SPRTN_CAEEL
ID SPRTN_CAEEL Reviewed; 368 AA.
AC Q22557;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA-dependent metalloprotease dvc-1 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9H040};
DE AltName: Full=DNA damage protein targeting VCP {ECO:0000303|PubMed:23042605};
DE Short=DVC1 {ECO:0000303|PubMed:23042605};
DE AltName: Full=Protein with SprT-like domain at the N terminus {ECO:0000250|UniProtKB:Q9H040};
DE Short=Spartan {ECO:0000250|UniProtKB:Q9H040};
GN Name=dvc-1 {ECO:0000303|PubMed:23042605}; ORFNames=T19B10.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=23042605; DOI=10.1038/nsmb.2395;
RA Mosbech A., Gibbs-Seymour I., Kagias K., Thorslund T., Beli P., Povlsen L.,
RA Nielsen S.V., Smedegaard S., Sedgwick G., Lukas C., Hartmann-Petersen R.,
RA Lukas J., Choudhary C., Pocock R., Bekker-Jensen S., Mailand N.;
RT "DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes
RT ubiquitin-dependent responses to replication blocks.";
RL Nat. Struct. Mol. Biol. 19:1084-1092(2012).
RN [3]
RP FUNCTION.
RX PubMed=27871365; DOI=10.1016/j.molcel.2016.09.031;
RA Stingele J., Bellelli R., Alte F., Hewitt G., Sarek G., Maslen S.L.,
RA Tsutakawa S.E., Borg A., Kjaer S., Tainer J.A., Skehel J.M., Groll M.,
RA Boulton S.J.;
RT "Mechanism and regulation of DNA-protein crosslink repair by the DNA-
RT dependent metalloprotease SPRTN.";
RL Mol. Cell 64:688-703(2016).
CC -!- FUNCTION: DNA-dependent metalloendopeptidase that mediates the
CC proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during
CC DNA synthesis, thereby playing a key role in maintaining genomic
CC integrity (PubMed:27871365). DPCs are highly toxic DNA lesions that
CC interfere with essential chromatin transactions, such as replication
CC and transcription, and which are induced by reactive agents, such as UV
CC light or formaldehyde (PubMed:27871365). Associates with the DNA
CC replication machinery and specifically removes DPCs during DNA
CC synthesis (PubMed:27871365). Regulator of UV-induced DNA damage
CC response: required to protect genome stability during DNA replication,
CC possibly via recruitment of vcp/p97 (cdc-48.1 or cdc-48.2) recruitment
CC (PubMed:23042605). {ECO:0000269|PubMed:23042605,
CC ECO:0000269|PubMed:27871365}.
CC -!- SUBUNIT: Interacts with vcp/p97 (cdc-48.1 or cdc-48.2).
CC {ECO:0000269|PubMed:23042605}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23042605}. Chromosome
CC {ECO:0000269|PubMed:23042605}. Note=Localizes to nuclear foci following
CC UV treatment.
CC -!- DISRUPTION PHENOTYPE: In normal conditions, no obvious developmental or
CC behavioral defects are observed, except that but the brood size is
CC smaller. Upon exposure of L1 larvae to hydroxyurea, replication stress
CC sensitivity is observed, resulting in increased sterility.
CC {ECO:0000269|PubMed:23042605}.
CC -!- SIMILARITY: Belongs to the Spartan family. {ECO:0000305}.
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DR EMBL; Z74043; CAA98538.1; -; Genomic_DNA.
DR PIR; T24974; T24974.
DR RefSeq; NP_505853.1; NM_073452.6.
DR AlphaFoldDB; Q22557; -.
DR SMR; Q22557; -.
DR BioGRID; 44581; 2.
DR IntAct; Q22557; 1.
DR STRING; 6239.T19B10.6.1; -.
DR EPD; Q22557; -.
DR PaxDb; Q22557; -.
DR PRIDE; Q22557; -.
DR EnsemblMetazoa; T19B10.6.1; T19B10.6.1; WBGene00011834.
DR EnsemblMetazoa; T19B10.6.2; T19B10.6.2; WBGene00011834.
DR EnsemblMetazoa; T19B10.6.3; T19B10.6.3; WBGene00011834.
DR GeneID; 179554; -.
DR UCSC; T19B10.6.1; c. elegans.
DR CTD; 179554; -.
DR WormBase; T19B10.6; CE06460; WBGene00011834; dvc-1.
DR eggNOG; KOG3931; Eukaryota.
DR GeneTree; ENSGT00390000003585; -.
DR HOGENOM; CLU_019426_0_0_1; -.
DR InParanoid; Q22557; -.
DR OMA; RDRRPFF; -.
DR OrthoDB; 1182873at2759; -.
DR PhylomeDB; Q22557; -.
DR Reactome; R-CEL-110320; Translesion Synthesis by POLH.
DR PRO; PR:Q22557; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011834; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR044245; Spartan.
DR InterPro; IPR006640; SprT-like_domain.
DR PANTHER; PTHR21220; PTHR21220; 1.
DR Pfam; PF10263; SprT-like; 1.
DR SMART; SM00731; SprT; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..368
FT /note="DNA-dependent metalloprotease dvc-1"
FT /id="PRO_0000420712"
FT DOMAIN 21..190
FT /note="SprT-like"
FT ZN_FING 344..368
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 187..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000250|UniProtKB:Q9H040,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H040,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H040,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9H040"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 368 AA; 40566 MW; 2888A871027A3C41 CRC64;
MSRSSLVDPS FELSDPCPDI HALFIQFDAR FFGGSLACCE VKWSPRMYAC AGICSYEIRG
GRGGLCSIRL SKPLLTLRPR SDLVETLLHE MIHAYLFVKE RNRDRDGHGP QFQAHMHRIN
QAGGTNITIY HSFHDEVRLY KQHWWRCSGP CRDRRPFFGY VKRSCNRAPG PNDRWWSQHQ
QSCGGNFLKV KEPEGYGQGK GSKRTNDKNK SGGPALKKTI TPPRVTLDDF FKKDGKNSSD
NSTSKSPTKP STSLFTGSGQ KLGGSSSTSS LLNSYPKATQ NSGGNRLGGT SGGVSRLLPP
VNFTSPSSAP VAEQVIDLGD SDDDDFQDMD DDALEISFVA SDNSVICPSC NTEVMENLIH
GHLDYCLG
