ID   UBP36_DROWI             Reviewed;        1311 AA.
AC   B4MLR8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, 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=GK17299;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH963847; EDW72994.1; -; Genomic_DNA.
DR   RefSeq; XP_002062008.2; XM_002061972.2.
DR   AlphaFoldDB; B4MLR8; -.
DR   SMR; B4MLR8; -.
DR   STRING; 7260.B4MLR8; -.
DR   eggNOG; KOG1865; Eukaryota.
DR   HOGENOM; CLU_006208_0_0_1; -.
DR   OMA; KRFSMMG; -.
DR   PhylomeDB; B4MLR8; -.
DR   ChiTaRS; scny; fly.
DR   Proteomes; UP000007798; 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:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR   GO; GO:0016242; P:negative regulation of macroautophagy; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..1311
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT                   /id="PRO_0000378504"
FT   DOMAIN          212..533
FT                   /note="USP"
FT   REGION          120..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..857
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..882
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1021
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1202..1224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        221
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        492
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         767
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         789
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         982
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         985
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         988
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1047
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1050
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1311 AA;  141002 MW;  408909EBD862A2ED CRC64;
     MPVSLAVCET TTTTTANVVN AALRESLLGG SRSGAAVAGS GSASSLISGA GGAGASAAND
     DDSSSTATAN TNLQNQIVAS AKRVLLAKIE YEEVENYNDS VLDNLKTKYV VIKSPTPAAA
     AAATNNGNSN SAGSKILGAN GHDNRQKQQN ANGGCSTPTT TTTQTSSSST SSSSIEHNNN
     PNELPKPKRV LYQRENIRIG WKQSERKWQI GAGMINVGNT CYLNSTLQAL FHIPALANWL
     NSEQSHLENC NIGGESGGGG GGGGGNNGGF CIICAMAKTL QSTQSNASAI RPYHIYSKLK
     QICKHMVIGR QEDAHEFLRF LVEAMEKAYL MRYRNYKELD QLVKETTPLN QIFGGYLRSE
     VRCLSCNHVS ITFQHFQDLL LDIRKSDTLD EAFDGYFSRE RLEDMGYKCE GCKKKVSATK
     QFSLQRAPIT LCIQLKRFSM IGNKLTKQIS FKPRIDLSRF AARSPTAQGQ LPLTYRLVSL
     VTHLGVSQHC GHYTAIGLTE SGSYYNFDDS YVRPIAMQSV CSTNSYIMFY ELDLNQPLAT
     PANKLNGLRQ LSNGHHHHQQ QQQQHQQQQQ QQPTVVATIA SSPMATTRFI GPQLPPGGLN
     GYAMTTTTTA TNNTTNGHSQ KTAIQFKPQQ NGILTVGSGK FQESGQQKSP LVGTNHKNEA
     PAVAPNANAN ANGKSSSNPN TNTTINTNTN NGNSNNNNTN ATTANNSNKL NQQQQQYLPM
     SSSDEEDSDE EKMKRPTTTT PQLPSMPKMD GGGDEKPKTL TLTPTTTPTA STPTVSNPLK
     RLVPYESASE EEESSSGTPS SSTPTTTTTA AAAAASSPMQ ATAAATLPPP PTPTNARKRS
     LPDHHHHHPH HHVMVNGHGK SPKPASMPPA TNFNSSSSKQ KTDAIDEIFK SLNNFNKKRI
     NNKNQKHNEG DEEEDDEETL EKETNNSSRL VSSSTNTSPT TNGWKQSQIV SSSSSNSKNV
     STSAAAAAAT TSSSTSTSAP PSPKTPPSPA VINSKTGLWK VTRNLDDDDD EEEEDEDDEE
     HIAPTPPPVV AKTHKNPFSS QQKPTPSPST EAAPKRQKLF NGTSSSTPHV GNGYQSEPST
     PNGGGSGSGS NGCLNELLKQ SHRGYGSSSV LSWNGKQTEL DKEPFELVCA KRIAVDHGDH
     DDGGGGDDGG GVGVVTTTTT TTTTTKNTTK TLTADAQEQR QRDLDDDEEN EMDRGRQRKV
     KTATANGKSS GNSNNTTPGY NPFQEYESQK RWHNKSSNGP PRFYTQHASS SYRSNFHQRN
     KFKCNRGGNG GGGSGGISKF DHRHGLQRHL AAGGGFPRRP NANQQQQQQQ S
//