UBP36_DROPS
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 03-AUG-2022, entry version 78.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379069; EAL29597.2; -; Genomic_DNA.
DR AlphaFoldDB; Q2LZB1; -.
DR SMR; Q2LZB1; -.
DR STRING; 7237.FBpp0274209; -.
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: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_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
