ZRN1B_DANRE
ID ZRN1B_DANRE Reviewed; 716 AA.
AC A0JMQ9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ubiquitin thioesterase zranb1-B {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9UGI0};
DE AltName: Full=Zinc finger Ran-binding domain-containing protein 1-B;
GN Name=zranb1b; Synonyms=zranb1; ORFNames=zgc:154177;
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].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-
CC 29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also
CC cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency
CC compared to 'Lys-29'-linked ones (By similarity). Positive regulator of
CC the Wnt signaling pathway that deubiquitinates apc protein, a negative
CC regulator of Wnt-mediated transcription (By similarity). Acts as a
CC regulator of autophagy by mediating deubiquitination of pik3c3/vps34,
CC thereby promoting autophagosome maturation (By similarity). Plays a
CC role in the regulation of cell morphology and cytoskeletal organization
CC (By similarity). Required in the stress fiber dynamics and cell
CC migration (By similarity). {ECO:0000250|UniProtKB:Q9UGI0}.
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; Evidence={ECO:0000250|UniProtKB:Q9UGI0};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization
CC in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}.
CC -!- DOMAIN: The RanBP2-type zinc fingers, also called NZFs, mediate the
CC interaction with ubiquitin and determine linkage specificity. RanBP2-
CC type zinc fingers 1 and 2 (also named NZF1 and NZF2) specifically
CC recognize and bind 'Lys-29'- and 'Lys-33'-linked ubiquitin. RanBP2-type
CC zinc finger 3 (also named NZF3) binds 'Lys-33'-linked ubiquitin and
CC shows weak binding to 'Lys-6'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin
CC chains but it does not interact with 'Lys-29'-linked chains.
CC {ECO:0000250|UniProtKB:Q9UGI0}.
CC -!- DOMAIN: The OTU domain mediates the deubiquitinating activity.
CC {ECO:0000250|UniProtKB:Q9UGI0}.
CC -!- DOMAIN: The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts
CC with ubiquitin hydrophobic patch and contributes to linkage
CC specificity. {ECO:0000250|UniProtKB:Q9UGI0}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
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DR EMBL; BC125972; AAI25973.1; -; mRNA.
DR RefSeq; NP_001071236.1; NM_001077768.1.
DR RefSeq; XP_005158652.1; XM_005158595.3.
DR AlphaFoldDB; A0JMQ9; -.
DR SMR; A0JMQ9; -.
DR BioGRID; 607517; 3.
DR STRING; 7955.ENSDARP00000086546; -.
DR MEROPS; C64.004; -.
DR PaxDb; A0JMQ9; -.
DR Ensembl; ENSDART00000092113; ENSDARP00000086546; ENSDARG00000063190.
DR GeneID; 777720; -.
DR KEGG; dre:777720; -.
DR CTD; 777720; -.
DR ZFIN; ZDB-GENE-061110-94; zranb1b.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158045; -.
DR HOGENOM; CLU_013907_0_0_1; -.
DR InParanoid; A0JMQ9; -.
DR OMA; CTYKNWP; -.
DR OrthoDB; 728724at2759; -.
DR PhylomeDB; A0JMQ9; -.
DR TreeFam; TF323312; -.
DR Reactome; R-DRE-5689896; Ovarian tumor domain proteases.
DR PRO; PR:A0JMQ9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000063190; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IGI:ZFIN.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0021551; P:central nervous system morphogenesis; IMP:ZFIN.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0035523; P:protein K29-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:1990168; P:protein K33-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF18418; AnkUBD; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF90209; SSF90209; 2.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protease;
KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..716
FT /note="Ubiquitin thioesterase zranb1-B"
FT /id="PRO_0000361555"
FT REPEAT 268..298
FT /note="ANK 1"
FT REPEAT 321..348
FT /note="ANK 2"
FT DOMAIN 440..600
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 3..33
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 82..111
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 152..181
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 113..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9UGI0"
FT ACT_SITE 593
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6GQQ9"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
SQ SEQUENCE 716 AA; 81193 MW; E18EB538F055BB75 CRC64;
MTDLGLKWSC EYCTYENWPS AIKCTMCRAQ RHNAPIITEE PFKSSSSLDP SLCTTQGGST
LLICPDSSAR PRVRIADELP ETSSKWSCHM CTYLNWPRAI RCTQCLSQRQ QGSQQHSPLS
PSETPQTSGS RPSPVTSDPC EEYNDRNRLN MHAQRWPCSA CTYENWPKSL RCVVCDHPKP
SGSPETPQQD SEAESATSPS IVNEQERENV RTAGGGGGGS RGRLRKLSPP MCKGQAEVKI
ELASGAVGSD NEQEADFKKL KQIRNRMRRS DWLFLNACAG VVEGDLAAVE AYKSSGGDIA
RQLTADEVRI LNRPSAFDAG FTLVHLAIRF QRQDMLAVLL TEVSQQTAKC IPALVCPELT
EQIRREVAAA LHRRKGEFPC YFFTDLVTFT LPADIEDLPP NVQEKLFDEV LDRDVQKELE
EESPIINWSL ELGTRLDSRL YALWNRTAGD CLLDSVLQAT WGIYDKDSVL RKSLNDSLHD
CSHWFYTRWK EWESWYSQSF GLHFSLREEQ WQEDWAFILS LASQPGASLE QTHVFVLAHI
LRRPIIVYGV KYYKSFRGET LGYTRFQGVY LPLLWEQSFC WKSPIALGYT RGHFSALVAM
ENDGYDNRGA GANLNTDDDV TVTFLPLVDS ERKLLHIHFL SAQEMGTEEQ QERMLRQWMD
CCVTEGGVLV AMQKSSRRRN HPLVTQMVEK WLDGYRQLAA CPTLSDGEEE EEDEDE
