ID UBP44_DANRE Reviewed; 695 AA. AC Q7ZUM8; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 104. 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; ORFNames=zgc:55661; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=AB; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Deubiquitinase that plays a key role in the spindle assembly 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; BC048060; AAH48060.1; -; mRNA. DR RefSeq; NP_956551.1; NM_200257.1. DR AlphaFoldDB; Q7ZUM8; -. DR SMR; Q7ZUM8; -. DR STRING; 7955.ENSDARP00000104741; -. DR MEROPS; C19.057; -. DR PaxDb; 7955-ENSDARP00000104741; -. DR GeneID; 393227; -. DR KEGG; dre:393227; -. DR AGR; ZFIN:ZDB-GENE-040426-774; -. DR CTD; 84101; -. DR ZFIN; ZDB-GENE-040426-774; usp44. DR eggNOG; KOG1867; Eukaryota. DR InParanoid; Q7ZUM8; -. DR OrthoDB; 227085at2759; -. DR PhylomeDB; Q7ZUM8; -. DR Reactome; R-DRE-5689880; Ub-specific processing proteases. DR PRO; PR:Q7ZUM8; -. DR Proteomes; UP000000437; Chromosome 4. 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:0021551; P:central nervous system morphogenesis; IMP:ZFIN. DR GO; GO:1904888; P:cranial skeletal system development; IMP:ZFIN. 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..695 FT /note="Ubiquitin carboxyl-terminal hydrolase 44" FT /id="PRO_0000395812" FT DOMAIN 295..684 FT /note="USP" FT ZN_FING 2..99 FT /note="UBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT REGION 198..294 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 240..255 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 304 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT ACT_SITE 642 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 695 AA; 79926 MW; CEAE12134C67ED9F CRC64; MDRCKHVGRL RLAQDHSILN PQKWHCVDCN TTESVWACLS CSHVACGRYI EEHALQHFKE QHHPLALEVN ELYVYCYLCD DYVLNDNATG DLKLLRSTLS AIKSQCYEVT TRSGRTLRSS SANGDQLSPS TQELQLRDED RMFTALWHRR RALIGRLFRL WFAQTERGKK RLEEERQQEE EEERKREARE RRRQLKRQLK EELESAPPRK SHRIRRQSLK ATSVKPARAP AKSTKSVRRR SAPARVSTPT PRTPRERTPQ QRPRPQAKAK RPQAPPSKTG DSPVKRRPTV TPGVTGLRNL GNTCYMNSIL QVLSHLHVFR ECFLRLDLNQ ALELLASAVS RKLGLSAQRV IQPKGLNQGS GLSGGASRSR NMELIQPKEP SSKHISLCHE LHTLFPVMWS GKWALVSPFA MLHSVWQLIP AFRGYAQQDA QEFLCELLDK VQHELERTRT LTPATVPANQ RRLIKQVLSV VNTIFHGQLL SQVRCLACDH RSNTIEPFWD LSLEFPERYH SNSKDAAQVP CGLTEMLAKF TETEALEGAI YACDYCNNKR RRFCSKQVVL TEAQKQLMVH KLPHVLRLHL KRFRWSGRNH REKIGVHVQF EQELNMEPYC CKDSGNLPHP QHFLYQLSAV VMHHGKGFGS GHYTAFCYNT EGGFWVHCND SKLSVCAVEE VCKAQAYILF YTQRNAQDKS KESDL //