ID A0A0G2JUH4_RAT Unreviewed; 525 AA.
AC A0A0G2JUH4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Polynucleotide kinase 3'-phosphatase {ECO:0000313|Ensembl:ENSRNOP00000069099.2};
GN Name=Pnkp {ECO:0000313|Ensembl:ENSRNOP00000069099.2,
GN ECO:0000313|RGD:1303331};
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 {ECO:0000313|Ensembl:ENSRNOP00000069099.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000069099.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069099.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
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).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000069099.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069099.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A0G2JUH4; -.
DR STRING; 10116.ENSRNOP00000069099; -.
DR jPOST; A0A0G2JUH4; -.
DR Ensembl; ENSRNOT00000083551.2; ENSRNOP00000069099.2; ENSRNOG00000020318.8.
DR AGR; RGD:1303331; -.
DR RGD; 1303331; Pnkp.
DR VEuPathDB; HostDB:ENSRNOG00000020318; -.
DR GeneTree; ENSGT00940000159302; -.
DR InParanoid; A0A0G2JUH4; -.
DR OMA; AADWKWW; -.
DR Reactome; R-RNO-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020318; Expressed in testis and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JUH4; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0035861; C:site of double-strand break; ISO:RGD.
DR GO; GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0046403; F:polynucleotide 3'-phosphatase activity; ISO:RGD.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISO:RGD.
DR GO; GO:0006974; P:DNA damage response; ISO:RGD.
DR GO; GO:0051103; P:DNA ligation involved in DNA repair; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; ISO:RGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:RGD.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISO:RGD.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR CDD; cd22736; FHA_PNKP; 1.
DR CDD; cd01625; HAD_PNP; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041388; FHA_2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013954; PNK3P.
DR InterPro; IPR006550; PNKP.
DR InterPro; IPR006551; Polynucleotide_phosphatase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR NCBIfam; TIGR01664; DNA-3'-Pase; 1.
DR NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR NCBIfam; TIGR01663; PNK-3'Pase; 1.
DR PANTHER; PTHR12083; BIFUNCTIONAL POLYNUCLEOTIDE PHOSPHATASE/KINASE; 1.
DR PANTHER; PTHR12083:SF9; BIFUNCTIONAL POLYNUCLEOTIDE PHOSPHATASE_KINASE; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF17913; FHA_2; 1.
DR Pfam; PF08645; PNK3P; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JUH4};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 11..80
FT /note="PNK FHA"
FT /evidence="ECO:0000259|Pfam:PF17913"
FT REGION 110..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 57489 MW; 703D0A1521604F4B CRC64;
MSELGSRGRL WLQSPTGGPP PIFLPSDGQA LVLGRGPLTQ VMDRKCSRNQ VELIADPETR
TVAVKQLGVN PSTVGVQELK PGVSGSLSVG DVLYLVNGLY PLTLRWEEIS TPGSPPDTPP
GNPVDPEEGK DTEPQKKRMR KSSPGWESFK QLLVFTASGV KPRGKVAAFD LDGTLITTRS
GKVFPTSPSD WRILYPEIPK KLQELAAEGY KLVILTNQMG IGRGKLPAEV FKAKVEAVLE
KLGVPFQVLV ATHAGLNRKP VSGMWDHLQE KGNEGIPISI GDSVFVGGKR APSQLGPREE
EKGFLLCRPP GKPGFALNVG LPFATPEEFF LKWPAARFEL PAFDPRTISS AGPLYLPESS
FLLSPNPEVV VAVGFPGAGK STFIQKHLVS AGYVHVNRDT LGSWQRCVNS CQAALRQGKQ
VVIDNTNPDI QSRARYIQCA KDAGVPCRCF SFCATIEQAR HNNRFREMTD PSHAPVSDMV
MFSYRKQFEP PTLAEGFLEI LQVPFRLQEH LDPALQRLYC QFSEG
//
