EEPD1_MOUSE
ID EEPD1_MOUSE Reviewed; 569 AA.
AC Q3TGW2; Q69ZC7; Q8K3B5; Q9D7J3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Endonuclease/exonuclease/phosphatase family domain-containing protein 1;
GN Name=Eepd1; Synonyms=Kiaa1706;
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 TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-110 AND SER-173, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND THR-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK173239; BAD32517.1; ALT_INIT; mRNA.
DR EMBL; AK009180; BAB26125.1; -; mRNA.
DR EMBL; AK168564; BAE40436.1; -; mRNA.
DR EMBL; BC025571; AAH25571.1; -; mRNA.
DR CCDS; CCDS22935.1; -.
DR RefSeq; NP_080465.3; NM_026189.3.
DR AlphaFoldDB; Q3TGW2; -.
DR SMR; Q3TGW2; -.
DR STRING; 10090.ENSMUSP00000047083; -.
DR iPTMnet; Q3TGW2; -.
DR PhosphoSitePlus; Q3TGW2; -.
DR SwissPalm; Q3TGW2; -.
DR jPOST; Q3TGW2; -.
DR MaxQB; Q3TGW2; -.
DR PaxDb; Q3TGW2; -.
DR PeptideAtlas; Q3TGW2; -.
DR PRIDE; Q3TGW2; -.
DR ProteomicsDB; 277685; -.
DR Antibodypedia; 26526; 98 antibodies from 19 providers.
DR DNASU; 67484; -.
DR Ensembl; ENSMUST00000040677; ENSMUSP00000047083; ENSMUSG00000036611.
DR GeneID; 67484; -.
DR KEGG; mmu:67484; -.
DR UCSC; uc009opn.1; mouse.
DR CTD; 80820; -.
DR MGI; MGI:1914734; Eepd1.
DR VEuPathDB; HostDB:ENSMUSG00000036611; -.
DR eggNOG; KOG1857; Eukaryota.
DR GeneTree; ENSGT00390000009677; -.
DR HOGENOM; CLU_033721_1_0_1; -.
DR InParanoid; Q3TGW2; -.
DR OMA; VRVATWS; -.
DR OrthoDB; 814192at2759; -.
DR PhylomeDB; Q3TGW2; -.
DR TreeFam; TF328735; -.
DR BioGRID-ORCS; 67484; 3 hits in 109 CRISPR screens.
DR PRO; PR:Q3TGW2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3TGW2; protein.
DR Bgee; ENSMUSG00000036611; Expressed in hindlimb stylopod muscle and 189 other tissues.
DR Genevisible; Q3TGW2; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR004509; Competence_ComEA_HhH.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR010994; RuvA_2-like.
DR SMART; SM00278; HhH1; 3.
DR SUPFAM; SSF47781; SSF47781; 2.
DR SUPFAM; SSF56219; SSF56219; 1.
DR TIGRFAMs; TIGR00426; TIGR00426; 1.
PE 1: Evidence at protein level;
KW Lipoprotein; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7L9B9"
FT CHAIN 2..569
FT /note="Endonuclease/exonuclease/phosphatase family domain-
FT containing protein 1"
FT /id="PRO_0000317262"
FT DOMAIN 38..67
FT /note="HhH"
FT REGION 200..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L9B9"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L9B9"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CONFLICT 30
FT /note="F -> L (in Ref. 2; BAB26125)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="A -> T (in Ref. 3; AAH25571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62953 MW; 9B4A49C082A3715F CRC64;
MGSTLGCHRS IPRDPSDLSH NRKFSAACNF SNILVNQERL NINTATEEEL MTLPGVTRAV
ARSIVEYREY IGGFKKVEDL ALVSGVGATK LEQVKFEICV SSKGNSAQHS PSSLRRDLLA
EQQPHHLTTT VPLTPRVNIN TATLAQLMSV RGLSEKMALS IVDYRREHGP FRSVEDLVRM
DGINAAFLDR IRHQVFAERS RPPSTHTNGG LTFTAKPHPS PTSLSLQSED LDLPPGGPTQ
IISMRPSVEA FGGMRDGRPV FRLATWNLQG CSVEKANNPG VREVVCMTLL ENSIKLLAVQ
ELLDKEALEK FCTELNQPIL PNIRKWKGSR GCWRSIVAEK PSNQLQKGPC YSGFLWDTAA
NVELRDIPGR ESSPSNGHAK AVGPSPFLAR FKVGSNDLTL VNLQLTALAL PGAENSSKNH
SDGHRLLNFA LTLQETLKGE KDVVILGDFG QGPDSNDYDI LRREKFHHLV PAHTFTNIST
RNPQGSKSVD NIWISKSLKK VFTGHWAVVR EGLTNPWIPD NWSWGGVASE HCPVLAELYM
EKDWSKKEVP RNGNGVTLEP SEANIKHER
