ZUP1_MACFA
ID ZUP1_MACFA Reviewed; 578 AA.
AC Q4R4A2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=Ubiquitin carboxyl-terminal hydrolase ZUFSP;
DE EC=3.4.19.12;
DE AltName: Full=Zinc finger with UFM1-specific peptidase domain protein;
GN Name=ZUP1 {ECO:0000250|UniProtKB:Q96AP4}; Synonyms=ZUFSP;
GN ORFNames=QtsA-11462;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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; AB179013; BAE02064.1; -; mRNA.
DR RefSeq; NP_001272087.1; NM_001285158.1.
DR AlphaFoldDB; Q4R4A2; -.
DR SMR; Q4R4A2; -.
DR STRING; 9541.XP_005551715.1; -.
DR GeneID; 101925089; -.
DR CTD; 221302; -.
DR eggNOG; KOG4696; Eukaryota.
DR OrthoDB; 788957at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..578
FT /note="Zinc finger-containing ubiquitin peptidase 1"
FT /id="PRO_0000244337"
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 154..177
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 193..215
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 226..248
FT /note="MIU"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT REGION 249..274
FT /note="zUBD/ZHA"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 360
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 491
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 512
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT SITE 487
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 262
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
SQ SEQUENCE 578 AA; 65775 MW; E09CD77DB037C1C4 CRC64;
MLSCDICGET VTSEPDMKAH LIVHMENEIV CPFCKLSGVS YDEMCFHIET AHFEQNTLER
NFERINTVQF GTSDNKKDNT LQCGMEVNSS ILSGCASNHP KNSSQCLTKD STLKHETFYS
ENLTESRKFL KSREKQSGLT EVKGSIYETT YGPPECPFCG KIEEHSEDME THVKTTHANL
LDISLEDCDQ PLYDCPMCGL ICTNYHILQE HVDLHLEENS FCQGMDRVQC SGDLQLAHQL
QQEEDRKRRS EESRQEIEEF QKLQRQYGLD NSGGYKQQQL RNMEIEVNRG RMPPSEFHRR
KADMMESLAI GIDDGKTKTS GIIEALHRYY QNAATDVRQV WLSSVVDHFH SSLGDKGWGC
GYRNFQMLLS SLLQNDAYDD CLKGMSVPCI PKIQSMIEDA WKEGFDPQGA SQLNNRLQGT
KAWIGACEVY ILLTSLRVKC HIVDFHKSTG PLGTHPRLFE WILNYYSSEG EGSPKVVCTS
KPPIYLQHQG HSRTVIGIEE KKNRTLCLLI FDPGCPSREM QKLLKQDVEA SSLKQLRKSM
GNLKHKQYQI VAVEGALSPE EKVARRQDSQ VFTAEKIP
