ZUP1_RAT
ID ZUP1_RAT Reviewed; 577 AA.
AC Q5U2S3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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:0000312|RGD:1307672}; Synonyms=Zufsp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC085885; AAH85885.1; -; mRNA.
DR RefSeq; NP_001008309.1; NM_001008308.1.
DR RefSeq; XP_017457109.1; XM_017601620.1.
DR AlphaFoldDB; Q5U2S3; -.
DR SMR; Q5U2S3; -.
DR STRING; 10116.ENSRNOP00000000448; -.
DR PaxDb; Q5U2S3; -.
DR Ensembl; ENSRNOT00000000448; ENSRNOP00000000448; ENSRNOG00000000398.
DR GeneID; 294390; -.
DR KEGG; rno:294390; -.
DR UCSC; RGD:1307672; rat.
DR CTD; 221302; -.
DR RGD; 1307672; Zup1.
DR eggNOG; KOG4696; Eukaryota.
DR GeneTree; ENSGT00390000008232; -.
DR HOGENOM; CLU_017060_1_1_1; -.
DR InParanoid; Q5U2S3; -.
DR OMA; EEPRIHT; -.
DR OrthoDB; 788957at2759; -.
DR PhylomeDB; Q5U2S3; -.
DR TreeFam; TF323699; -.
DR PRO; PR:Q5U2S3; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000398; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q5U2S3; RN.
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; IPR038765; Papain-like_cys_pep_sf.
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 SUPFAM; SSF54001; SSF54001; 1.
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..577
FT /note="Zinc finger-containing ubiquitin peptidase 1"
FT /id="PRO_0000244339"
FT ZN_FING 2..24
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 29..52
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ZN_FING 153..176
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..214
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 225..247
FT /note="MIU"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT REGION 231..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..273
FT /note="zUBD/ZHA"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 490
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 511
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT SITE 486
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 261
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
SQ SEQUENCE 577 AA; 65722 MW; 1CF1EFC2EF2057CE CRC64;
MLSCDICGET VTSEPDRKAH LIVHMENEII CPFCKLSGIN YNEMCFHIET AHFEQTTPEK
SFETLAAVQY ENSDLGNTKL HSTVEVTSGI HSACASNFPK ESSESLSKDR TLKQEAFYTE
SVAESRKYQK SREKQSGLSE AQGSIYETTY SPPECPFCGR IERYSQDMEI HVKTKHASLL
ESPLEDCHQP LYDCPMCGLV CTNYHILQEH VDLHLEESSF QQGMDRVQCS SDRELAHQLQ
QEEERKRKSE ESRQEREEFQ KLQRQYGLDN SGGYKQQQLR HMELEVTRGR MHPSEFHSRK
ADMLESIAVG IDDGKTKTSG IIEALHRYYQ NIATDVRCVW LSTVVDHFHS SFGDKGWGCG
YRNFQMLLSS LLQNEVYSDC LKGMSVPCIP KIQSMIEDAW NEGFDPQGAS QLNNKLQGTK
AWIGACEIYT LLTSLKVKCR IIDFHKSTGP SGTHPRLFEW ILNYYSSETE GAPKVVCTSK
PPVYLQHQGH SRTVVGIEER KNRTLCLLIF DPGCPSREMQ KLLKQDMEAG SLRQLRKCVG
NLKHKQYQIV AVEGILSPEE RAARKQASQV FTAEKIP
