UBP36_DROMO
ID UBP36_DROMO Reviewed; 1185 AA.
AC B4KXJ5;
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=GI13361;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933809; EDW18681.1; -; Genomic_DNA.
DR RefSeq; XP_002008205.2; XM_002008169.2.
DR AlphaFoldDB; B4KXJ5; -.
DR SMR; B4KXJ5; -.
DR STRING; 7230.FBpp0162578; -.
DR GeneID; 6582504; -.
DR KEGG; dmo:Dmoj_GI13361; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_006208_0_0_1; -.
DR InParanoid; B4KXJ5; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B4KXJ5; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000009192; 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..1185
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378499"
FT DOMAIN 199..509
FT /note="USP"
FT REGION 126..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..920
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 716
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 870
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1185 AA; 128969 MW; E42B490B122CB5A1 CRC64;
MPVSLAVCET ANVVNAALRE SLGGGGGSGC VAAAAASGRS GSGSSSTAAA AASADEAKIG
DPSATDNLQS QIVANAKRVL LAKIEYEEVE NYHESVLAKL KSKYIVIKPD NSGAANCSYK
TNGASTGKAL SSNGHDNTNG VNGSSAATVN GNRKQTVEQS NQNSTTNPNE LPKPKRVLYP
RENIRIGWKQ SDRKWQVGAG MLNVGNTCYL NSTLQALFHI PALANWLVSE TAHVENCNIS
ESCGSGGCII CAMAKTLQTT QSNQTAVRPF LIYTKLRQIC KHMVVGRQED AHEFLRFLVE
AMEKAYLMRF RNYKELDQLV KETTPLSQIF GGYLRSEVRC LSCNHVSITF QHFQDLLLDI
RKADTLEEAF DGYFSRERLE DMGYKCEGCK KKVSATKQFS LERAPITLCI QLKRFSMMGN
KLTKQISFKP RIDLSRFAAR SPAASTQPLS YRLVSMVTHL GVSQHCGHYT AIGLTESGSY
YNFDDSYVRP IAMQSVCNTN AYIMFYELDV ASSSINSSSS CSTSVPKLNG LRLNGQHSPS
VATTAVAATA TSTSASAVSP RFIGPQLPNG YANNNGHVLG AAKTSIQFKS SPQKQPQQQQ
HNGLLMGANK FQESAQSKHS LVGSLHKGET AANASANAIS NANSNKSSCN NNTLTTNSQH
QQQHILPISS DEEDEDEDSD DDVDVKANTA PQLPSMPKMF EDAESVAQTA KLKPKTPLKS
LVPYESASEE EQEQQQQQQQ LLVSPQLQPA NPRKRRSGAD SSESEDEPPS IMRNGHAKSN
GSGNESSTST SIKSNNNKQK TDAIDEIFKS LNNYKNKHRA TAAGTTTADA DEDEQQQQQV
TKKPSNSSSS LISKNGWQSQ NGKAPASPKT PPSPAVIKSK TGIWQITRTD DDNDDDDEDA
DEEDDADADA EQEEYDDEVV VVETTPSITT KNLNNPFASK PSSADAMPGA KRQKLLNGSA
KSAQTPRVGN GYQSEATANG NAVSELLKQT HRGYGTSVLS WTGKTSDLDK QSFDLVCAKR
IAGYGDMDGS VGVSSDSNIN NSKNIDSNSN IKSLTAPTLL AEAREQRKRD AEDDEENEMD
RGRQRKVKSA SVKSNNGIPG YNPFQEFESQ KRWNGNKSGS FPRFYQNYRQ NFQQRNKFKY
NRFGGGGAKF QQQRALQRHL AAGGGFTRRQ HQSTGHQQQQ QQQQS
