UBP44_DANRE
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 03-AUG-2022, entry version 98.
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}.
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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; Q7ZUM8; -.
DR GeneID; 393227; -.
DR KEGG; dre:393227; -.
DR CTD; 84101; -.
DR ZFIN; ZDB-GENE-040426-774; usp44.
DR eggNOG; KOG1867; Eukaryota.
DR InParanoid; Q7ZUM8; -.
DR OrthoDB; 1230415at2759; -.
DR PhylomeDB; Q7ZUM8; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR PRO; PR:Q7ZUM8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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: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: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..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
