ZUP1_BOVIN
ID ZUP1_BOVIN Reviewed; 579 AA.
AC Q3SWY8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Zinc finger-containing ubiquitin peptidase 1 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96AP4};
DE AltName: Full=Lys-63-specific deubiquitinase ZUFSP;
DE Short=DUB;
DE AltName: Full=Zinc finger with UFM1-specific peptidase domain protein;
GN Name=ZUP1 {ECO:0000250|UniProtKB:Q96AP4}; Synonyms=ZUFSP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinase with endodeubiquitinase activity that
CC specifically interacts with and cleaves 'Lys-63'-linked long
CC polyubiquitin chains. Shows only weak activity against 'Lys-11' and
CC 'Lys-48'-linked chains. Plays an important role in genome stability
CC pathways, functioning to prevent spontaneous DNA damage and also
CC promote cellular survival in response to exogenous DNA damage.
CC Modulates the ubiquitination status of replication protein A (RPA)
CC complex proteins in response to replication stress.
CC {ECO:0000250|UniProtKB:Q96AP4}.
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:Q96AP4};
CC -!- SUBUNIT: Interacts with RPA1 and RPA2. {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AP4}. Nucleus
CC {ECO:0000250|UniProtKB:Q96AP4}. Note=Mostly present in the nuclear
CC fraction. Localizes to DNA lesions. {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- DOMAIN: The motif interacting with ubiquitin (MIU) and ZUFSP ubiquitin-
CC binding domain (zUBD, also called ZUFSP helical arm ZHA) are
CC responsible for binding the distal (outgoing) ubiquitin units S1 and S2
CC respectively. {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- DOMAIN: C2H2-type zinc finger 4 is a ubiquitin-binding zinc finger
CC (UBZ) and required for polyubiquitin binding, possibly binding the
CC proximal ubiqutin, and for catalytic activity. C2H2-type zinc fingers
CC 1-3 are required for localization to sites of DNA damage.
CC {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. ZUFSP subfamily.
CC {ECO:0000305}.
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DR EMBL; BC104595; AAI04596.1; -; mRNA.
DR RefSeq; NP_001029766.1; NM_001034594.1.
DR AlphaFoldDB; Q3SWY8; -.
DR SMR; Q3SWY8; -.
DR STRING; 9913.ENSBTAP00000005061; -.
DR PaxDb; Q3SWY8; -.
DR PRIDE; Q3SWY8; -.
DR GeneID; 533724; -.
DR KEGG; bta:533724; -.
DR CTD; 221302; -.
DR eggNOG; KOG4696; Eukaryota.
DR InParanoid; Q3SWY8; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07910; Peptidase_C78; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..579
FT /note="Zinc finger-containing ubiquitin peptidase 1"
FT /id="PRO_0000244335"
FT ZN_FING 2..25
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 30..53
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ZN_FING 155..178
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 194..216
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 227..249
FT /note="MIU"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT REGION 250..275
FT /note="zUBD/ZHA"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 492
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 513
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT SITE 488
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
SQ SEQUENCE 579 AA; 66307 MW; 8920D6D34F2362A5 CRC64;
MLSCDICGET VSSEPDMKAH LLIVHMENEV ICPFCKLSGV NYDEMCFHIE TAHFEQNELE
RNFERINTVQ YGISDNRKDS SLQCRADINS SVHSACASNQ PKISAQSLPK DGTLKHKDFY
SENLTESRKF LKSTEKQSDR TKIKESIYET MYSPPECPFC GKIEDNSQDM ETHVKTKHAD
LLDTPLEDCN QLLYDCPMCG LVCTNYHILQ EHVDLHLEES SFGQGVNRVQ CSRDLELAQQ
LQQEEDRKRR SEESRQEMEE FQKLQRQYGL DNSGGYKQQQ LRNMEIEVNR GRMHPSEFHR
RKADMMESLA IGVDDGKTKT SGIMEALYRY YQNAATDVRR VWLSAGVDHF HSSFGDKGWG
CGYRNFQMLL SSLLQNDAYD DSLKGMSVPC IPKIQSMIED AWKEGFDPQG ASQLNDKLQG
TKAWIGACEI YTLLTSLRIK CRIVDFHKST GPLGTHPRLF EWILSYYASE REGSPKVVCT
SKPPIYLQHQ GHSRTVVGIE EKKNRTLCLL VFDPGCPSRE MQKLLKHDME VSSLKQLRKF
VGNLKHKQYQ IVAVEGVLSS EEKIARRQAS QVFTAEKIP
