UBP44_XENTR
ID UBP44_XENTR Reviewed; 652 AA.
AC Q0V9G5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 44;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 44;
DE AltName: Full=Ubiquitin thioesterase 44;
DE AltName: Full=Ubiquitin-specific-processing protease 44;
GN Name=usp44;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinase that plays a key role in the spindle
CC checkpoint by preventing premature anaphase onset. Acts by specifically
CC mediating deubiquitination of cdc20, a negative regulator of the
CC anaphase promoting complex/cyclosome (APC/C) (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily.
CC {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; BC121579; AAI21580.1; -; mRNA.
DR RefSeq; NP_001072389.1; NM_001078921.1.
DR AlphaFoldDB; Q0V9G5; -.
DR STRING; 8364.ENSXETP00000020288; -.
DR PaxDb; Q0V9G5; -.
DR DNASU; 779843; -.
DR GeneID; 779843; -.
DR KEGG; xtr:779843; -.
DR CTD; 84101; -.
DR Xenbase; XB-GENE-1014112; usp44.
DR eggNOG; KOG1867; Eukaryota.
DR HOGENOM; CLU_008279_13_1_1; -.
DR InParanoid; Q0V9G5; -.
DR OrthoDB; 1230415at2759; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Hydrolase; Metal-binding; Mitosis; Nucleus;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..652
FT /note="Ubiquitin carboxyl-terminal hydrolase 44"
FT /id="PRO_0000395815"
FT DOMAIN 274..652
FT /note="USP"
FT ZN_FING 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 184..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 639
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
SQ SEQUENCE 652 AA; 74676 MW; A95E03024EA2AF44 CRC64;
MDKCKHVGRL RLAQDHSILN PQKWHCVDCN TTESVWACLS CSHVACGRYI EEHALRHFQD
SKHPLALEVN ELYVFCYLCD DYVLNDNTTG DLKLLRSTLS AIKSQNYDCT TRSGRTLRSM
VTADDSFISH EGAQAFLQNE DRAFTALWHR RHALLGKVFR SWFALTPKGK QRLEEERLRE
VAEQKREEAR KRRQQLKRKL KEEMESTPPR KSSRLKQQMQ PSPKTELPSV QKMNQKYTPT
TKQKPPAPTS IEVCLKKIGN SPIKRKPTVT PGVTGLRNLG NTCYMNSILQ ILSHLHVFRE
CFLQLDLNQT QELLAAAGSG KTRLSSKYPP SAVLPKVTQK HTKVQRSLAR RQSFSSGLSG
GASNSRNMEL IQPKEPSSKH ISLCHELHTL FQVMWSGKWA LVSPFAMLHS VWRLIPAFRG
YAQQDAQEFL CELLDKVQQE LETTGTRYPT LIPASQRKLI KQVLNIVNNI FHGQLLSQVT
CLACDHKSNT IEPFWDLSLE FPERYHFNGK ETASQRPCLL TEMLAKFTET EALEGKIYAC
DQCNTKRRKF SSKPVVLTEA QKQLMVCRLP QVLRLHLKRF RWSGRNHREK IGVHVRFDQM
LNMEPYCCRE STAALRADCF IYDLSSVVMH HGKGFGSGHY TAFCYNPEGG NG
