTFGNKNNAG KIVGANGHDN
NGRKLSDHPN QNHNHANPNG HHANPNELPK PKRVLYPREN IRIGWKQSER KWQVGSGMIN
AGNTCYLNST LQALFHIPAL ANWLVSEQAH MENCNVSESG SFCIICAMAK TLQATQTTQS
AVRPFLIYTK LKQICKHMIV GRQEDAHEFL RFLVEAMERA YLMRFRNYKE LDQLVKETTP
LGQIFGGYLR SEVRCLSCNH VSITFQHFQD LLLDIRKSDS LEEAFEGYFS REKLEDFGYK
CEGCKKKVSA TKQFRLERAP ITLCIQLKRF SMMGNKLTKQ ITFKPRIDLS KFAARSPAAS
VQPLIYRLVS MVTHLGVSQH CGHYTAIGST EAGSYYNFDD SYVRPIAIQS VCNTNAYIMF
YELDPLQTSS PAAARANGLR LTNGHGPVPV AVPATVSSPL PSPAKFIGPQ LPPGGINGYS
NGHGPKTTIQ FKPQHQPSHQ QNGVQQSAKS PLLSTHVKVE AAAGAAALAA SAAPTANGNK
SSSNHSNHKS VNQQHYLPIS SEDEDSEDEV KARPTVQLPS MPKMDDCMDS GKPKSPVKTP
VKTPLKSLVP YESASEEEEV VPLPNPNARK RSSDSSDSEH EPTTSSVQLN GHSKTNGSLS
NGSSKSTDAI DEIFKSLKGY QAKKKSADSE DDDDDEDEPN NQLTNGWHPQ KQSQSQSRSG
PPSPKTPPSP AVIKSKTGIW KVTRDDGDDD EDDDDDDDEV VEEARAVRTP VKNHRNPFAS
SKTATDSPTT PGAKRQKLLN GSAIKTQQQP RAGNGYQSEA TANGGTVNEL LKQSHRGYSS
SVLSWNGKPA ELEKEPFVLV CAKRIAGHGS LDGSGSGSNT DIIDTEIPAA AVNFPSGSCS
FSLLADARDQ RQRDLADDEE NEMDRGRQRK VKSGSAKISN STPGYNPFME FENQKRWHKN
GGGGGFPRFY QNQNFRQGFQ QRNKFKFNRF GGPGSAKFQQ QRALQRHLAA GGGFTRRQPT
HSAQQQQQQQ S
