ID UBP36_DROVI Reviewed; 1214 AA.
AC B4LG38;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=GJ13192;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940647; EDW69346.1; -; Genomic_DNA.
DR RefSeq; XP_002047004.2; XM_002046968.2.
DR AlphaFoldDB; B4LG38; -.
DR SMR; B4LG38; -.
DR STRING; 7244.B4LG38; -.
DR GeneID; 6622549; -.
DR KEGG; dvi:6622549; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_006208_0_0_1; -.
DR InParanoid; B4LG38; -.
DR OMA; KRFSMMG; -.
DR OrthoDB; 227085at2759; -.
DR PhylomeDB; B4LG38; -.
DR ChiTaRS; scny; fly.
DR Proteomes; UP000008792; 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:K63-linked deubiquitinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin formation; 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:0070536; P:protein K63-linked deubiquitination; IEA:EnsemblMetazoa.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
DR CDD; cd02661; Peptidase_C19E; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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 PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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..1214
FT /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT /id="PRO_0000378503"
FT DOMAIN 192..502
FT /note="USP"
FT REGION 124..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..686
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..943
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 461
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 717
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 894
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 951
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1214 AA; 132000 MW; BC3028B949547093 CRC64;
MPVSLAVCET ANVVNAALRE SLGSGIGGGG GCVAAAASRS SAGSGSGSVA GVDEAKIGDV
SGTDNLQSQI VANAKRVLLA KIEYEEVENY HESVLAKLKS KYIVIKPDNN NGAANCNYKT
NGKAVGSNGH DNNTVNGGTV NGNRKQTVDS GQSNQNSSAN PNELPKPKRV LYPRENIRIG
WKQSERKWQV GAGMLNVGNT CYLNSTLQAL FHIPALANWL VSETSHVENC NISESCGSGG
CIICAMAKTL QTTQSNQSAV RPFLIYTKLR QICKHMVVGR QEDAHEFLRF LVEAMEKAYL
MRFRNFKELD QLVKETTPIS QIFGGYLRSE VRCLSCNHVS ITFQHFQDLL LDIRKADTLE
EAFDGYFSRE RLEDMGYKCE GCKKKVSATK QFSLERAPIT LCIQLKRFSM MGNKLTKQIS
FKPRIDLSRF AARSPTAAAQ PLSYRLVSMV THLGVSQHCG HYTAIGLTEA GSYYNFDDSY
VKPIAMQSVC NTNAYIMFYE LDVANSSSSS TINNNSSSSS NNSVAPKLNG LRLSNGAHSP
AAATVAVAAT ATSTSASAVS PRFIGPQLPN GYANSNGHAL GGAKTTIQFK TTPQKQLQQQ
QQQQNGLLMG ANKFQESSQS KHSLAGTLHK GEAAPNANTN ANANKSSCNN NITSQHQQQH
ILPISSDEDE DEDDSDDDDD DDDDDVKANT APQLPSMPKM FEDSESVAQT AKLKPKTPLK
SLVPYESASE EEQEQQQQQQ QQQLLQTPQQ LAANPRKRRS GSDSSESEEE APPPLPSILR
NGHAKTNGSV SNTSNSSHSK AKSASNASSA NVNSSKQKTD AIDEIFKSLN NYKNKHRIAA
DDDEDGDGDG DGHGNEQVQT EQGTKKLNSA SSASASKSNG WQSQNGKAPS SPKTPPSPAV
IKSKTGIWQI TRTNDDDDEE DEEEDDVEAD ADQEDDDDEV VVVEEPQVSV TPKNPKNPFA
ASKSAEANAT IAGAKRQKLL NGSAKSAATT RPGNGYQSES VANGSAVSEL LKQNHRGYGT
SVLSWNGKPS ELDKESFDLV CAKRIAGHGD TDVHSDVNSS SNNSSNINSN SNSNSNGNGK
RKNSTLLAEA REQRKRDAED EEENEMDRGR QRKVKSASVK SNNSTPGYNP FQEFENQKRW
HSNKSGTFPR FYHQNNRPNF QQRNKFKFNR FGGGAKFQQQ RALQRHLAAG GGFTRRQQQS
TGQQQQQQQQ QQQS
//
