WRIP1_RAT
ID WRIP1_RAT Reviewed; 660 AA.
AC Q8CG07;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ATPase WRNIP1;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q96S55};
DE AltName: Full=Werner helicase-interacting protein 1;
GN Name=Wrnip1 {ECO:0000250|UniProtKB:Q96S55};
GN Synonyms=Wrnip {ECO:0000312|EMBL:AAN15750.1, ECO:0000312|RGD:628836};
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] {ECO:0000312|EMBL:AAN15750.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAN15750.1};
RA Liaw L., Lindner V.;
RT "Expression of sequences in balloon-injured rat arteries.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-91; SER-92 AND
RP SER-153, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as a modulator of initiation or reinitiation events
CC during DNA polymerase delta-mediated DNA synthesis. In the presence of
CC ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is
CC decreased. Also plays a role in the innate immune defense against
CC viruses. Stabilizes the RIG-I/DDX58 dsRNA interaction and promotes RIG-
CC I/DDX58 'Lys-63'-linked polyubiquitination. In turn, RIG-I/DDX58
CC transmits the signal through mitochondrial MAVS.
CC {ECO:0000250|UniProtKB:Q96S55}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q96S55};
CC -!- SUBUNIT: Forms homooligomers, possibly octamers. Directly interacts
CC with POLD1, POLD2 and POLD4. Interacts with the N-terminal domain of
CC WRN. Interacts (via UBZ4-type zinc finger) with monoubiquitin and
CC polyubiquitin. Interacts with TRIM14 and PPP6C; these interactions
CC positively regulate the RIG-I/DDX58 signaling pathway.
CC {ECO:0000250|UniProtKB:Q91XU0, ECO:0000250|UniProtKB:Q96S55}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96S55}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96S55}. Note=Colocalizes with WRN in granular
CC structures in the nucleus. {ECO:0000250|UniProtKB:Q96S55}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000250|UniProtKB:Q96S55}.
CC -!- DOMAIN: The UBZ4-type zinc finger binds ubiquitin.
CC {ECO:0000250|UniProtKB:Q96S55}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2/3. {ECO:0000250|UniProtKB:Q96S55}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY136827; AAN15750.1; -; mRNA.
DR EMBL; BC098652; AAH98652.1; -; mRNA.
DR RefSeq; NP_758835.1; NM_172332.2.
DR AlphaFoldDB; Q8CG07; -.
DR SMR; Q8CG07; -.
DR STRING; 10116.ENSRNOP00000023332; -.
DR iPTMnet; Q8CG07; -.
DR PhosphoSitePlus; Q8CG07; -.
DR jPOST; Q8CG07; -.
DR PaxDb; Q8CG07; -.
DR PRIDE; Q8CG07; -.
DR Ensembl; ENSRNOT00000023332; ENSRNOP00000023332; ENSRNOG00000017040.
DR GeneID; 282835; -.
DR KEGG; rno:282835; -.
DR UCSC; RGD:628836; rat.
DR CTD; 56897; -.
DR RGD; 628836; Wrnip1.
DR eggNOG; KOG2028; Eukaryota.
DR InParanoid; Q8CG07; -.
DR OrthoDB; 580439at2759; -.
DR PhylomeDB; Q8CG07; -.
DR TreeFam; TF324547; -.
DR PRO; PR:Q8CG07; -.
DR Proteomes; UP000002494; Chromosome 17.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR040539; Znf-WRNIP1_ubi.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR Pfam; PF18279; zf-WRNIP1_ubi; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; Hydrolase; Immunity; Innate immunity; Isopeptide bond;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..660
FT /note="ATPase WRNIP1"
FT /id="PRO_0000084787"
FT ZN_FING 17..44
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 50..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 265..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 529
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT MOD_RES 557
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT MOD_RES 628
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
FT CROSSLNK 631
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96S55"
SQ SEQUENCE 660 AA; 71934 MW; 5FE09B9C225840F8 CRC64;
MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP AAGPHRAGER
AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD DGGETESRES YDAPPTPSGA
RLIPDFPVAR SSSPARKGLG KRPAAAAAAG SASPRSWDET EAQEEEEAGV DGDGDADVDG
EDDPGHWDAD AADASFGVSA GRAHPRALPA EEIRQMLEGK PLADKMRPDT LQDYIGQSRA
VGQETLLRSL LETNEIPSLI LWGPPGCGKT TLAHIIANNS KKHSIRFVTL SATNAKTNDV
RDVIKQAQNE KSFFKRKTIL FIDEIHRFNK SQQDTFLPHV ECGTITLIGA TTENPSFQVN
TALLSRCRVI VLEKLPVEAM VTILMRAINS LGIHVLDSSR PTDPLSHSSN CSSEPSVFIE
DKAVDTLAYL SDGDARTGLN GLQLAVLARL SSRKMFCKKS GQTYSPSRVL ITENDVKEGL
QRSHILYDRA GEEHYNCISA LHKAMRGSDQ NASLYWLARM LEGGEDPLYV ARRLVRFASE
DIGLADPSAL AQAVAAYQGC HFIGMPECEV LLAQCVVYFA RAPKSIEVYS AYNNVKACLR
SHQGPLPPVP LHLRNAPTRL MKDLGYGKGY KYNPMYSEPV DQDYLPEELR GVDFFKQRRC
