ID   UBP36_DROPS             Reviewed;        1059 AA.
AC   Q2LZB1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   24-JAN-2024, entry version 82.
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=GA18934;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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; CH379069; EAL29597.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LZB1; -.
DR   SMR; Q2LZB1; -.
DR   STRING; 46245.Q2LZB1; -.
DR   eggNOG; KOG1865; Eukaryota.
DR   HOGENOM; CLU_006208_0_0_1; -.
DR   InParanoid; Q2LZB1; -.
DR   OMA; KRFSMMG; -.
DR   ChiTaRS; scny; fly.
DR   Proteomes; UP000001819; Genome assembly.
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..1059
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 36"
FT                   /id="PRO_0000378500"
FT   DOMAIN          171..479
FT                   /note="USP"
FT   REGION          24..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..840
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..956
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..975
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..998
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1059
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        438
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         508
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         673
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         682
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         692
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         694
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         766
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         801
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         804
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         807
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         846
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         861
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1059 AA;  116372 MW;  A479D84A1DBFE65D CRC64;
     MPVSMAVCET ANVVNAALRE SLGVGNGSRA ADEAKKTGGG GGDDSDSEMH NQIAVSAYAK
     RILMSKIEYE EVPNYHDSVL EQLKNKYIVI KQPSNNNNSS SCNGSNFGNS KVVGANGHDN
     GNNGHRKLTQ SESTQSGPSP NELPKPKRVL YPRENIRIGW KQSERKWQVG TGMINVGNTC
     YLNSTLQALF HIPALANWLV SEQTHLENCN ITESNGGCII CAMAKTLQST QSCQSAMRPF
     HIYSKLKQIC KHMVVGRQED AHEFLRFLVE AMEKAYLMRF RNFKELDQLV KETTPLNQIF
     GGYLRSEVRC LSCSHVSITF QHFQDLLLDI RKSDTLEEAF DGYFSRERLE DMGYKCEGCK
     KKVSATKQFS LERAPITLCI QLKRFSMIGN KLTKTISFKP RIDLSRFAAR SPAAAAQPLT
     YRLVSMVTHL GVSQHCGHYT AIGMTESGSY YNFDDSYVRP IAMQSVCNTN AYIMFYELDL
     SQTTPLKSNG LRLTNGHSQV AVPATVSSSS PTHTRFIGPQ LPPGGINGYS NGHATGSSNA
     QKTAIQFKQQ QQHPQQNGLQ VGTGKFQEPP HAKSPLAGAY NKGEAFPATT ANGNKSSSSS
     ASNSNHNKSV NQLQHQQHYL PISSEDEDSE DGATATATAT ATARPTAQLP SMPKMTEDSS
     DKPKTPLKSS VKTNLVKSLL KTPLKSLVPY ESASEEDEPL PNPRKRRSDS DSNDSGDSDP
     QPGHVNGHTK TNGGSLTNGN GLGKAKTILA TSSSSSLASA SASAASDDED ADEEEENSKL
     TNGWQPQKQS QSLTQSKAPP SPKTPPSPAV IKSKTGIWKV TRNDDNEDED DDDDEDEEEQ
     HQVVSTPSKN PRNPFAKSST TPGAKRQKLL NGIAVKSQQQ PRVGNGYQSE ASTNGNVVNE
     LLKQTHRGYG SASVLSWSGK PAELEKELVA EAREQRQHDH DDEEENEMDR GRQRKVKSAT
     AKAYNSSTPG YNPFQEYESQ KRWHKSSNGG GSFPRYHNQN FRQNFQQRNK FKYNRFGGPG
     GAKFQQQRAL QRHLASGGVF NRRQPTGQQQ QQQSQQSSS
//