ZRAB3_MOUSE
ID ZRAB3_MOUSE Reviewed; 1069 AA.
AC Q6NZP1; Q148X9; Q8BJJ3; Q8BWT6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=DNA annealing helicase and endonuclease ZRANB3;
DE AltName: Full=Annealing helicase 2;
DE Short=AH2;
DE AltName: Full=Zinc finger Ran-binding domain-containing protein 3;
DE Includes:
DE RecName: Full=DNA annealing helicase ZRANB3;
DE EC=3.6.4.-;
DE Includes:
DE RecName: Full=Endonuclease ZRANB3;
DE EC=3.1.-.-;
GN Name=Zranb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 557-566, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: DNA annealing helicase and endonuclease required to maintain
CC genome stability at stalled or collapsed replication forks by
CC facilitating fork restart and limiting inappropriate recombination that
CC could occur during template switching events. Recruited to the sites of
CC stalled DNA replication by polyubiquitinated PCNA and acts as a
CC structure-specific endonuclease that cleaves the replication fork D-
CC loop intermediate, generating an accessible 3'-OH group in the template
CC of the leading strand, which is amenable to extension by DNA
CC polymerase. In addition to endonuclease activity, also catalyzes the
CC fork regression via annealing helicase activity in order to prevent
CC disintegration of the replication fork and the formation of double-
CC strand breaks. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- SUBUNIT: Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA
CC (when PCNA is polyubiquitinated via 'Lys-63'-linked polyubiquitin).
CC {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FWF4}.
CC Chromosome {ECO:0000250|UniProtKB:Q5FWF4}. Note=Following DNA damage,
CC recruited to sites of DNA damage and stalled replication forks by
CC polyubiquitinated PCNA. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA, while the
CC RanBP2-type zinc finger mediates binding to 'Lys-63'-linked
CC polyubiquitin. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- MISCELLANEOUS: In contrast to classical helicases that unwing DNA,
CC annealing helicases rewind it. {ECO:0000250|UniProtKB:Q5FWF4}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AK050039; BAC34042.1; -; mRNA.
DR EMBL; AK083641; BAC38978.1; -; mRNA.
DR EMBL; BC066035; AAH66035.1; -; mRNA.
DR EMBL; BC117921; AAI17922.1; -; mRNA.
DR EMBL; BC117922; AAI17923.1; -; mRNA.
DR CCDS; CCDS35697.1; -.
DR RefSeq; NP_001272874.1; NM_001285945.1.
DR RefSeq; NP_081954.1; NM_027678.3.
DR RefSeq; XP_006529475.1; XM_006529412.2.
DR AlphaFoldDB; Q6NZP1; -.
DR SMR; Q6NZP1; -.
DR BioGRID; 230505; 2.
DR STRING; 10090.ENSMUSP00000083806; -.
DR iPTMnet; Q6NZP1; -.
DR PhosphoSitePlus; Q6NZP1; -.
DR EPD; Q6NZP1; -.
DR MaxQB; Q6NZP1; -.
DR PaxDb; Q6NZP1; -.
DR PeptideAtlas; Q6NZP1; -.
DR PRIDE; Q6NZP1; -.
DR ProteomicsDB; 275160; -.
DR Antibodypedia; 56175; 79 antibodies from 18 providers.
DR Ensembl; ENSMUST00000086614; ENSMUSP00000083806; ENSMUSG00000036086.
DR Ensembl; ENSMUST00000112538; ENSMUSP00000108157; ENSMUSG00000036086.
DR GeneID; 226409; -.
DR KEGG; mmu:226409; -.
DR UCSC; uc007cld.2; mouse.
DR CTD; 84083; -.
DR MGI; MGI:1918362; Zranb3.
DR VEuPathDB; HostDB:ENSMUSG00000036086; -.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000158559; -.
DR HOGENOM; CLU_004251_0_0_1; -.
DR InParanoid; Q6NZP1; -.
DR OMA; PGFSEWF; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; Q6NZP1; -.
DR TreeFam; TF354227; -.
DR BioGRID-ORCS; 226409; 5 hits in 112 CRISPR screens.
DR ChiTaRS; Zranb3; mouse.
DR PRO; PR:Q6NZP1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6NZP1; protein.
DR Bgee; ENSMUSG00000036086; Expressed in dorsal pancreas and 175 other tissues.
