UBP36_DROSE
ID UBP36_DROSE Reviewed; 1059 AA.
AC B4HUI5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=GM14719;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480817; EDW50606.1; -; Genomic_DNA.
DR RefSeq; XP_002035470.1; XM_002035434.1.
DR AlphaFoldDB; B4HUI5; -.
DR SMR; B4HUI5; -.
DR STRING; 7238.B4HUI5; -.
DR PRIDE; B4HUI5; -.
DR EnsemblMetazoa; FBtr0197704; FBpp0196196; FBgn0169640.
DR HOGENOM; CLU_006208_0_0_1; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B4HUI5; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000001292; 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..1059
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378501"
FT DOMAIN 168..457
FT /note="USP"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 416
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 636
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 756
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 799
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 820
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1059 AA; 115591 MW; EB4DAC63DA00063E CRC64;
MPVSMAVCET ANVVNAALRE SLGGNSSAGS STDQAKSGED TNGSLQNHIV ANAKRILMAK
IEYEEVPNYH ESVLENLKSK YIVIKPGNPG AINGFSGKNN TGKLVGANGH DNNGARKQAE
HPNNQSHHNH PHPTSNPNEL PKPKRVLYPR ENIRIGWKQS ERKWQVGTGM INVGNTCYLN
STLQALLHIP ALANWLVSEQ AHLADCNVAE PGSGCIICAM AKTLLATQSN QSAVRPFLIY
SKLKQICKHM VVGRQEDAHE FLRFLVEAME RAYLMRFRNY KELDQLVKET TPLGQIFGGY
LRSEVRCLSC NHVSITFQHF QDLLLDIRKA DSLEDAFEGH FSRERLEDMG YKCEGCKKKL
KRFSMIGNKL TKQISFKPRI DLSKYAARSP AAQAQPLTYR LVSMVTHLGA SQHCGHYTAI
GSTDTGSFYN FDDSYVRPIT MQNVCNTNAY IMFFELDLSQ AASPPANRPN GVRLTNGHST
TPVPAATVSS PSPTRFIGPQ LPPGGANGYT NGNAQKTAIQ FKQQNQQNGL QLGTGKFQDT
AKPPLVGAYA KGEATSAPTA NGNKSSSPSS NSSSNHKSIN QQQYLPISSD DEDIDDEMKP
GPTTAQLPSM PNMTEDNTEP KAKSPVKIHL KTPVKTPLKS LVPYESASEE EEAPLPNPRQ
SPGGEDFSES DQESGQTNGH SKTNGSLTNG SASSSVHVNN SKQKTDAIDE IFKSLKKSAD
SEEDDDEEEP SIQLTNGWHP QKQSQSQSKA PPSPKTPPSP AVIKSKTGIW KVTRKDEVDA
IDDDDDAVVV EGAPVKIPTP NKTHRNPFSS SKPSTDSPAT PGAKRQKLLN GSALKSHQQP
RVGNGYQSNV TSNGSTVNEL LKQSYRGYGA SVLSWNGKPA ELEKEPFELV CAKRIAGHGS
VEGSDIVEGS VAVDAAVTSS SNSNDVVVIA VALLVDAREQ RQRDLDDDEE NEMDRGRQRK
VKSGSAKGNN ASNSTPGYNP FQEYEGQKRW NKNGGGGGFS RFYNQNYRQN FQQRNKFKFN
RFGGAGSAKF QQQRALQRHL SAGGGFSRRQ PSAQQQQQT
