ID ZRAN1_MOUSE Reviewed; 708 AA. AC Q7M760; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 138. 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 {ECO:0000312|MGI:MGI:106441}; GN Name=Zranb1 {ECO:0000312|MGI:MGI:106441}; GN Synonyms=Trabid {ECO:0000312|MGI:MGI:106441}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP IDENTIFICATION. RX PubMed=12838346; DOI=10.1038/nrg1111; RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.; RT "Human and mouse proteases: a comparative genomic approach."; RL Nat. Rev. Genet. 4:544-558(2003). 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 -!- SUBUNIT: Interacts with TRAF6. Interacts with APC. CC {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}. 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; AC119806; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BN000126; CAD67576.1; -; mRNA. DR CCDS; CCDS21929.1; -. DR RefSeq; NP_997185.1; NM_207302.1. DR RefSeq; XP_006508030.1; XM_006507967.3. DR AlphaFoldDB; Q7M760; -. DR SMR; Q7M760; -. DR BioGRID; 237529; 4. DR STRING; 10090.ENSMUSP00000101763; -. DR MEROPS; C64.004; -. DR iPTMnet; Q7M760; -. DR PhosphoSitePlus; Q7M760; -. DR jPOST; Q7M760; -. DR PaxDb; 10090-ENSMUSP00000101763; -. DR ProteomicsDB; 275161; -. DR Antibodypedia; 35158; 185 antibodies from 27 providers. DR DNASU; 360216; -. DR Ensembl; ENSMUST00000033265.5; ENSMUSP00000033265.5; ENSMUSG00000030967.16. DR Ensembl; ENSMUST00000106157.8; ENSMUSP00000101763.2; ENSMUSG00000030967.16. DR GeneID; 360216; -. DR KEGG; mmu:360216; -. DR UCSC; uc009kcv.2; mouse. DR AGR; MGI:106441; -. DR CTD; 54764; -. DR MGI; MGI:106441; Zranb1. DR VEuPathDB; HostDB:ENSMUSG00000030967; -. DR eggNOG; KOG4345; Eukaryota. DR GeneTree; ENSGT00940000158045; -. DR HOGENOM; CLU_013907_0_0_1; -. DR InParanoid; Q7M760; -. DR OMA; MCDTKDD; -. DR OrthoDB; 2909231at2759; -. DR PhylomeDB; Q7M760; -. DR TreeFam; TF323312; -. DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases. DR BioGRID-ORCS; 360216; 10 hits in 78 CRISPR screens. DR ChiTaRS; Zranb1; mouse. DR PRO; PR:Q7M760; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q7M760; Protein. DR Bgee; ENSMUSG00000030967; Expressed in rostral migratory stream and 268 other cell types or tissues. DR ExpressionAtlas; Q7M760; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0101005; F:deubiquitinase activity; ISO:MGI. DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI. 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: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:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd22767; OTU_ZRANB1; 1. DR Gene3D; 1.25.40.560; -; 1. DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3. DR InterPro; IPR041294; AnkUBD. DR InterPro; IPR003323; OTU_dom. DR InterPro; IPR001876; Znf_RanBP2. DR InterPro; IPR036443; Znf_RanBP2_sf. DR InterPro; IPR049768; ZRANB1_OTU. DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1. DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1. 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; Ran binding protein zinc finger-like; 2. DR PROSITE; PS50802; OTU; 1. DR PROSITE; PS01358; ZF_RANBP2_1; 3. DR PROSITE; PS50199; ZF_RANBP2_2; 3. DR Genevisible; Q7M760; MM. 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..708 FT /note="Ubiquitin thioesterase Zranb1" FT /id="PRO_0000361554" FT REPEAT 260..290 FT /note="ANK 1" FT REPEAT 313..340 FT /note="ANK 2" FT DOMAIN 432..592 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 84..113 FT /note="RanBP2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT ZN_FING 149..178 FT /note="RanBP2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT REGION 38..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 202..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..65 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 443 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q9UGI0" FT ACT_SITE 585 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 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" 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 169 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" SQ SEQUENCE 708 AA; 80934 MW; B7C15B5E01DDF931 CRC64; MSEHGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG RDWDPSSTEG GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR AIRCTQCLSQ RRTRSPTESP QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT QHWTCSVCTY ENWAKAKKCV VCDHPRPNNI EAIELAETEE ASSIINEQDR ARWRGGCSSG NSQRRSPPTT KRDSEVKMDF QRIELAGAVG TKEELEVDFK KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQQAA KCIPAMVCPE LTEQIRREIA ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPTVQEKLFD EVLDRDVQKE LEEESPIINW SLELATRLDS RLYALWNRTA GDCLLDSVLQ ATWGIYDKDS VLRKALHDSL HDCSHWFYTR WKDWESWYSQ SFGLHFSLRE EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY GVKYYKSFRG ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW LDCCVTEGGV LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE EDEDDEDE //