DR Genevisible; Q6NZP1; MM.
DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0036292; P:DNA rewinding; ISS:UniProtKB.
DR GO; GO:0045910; P:negative regulation of DNA recombination; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR CDD; cd00085; HNHc; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002711; HNH.
DR InterPro; IPR003615; HNH_nuc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01844; HNH; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00507; HNHc; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Direct protein sequencing; DNA damage; DNA repair;
KW Endonuclease; Helicase; Hydrolase; Metal-binding; Multifunctional enzyme;
KW Nuclease; Nucleotide-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..1069
FT /note="DNA annealing helicase and endonuclease ZRANB3"
FT /id="PRO_0000278183"
FT DOMAIN 46..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 325..485
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1001..1041
FT /note="HNH"
FT ZN_FING 617..646
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 46..481
FT /note="DNA annealing helicase activity"
FT /evidence="ECO:0000250"
FT REGION 648..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1069
FT /note="Endonuclease activity"
FT /evidence="ECO:0000250"
FT MOTIF 157..160
FT /note="DEAH box"
FT MOTIF 518..525
FT /note="PIP-box"
FT MOTIF 1064..1068
FT /note="APIM motif"
FT COMPBIAS 651..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 311
FT /note="I -> M (in Ref. 1; BAC34042)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="G -> R (in Ref. 1; BAC38978)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="I -> L (in Ref. 2; AAI17923/AAI17922)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="S -> T (in Ref. 2; AAI17923/AAI17922)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="H -> R (in Ref. 2; AAI17923/AAI17922)"
FT /evidence="ECO:0000305"
FT CONFLICT 968
FT /note="R -> W (in Ref. 2; AAI17923/AAI17922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1069 AA; 120896 MW; A12C95AE382A4E75 CRC64;
MPTAGSKKKA PTPQISCLTS ESYTQLDFLP DKLRTKLLPF QKDGIVFALR RDGRCMVADE
MGLGKTIQAI AIAYFYKEEW PLLIVVPSSL RYPWIEELEK WIPELEPEEI NVVMNKTDIG
RIPGSRVTVL GYGLLTTDAE TLLDALNTQN FRVVIVDESH YMKSRTAARS KILLPMVQKA
RRAILLTGTP ALGRPEELFM QIEALFPQKF GTWIEYAKRY CNAHVRYFGK RRQWDCRGAS
NLSELHQLLN DIMIRRLKSE VLSQLPPKVR QRIPFDLPPA AVKELNASFE EWQKLMRAPN
SGAMETVMGL ITRMFKQTAI AKAGAVKDYI KMLLQNDSLK FLVFAHHLSM LQACTEAVIE
SKSRYIRIDG SVPSSERIHL VNQFQKDPDT RVAILSIQAA GQGLTFTAAS HVVFAELYWD
PGHIKQAEDR AHRIGQCSSV NIHYLIANGT LDSLMWAMLN RKAQVTGSTL NGRKEKLQAT
EDDKEKWGFL QFAEAWTPSD SFEELKDSVF THFEKEKQHD IRSFFLPKLK KRQLETTCDD
PEAFKEKITV ASDPRKMATS DSTADKNGCE PEAKRLKSLS TEDHSSALEE GPSLQARATS
MEVVHEVKPP LASPALPEKG WQCGFCTFLN NPGLPYCEMC ENPRSRAAGR NHLQDNNKND
EDAAQESTSK SDQAGLECER QCPERLEAEQ SANSKEEALE GGGEDRLPSQ PEIGQLNNSG
TLPVRETFMF CASRNTDRIH LYTKDGKPMN CNFIPLDIKL DLWEDLPATF QLKQNRSLIL
RFVREWSSLT AMKQRVLRKS GQLFCSPLLA SEEITKQQAK ENNTRRYITK EDVAKASMNK
VKSDGGHIRL ITKESMTQDS SLKKIDSACV PSLNPCPADL TVEPSPSKGY IQAVDKEGRP
LCLRCQHPTC QPEQTAKASA WDSRFCSLKC QEEFWIRSNN SYLRAQVFAT EHGVCQHCGV
DAQELFLRMR DAPKSHRKSL LNAAWTAKLP LEQLNEMLRN PGEGHFWQVD HIRPVYEGGG
QCSLDNLQTL CTVCHKERTA QQAKERSQVR RLSLATKHGS DITRFLVKK
