ID UP44A_XENLA Reviewed; 690 AA. AC Q6NTR6; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 44-A; DE EC=3.4.19.12; DE AltName: Full=Deubiquitinating enzyme 44-A; DE AltName: Full=Ubiquitin thioesterase 44-A; DE AltName: Full=Ubiquitin-specific-processing protease 44-A; GN Name=usp44-a; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (APR-2004) 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; BC068889; AAH68889.1; -; mRNA. DR RefSeq; NP_001084641.1; NM_001091172.1. DR AlphaFoldDB; Q6NTR6; -. DR DNASU; 414600; -. DR GeneID; 414600; -. DR KEGG; xla:414600; -. DR AGR; Xenbase:XB-GENE-1014118; -. DR CTD; 414600; -. DR Xenbase; XB-GENE-1014118; usp44.L. DR OrthoDB; 227085at2759; -. DR Proteomes; UP000186698; Chromosome 3L. DR Bgee; 414600; Expressed in blastula and 19 other cell types or tissues. 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:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR21646:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 1. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF57850; RING/U-box; 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..690 FT /note="Ubiquitin carboxyl-terminal hydrolase 44-A" FT /id="PRO_0000395813" FT DOMAIN 274..667 FT /note="USP" FT ZN_FING 2..99 FT /note="UBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT REGION 185..253 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 211..248 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 625 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 690 AA; 79011 MW; 77A3C98DB6F8E5BA CRC64; MDKCKHVGRL RLAQDHSILN PQKWHCVDCN TTESVWACLS CSHVACGRYI EEHALRHFQD SKHPLALEVN ELYVFCYLCD DYVLNDNTTG DLKLLRSTLS AIKSQNYDCT TRSGRTLRSM VTADDSFISH EGAQAFLQNE DRAFTALWHR RHALLGKVFR SWFALTPKGK QRLEEERLRE EAEQKREEAR KKRQQLKRKL KEEMESTSPR KSSRLQHQIQ PSPKTELPSV QKMNQKNSPT TKQKTPAPTS DKACFKKIGN SPIKRKPTVT PGVTGLRNLG NTCYMNSILQ ILSHLHVFRE CFLQLDLNQT QELLAAAGSG KTRLSSKYPP GAELPRVTQK HTKVQRSLAR RQSFSLGLSG GASNSRNMEL IQPKEPSSKH ISLCHELHTL FQVMWSGKWA LVSPFAMLHS VWRLIPAFRG YAQQDAQEFL CELLDKVQQE LETTGTRYPA LIPTSQRKLI KQVLNVVNNI FHGQLLSQVT CLVCDHKSNT IEPFWDLSLE FPERYHFNGK ETASQRPCLL TEMLAKFTET EALEGKIYAC DQCNKAQKQL MVCRLPQVLR LHLKRFRWSG RNHREKIGVH VRFDQMLNME PYCCRESTAA LRADCFIYDL SSVVMHHGKG FGSGHYTAFC YNPEGGFWVH CNDSKLHSCT VEEVCKAQAY ILFYTQRVTQ ENGHLSDTLP VHGSPQSPPR //