UBP36_DROGR
ID UBP36_DROGR Reviewed; 1240 AA.
AC B4IXE0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=GH16215;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916366; EDV96377.1; -; Genomic_DNA.
DR RefSeq; XP_001984029.1; XM_001983993.1.
DR AlphaFoldDB; B4IXE0; -.
DR SMR; B4IXE0; -.
DR STRING; 7222.FBpp0150121; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_006208_0_0_1; -.
DR InParanoid; B4IXE0; -.
DR OMA; KRFSMMG; -.
DR PhylomeDB; B4IXE0; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000001070; 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..1240
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378497"
FT DOMAIN 202..512
FT /note="USP"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..941
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 471
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 715
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 898
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1240 AA; 134998 MW; D083740CBD133FF9 CRC64;
MPVSLAVCET TANVVNAALR ESLGSCVARA ALSADEAKTS NGGGDGSSTS GSSTDNLQSQ
IVANAKRVLL AKIDYEEVDN YHESVLAKLK SKYIVIKPDS NGGAASNGNG NYNGSNKTNG
KFGAGNGHDN NGNGNGIVNG GTSALNGGNN RKQIVVVDHQ SSNQHGSPSN PNELPKPKRV
LYQREHIRIG WKQSERKWQV GTGMLNVGNT CYLNSSLQAL FHIPSLANWL VSESAHLENC
NISESCGSNG CIICAMAKTL QSTQSNQSAV RPFLIYSKLR QICKHMVVGR QEDAHEFLRF
LIEAMEKAYL MRFRNYKELD QLVKETTPLN QIFGGYLRSE VRCLSCNHVS ITFQHFQDLL
LDIRKSDTLE DAFDGYFSRE RLEDMGYKCE GCKKKVSATK QFSLERAPIT LCIQLKRFSM
MGNKLTKQIS FKPRIDLSRF AARSPTAAAQ PLSYRLVSMV THLGVSQHCG HYTAIGLTET
GSYYNFDDSC VRPIAMQSVC NTNAYIMFYE LDVNGNGHVV APKMNGMRLT TNGGQQHSSP
VVATAPAAVV SATATSTSAS VSAAAVTSPR FIGPQLPNGY GNSNGHALGG GAAKTAIQFK
TTPQKHQQQQ QAQTQYQLNG HINGAAKFQT GAANANANKS SCNTLNNSKQ HQPQQQQQQP
QHILPISSDE EEDSDDDNDN DNVKTNKAPQ LPSMPKMFEE SSESVALTAK LKPKTALKSL
VPYESASEEE EQQQQQQQQT LQQQAATNSR KRRSGADSSD TDDDDDEEQQ QQQQQQPSLI
LRNGHAKTNG NLLNSSSSKT KSASNASSAN VNSSKQKTDA IDEIFKSLNN YKNKHRNDHN
HVDDDDDDDE DEDEDEDEAQ AQAEKKTVTK SSSSSSSTSL TNGWQQSQNG KATASPKTPP
SPAVIKTKTG IWQVTRNDED DDENVDGVAD ADDDDDNDEV AEPAVVTAKN HKNPFAAGKA
TATTDANPSA KRQKLLNGSS KSQQTTPRIG NGYQGESLPN GNAVVSELLK QNHRGYGSSV
LSWNGKASEL DKETFDLVCA KRIAGYGAAA ADEHCCDVNS GHSSNYGTNY KSLNNDMSSS
SSSSSSTNSS SNSSSRSNGN SSNCPPCDLL AEAREQRKRD DDDEEENEMD RGRQRKIKSA
SVKCGSGATA APPGYNPFQE YESQKRWHSN KSGSYSRFYH HPNYRSNFQQ RNKFKHNRFA
GGGGGAKFQQ QRALQRHLAS GGGFTRRQHH QSSGQQQQQS
