ENDD1_HUMAN
ID ENDD1_HUMAN Reviewed; 500 AA.
AC O94919; A8K6K8; Q6GQY5; Q8TAQ8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Endonuclease domain-containing 1 protein;
DE EC=3.1.30.-;
DE Flags: Precursor;
GN Name=ENDOD1; Synonyms=KIAA0830;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=11921445;
RX DOI=10.1002/1615-9861(200203)2:3<288::aid-prot288>3.0.co;2-0;
RA O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA Watson S.P., Hebestreit H.F.;
RT "Towards complete analysis of the platelet proteome.";
RL Proteomics 2:288-305(2002).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH RNF26.
RX PubMed=32614325; DOI=10.7554/elife.57306;
RA Fenech E.J., Lari F., Charles P.D., Fischer R., Laetitia-Thezenas M.,
RA Bagola K., Paton A.W., Paton J.C., Gyrd-Hansen M., Kessler B.M.,
RA Christianson J.C.;
RT "Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies
RT modulators of innate immune signalling.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: May act as a DNase and a RNase. Plays a role in the
CC modulation of innate immune signaling through the cGAS-STING pathway by
CC interacting with RNF26. {ECO:0000269|PubMed:32614325}.
CC -!- SUBUNIT: Interacts with RNF26; this interaction is important to
CC modulate innate immune signaling through the cGAS-STING pathway
CC (PubMed:32614325). {ECO:0000269|PubMed:32614325}.
CC -!- INTERACTION:
CC O94919; P62760: VSNL1; NbExp=3; IntAct=EBI-6163734, EBI-740943;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020637; BAA74853.1; ALT_INIT; mRNA.
DR EMBL; AK291673; BAF84362.1; -; mRNA.
DR EMBL; BC026191; AAH26191.1; -; mRNA.
DR EMBL; BC071171; AAH71171.1; -; mRNA.
DR CCDS; CCDS41699.1; -.
DR RefSeq; NP_055851.1; NM_015036.2.
DR AlphaFoldDB; O94919; -.
DR SMR; O94919; -.
DR BioGRID; 116689; 124.
DR IntAct; O94919; 26.
DR MINT; O94919; -.
DR STRING; 9606.ENSP00000278505; -.
DR GlyGen; O94919; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94919; -.
DR MetOSite; O94919; -.
DR PhosphoSitePlus; O94919; -.
DR SwissPalm; O94919; -.
DR BioMuta; ENDOD1; -.
DR OGP; O94919; -.
DR EPD; O94919; -.
DR jPOST; O94919; -.
DR MassIVE; O94919; -.
DR MaxQB; O94919; -.
DR PaxDb; O94919; -.
DR PeptideAtlas; O94919; -.
DR PRIDE; O94919; -.
DR ProteomicsDB; 50555; -.
DR Antibodypedia; 2196; 99 antibodies from 21 providers.
DR DNASU; 23052; -.
DR Ensembl; ENST00000278505.5; ENSP00000278505.4; ENSG00000149218.5.
DR GeneID; 23052; -.
DR KEGG; hsa:23052; -.
DR MANE-Select; ENST00000278505.5; ENSP00000278505.4; NM_015036.3; NP_055851.1.
DR UCSC; uc001pfh.4; human.
DR CTD; 23052; -.
DR DisGeNET; 23052; -.
DR GeneCards; ENDOD1; -.
DR HGNC; HGNC:29129; ENDOD1.
DR HPA; ENSG00000149218; Low tissue specificity.
DR MIM; 619568; gene.
DR neXtProt; NX_O94919; -.
DR OpenTargets; ENSG00000149218; -.
DR PharmGKB; PA143485454; -.
DR VEuPathDB; HostDB:ENSG00000149218; -.
DR eggNOG; ENOG502QQYK; Eukaryota.
DR GeneTree; ENSGT01030000234592; -.
DR HOGENOM; CLU_035817_0_0_1; -.
DR InParanoid; O94919; -.
DR OMA; FQERWYM; -.
DR OrthoDB; 858590at2759; -.
DR PhylomeDB; O94919; -.
DR TreeFam; TF333322; -.
DR PathwayCommons; O94919; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; O94919; -.
DR BioGRID-ORCS; 23052; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; ENDOD1; human.
DR GenomeRNAi; 23052; -.
DR Pharos; O94919; Tdark.
DR PRO; PR:O94919; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O94919; protein.
DR Bgee; ENSG00000149218; Expressed in dorsal root ganglion and 203 other tissues.
DR Genevisible; O94919; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR039015; ENDOD1.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR PANTHER; PTHR21472; PTHR21472; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endonuclease; Hydrolase; Immunity; Innate immunity; Nuclease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..500
FT /note="Endonuclease domain-containing 1 protein"
FT /id="PRO_0000019924"
FT REGION 293..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 407
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 350
FT /note="V -> M (in dbSNP:rs3740862)"
FT /id="VAR_022044"
FT VARIANT 446
FT /note="G -> V (in dbSNP:rs3740861)"
FT /id="VAR_022045"
FT CONFLICT 113
FT /note="N -> I (in Ref. 2; BAF84362)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="Q -> R (in Ref. 2; BAF84362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55017 MW; 5B62754FE2E9AD9C CRC64;
MGTARWLALG SLFALAGLLE GRLVGEEEAG FGECDKFFYA GTPPAGLAAD SHVKICQRAE
GAERFATLYS TRDRIPVYSA FRAPRPAPGG AEQRWLVEPQ IDDPNSNLEE AINEAEAITS
VNSLGSKQAL NTDYLDSDYQ RGQLYPFSLS SDVQVATFTL TNSAPMTQSF QERWYVNLHS
LMDRALTPQC GSGEDLYILT GTVPSDYRVK DKVAVPEFVW LAACCAVPGG GWAMGFVKHT
RDSDIIEDVM VKDLQKLLPF NPQLFQNNCG ETEQDTEKMK KILEVVNQIQ DEERMVQSQK
SSSPLSSTRS KRSTLLPPEA SEGSSSFLGK LMGFIATPFI KLFQLIYYLV VAILKNIVYF
LWCVTKQVIN GIESCLYRLG SATISYFMAI GEELVSIPWK VLKVVAKVIR ALLRILCCLL
KAICRVLSIP VRVLVDVATF PVYTMGAIPI VCKDIALGLG GTVSLLFDTA FGTLGGLFQV
VFSVCKRIGY KVTFDNSGEL
