UBP33_XENTR
ID UBP33_XENTR Reviewed; 892 AA.
AC Q28CN3; B7ZU27; F7EIJ9;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 33;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 33;
DE AltName: Full=Ubiquitin thioesterase 33;
DE AltName: Full=Ubiquitin-specific-processing protease 33;
GN Name=usp33; ORFNames=TEgg041n23.1;
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 TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme involved in various processes such as
CC centrosome duplication, cellular migration and beta-2 adrenergic
CC receptor/ADRB2 recycling. Involved in regulation of centrosome
CC duplication by mediating deubiquitination of ccp110 in S and G2/M
CC phase, leading to stabilize ccp110 during the period which centrioles
CC duplicate and elongate. Involved in cell migration via its interaction
CC with intracellular domain of robo1, leading to regulate the Slit
CC signaling. Plays a role in commissural axon guidance cross the ventral
CC midline of the neural tube in a Slit-dependent manner, possibly by
CC mediating the deubiquitination of robo1. Acts as a regulator of G-
CC protein coupled receptor (GPCR) signaling by mediating the
CC deubiquitination of beta-arrestins (arrb1 and arrb2) and beta-2
CC adrenergic receptor (adrb2). Deubiquitinates dio2, thereby regulating
CC thyroid hormone regulation. Mediates deubiquitination of both 'Lys-
CC 48'- and 'Lys-63'-linked polyubiquitin chains (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: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}.
CC Note=Associates with centrosomes predominantly in S and G2 phases but
CC less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
CC -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does
CC not bind ubiquitin, probably because the conserved Arg in position 55
CC is replaced by a Glu residue (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR926290; CAJ82183.1; -; mRNA.
DR EMBL; AAMC01095352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01095353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC171081; AAI71081.1; -; mRNA.
DR RefSeq; NP_001016228.1; NM_001016228.2.
DR RefSeq; XP_012816527.1; XM_012961073.2.
DR AlphaFoldDB; Q28CN3; -.
DR STRING; 8364.ENSXETP00000028749; -.
DR MEROPS; C19.037; -.
DR PaxDb; Q28CN3; -.
DR Ensembl; ENSXETT00000028749; ENSXETP00000028749; ENSXETG00000013118.
DR GeneID; 548982; -.
DR KEGG; xtr:548982; -.
DR CTD; 23032; -.
DR Xenbase; XB-GENE-1016674; usp33.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_004896_0_0_1; -.
DR InParanoid; Q28CN3; -.
DR OrthoDB; 147564at2759; -.
DR PhylomeDB; Q28CN3; -.
DR TreeFam; TF352179; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Reactome; R-XTR-9010553; Regulation of expression of SLITs and ROBOs.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013118; Expressed in testis and 15 other tissues.
DR ExpressionAtlas; Q28CN3; baseline.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
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; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF143791; SSF143791; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 2.
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 Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..892
FT /note="Ubiquitin carboxyl-terminal hydrolase 33"
FT /id="PRO_0000390427"
FT DOMAIN 148..665
FT /note="USP"
FT DOMAIN 667..760
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 768..871
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT ZN_FING 6..109
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 268..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 623
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT CONFLICT 320
FT /note="S -> I (in Ref. 1; CAJ82183)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="K -> I (in Ref. 3; AAI71081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 892 AA; 100733 MW; 8605699C7AB5B8AC CRC64;
MSSLVCDCPH LESVGEVTKE ELIKKSHGSC QDCRVRGPNL WACLENGCSY VGCGESHVDH
STLHSQDTKH CLTVNLTTLR VWCYTCSKEV FLDRKLSTQP TSAKLQDSHT QESKMSSSLT
LKIPAAVVSE NLDIELEEED ELKTRGLTGL KNIGNTCYMN AALQALSNCP PLTHYFLDCG
GLARTDKKPA LCKSYQKLMS DIWHKNRPGF VIPTNLFQGI KSVNPTFRGY SQQDAQEFLR
CLMDVLHEEL KEQIVEVEED AQTGIVEENL DEDKSQSDND FHSCDSGSSS DHAESESRKL
SEELTESTML IHEDQKDVES CKTWQKEKKF SNNLNQNHFL QDFEKNIQST IEESECLKQE
TVKVQIQSKA ADFTAEVNMN DLPTSQTPLL NEGATTHLSS SPPKPGAVWT GHKKVPGLCP
AKKRKQKKYH SVIADIFDGT IVSSVQCLTC DRVSVTLETF QDLSLPIPGK EDLAKLHSSS
HQSSLVKAGS CGEAYAPQGW IAFFLEYFKS WFWGPTVTLQ DCLAAFFARD ELKGDNMYSC
EKCKKLRNGV KFCKVQKFPE ILCIHLKRFR HELMFSTKIG THVSFPLEGL DLQPFLAKDS
PSQIVTYDLL SVICHHGTAS SGHYIAYCRN NLNNLWYEFD DQSVTEVSEA TVQNAEAYVL
FYRKASEEAQ KERRRVSCLL NIMEPSLLQF YISRQWLNKF KTFAEPGPIS NNDFLCIHGG
VPPRKASFIE DLVVMLPQNI WDYLYSRYGG GPAVNHLYVC YTCQTEMEKI EKRRKMELET
FIRLNKAFQE EESPAVIYCI SMQWFREWEG FVKSKDSDPP GPIDNTKIAA AKCGHITLRQ
GADSGQISEE TWLFLQSIYG GGPEITLRQN VTLAESEGGH AEEKIDVETR NI
