ZRAN1_XENTR
ID ZRAN1_XENTR Reviewed; 701 AA.
AC B1H2Q2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ubiquitin thioesterase zranb1 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9UGI0};
DE AltName: Full=Zinc finger Ran-binding domain-containing protein 1;
GN Name=zranb1;
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=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) 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; BC161086; AAI61086.1; -; mRNA.
DR RefSeq; NP_001116900.1; NM_001123428.1.
DR AlphaFoldDB; B1H2Q2; -.
DR SMR; B1H2Q2; -.
DR MEROPS; C64.004; -.
DR PaxDb; B1H2Q2; -.
DR GeneID; 100144659; -.
DR KEGG; xtr:100144659; -.
DR CTD; 54764; -.
DR Xenbase; XB-GENE-876399; zranb1.
DR eggNOG; KOG4345; Eukaryota.
DR InParanoid; B1H2Q2; -.
DR Reactome; R-XTR-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-XTR-5689896; Ovarian tumor domain proteases.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
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:0016477; P:cell migration; ISS:UniProtKB.
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; 2.
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..701
FT /note="Ubiquitin thioesterase zranb1"
FT /id="PRO_0000361558"
FT REPEAT 253..283
FT /note="ANK 1"
FT REPEAT 306..333
FT /note="ANK 2"
FT DOMAIN 425..585
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 79..108
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 143..173
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9UGI0"
FT ACT_SITE 578
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 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 99
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 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
SQ SEQUENCE 701 AA; 80037 MW; DD3A68A82AF3DADE CRC64;
MTEHGIKWAC EYCTYENWPS AIKCTMCRAP RPSGAIITEE PFKNSTPDVG SMERESGSPL
ICPDSSARPR VKSSYSMETS TKWSCHMCTY LNWPRAIRCT QCLSQRRTRS PTESPQSSGS
SLRAIPSPID PCEEYNDRNK LNIKGQHWTC SACTYENCAK AKKCVVCDHP TPNNMDAIEL
ANTDEASSII NEQDRARWRG GCSSSNSQRR SPPTSKRDSD MDFQRIELAG AVGSKEEFEL
DLKKLKQIKN RMRKTDWLFL NACVGVVEGD LSAVEAYKTS GGDIARQLSA DEVRLLNRPS
AFDVGYTLVH LSIRFQRQDM LAILLTEFSQ HAAKCIPAMV CPELTEQIRR EIAASVHQRK
GDFACYFLTD LVTFTLPADI EDLPPTVQEK LFDEVLDRDV QKELEEESPI INWSLELGTR
LDSRLYALWN RTAGDCLLDS VLQATWGIYD KDSVLRKALH DSLHDCSHWF YSRWKEWESW
YSQSFGLHFS LREEQWQEDW AFILSLASQP GASLEQTHIF VLAHILRRPI IVYGVKYYKS
FRGETLGYTR FQGVYLPLLW EQSFCWKSPI ALGYTRGHFS ALVAMENDGF DNRGAGANLN
TDDDVTVTFL PLVDSERKLL HIHFLSAQEL GNEDQQEKLL REWMDCCVTE GGVLVAMQKS
SRRRNHPLVT QMVEKWLDGY RQIRPCTALS DGEEDEDDED E
