DNSL1_HUMAN
ID DNSL1_HUMAN Reviewed; 302 AA.
AC P49184; D3DWW7; Q5HY41;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Deoxyribonuclease-1-like 1;
DE EC=3.1.21.-;
DE AltName: Full=DNase X;
DE AltName: Full=Deoxyribonuclease I-like 1;
DE Short=DNase I-like 1;
DE AltName: Full=Muscle-specific DNase I-like;
DE AltName: Full=XIB;
DE Flags: Precursor;
GN Name=DNASE1L1; Synonyms=DNAS1L1, DNL1L;
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 [MRNA].
RX PubMed=17180083;
RA Coy J.F., Velhagen I., Himmele R., Delius H., Poustka A., Zentgraf H.;
RT "Isolation, differential splicing and protein expression of a DNase on the
RT human X chromosome.";
RL Cell Death Differ. 3:199-206(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=8541839; DOI=10.1093/hmg/4.9.1557;
RA Parrish J.E., Ciccodicola A., Wehnert M., Cox G.F., Chen E., Nelson D.L.;
RT "A muscle-specific DNase I-like gene in human Xq28.";
RL Hum. Mol. Genet. 4:1557-1564(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=8654957; DOI=10.1016/0378-1119(95)00741-5;
RA Pergolizzi R., Appierto V., Bosetti A., Debellis G.L., Rovida E.,
RA Biunno I.;
RT "Cloning of a gene encoding a DNase I-like endonuclease in the human Xq28
RT region.";
RL Gene 168:267-270(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Cervix;
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 [8]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-261.
RX PubMed=16107205; DOI=10.1042/bj20051114;
RA Shiokawa D., Shika Y., Saito K., Yamazaki K., Tanuma S.;
RT "Physical and biochemical properties of mammalian DNase X proteins: non-AUG
RT translation initiation of porcine and bovine mRNAs for DNase X.";
RL Biochem. J. 392:511-517(2005).
CC -!- INTERACTION:
CC P49184; P23560-2: BDNF; NbExp=3; IntAct=EBI-20894690, EBI-12275524;
CC P49184; P27797: CALR; NbExp=3; IntAct=EBI-20894690, EBI-1049597;
CC P49184; P12830: CDH1; NbExp=3; IntAct=EBI-20894690, EBI-727477;
CC P49184; Q15078: CDK5R1; NbExp=3; IntAct=EBI-20894690, EBI-746189;
CC P49184; P36957: DLST; NbExp=3; IntAct=EBI-20894690, EBI-351007;
CC P49184; P28799: GRN; NbExp=3; IntAct=EBI-20894690, EBI-747754;
CC P49184; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-20894690, EBI-1055945;
CC P49184; P16284: PECAM1; NbExp=3; IntAct=EBI-20894690, EBI-716404;
CC P49184; P50454: SERPINH1; NbExp=3; IntAct=EBI-20894690, EBI-350723;
CC P49184; P37173: TGFBR2; NbExp=3; IntAct=EBI-20894690, EBI-296151;
CC P49184; O76024: WFS1; NbExp=3; IntAct=EBI-20894690, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16107205}.
CC -!- TISSUE SPECIFICITY: Highest levels in skeletal and cardiac muscles.
CC Detectable in all other tissues tested except brain.
CC {ECO:0000269|PubMed:8541839}.
CC -!- SIMILARITY: Belongs to the DNase I family. {ECO:0000305}.
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DR EMBL; X90392; CAA62037.1; -; mRNA.
DR EMBL; L40817; AAB00495.1; -; Genomic_DNA.
DR EMBL; L40823; AAB00496.1; -; mRNA.
DR EMBL; L44140; AAA92647.1; -; Genomic_DNA.
DR EMBL; U06846; AAB17022.1; -; mRNA.
DR EMBL; BX936347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72731.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72732.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72733.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72734.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72735.1; -; Genomic_DNA.
DR EMBL; BC001561; AAH01561.1; -; mRNA.
DR EMBL; BC028092; AAH28092.1; -; mRNA.
DR CCDS; CCDS14747.1; -.
DR PIR; JC4633; JC4633.
DR RefSeq; NP_001009932.1; NM_001009932.2.
DR RefSeq; NP_001009933.1; NM_001009933.2.
DR RefSeq; NP_001009934.1; NM_001009934.2.
DR RefSeq; NP_001290549.1; NM_001303620.1.
DR RefSeq; NP_006721.1; NM_006730.3.
DR RefSeq; XP_005277886.1; XM_005277829.4.
DR RefSeq; XP_011529424.1; XM_011531122.2.
DR RefSeq; XP_016884821.1; XM_017029332.1.
DR AlphaFoldDB; P49184; -.
DR SMR; P49184; -.
DR BioGRID; 108113; 137.
DR IntAct; P49184; 18.
DR STRING; 9606.ENSP00000358824; -.
DR GlyGen; P49184; 1 site.
DR iPTMnet; P49184; -.
DR PhosphoSitePlus; P49184; -.
DR BioMuta; DNASE1L1; -.
DR DMDM; 1352319; -.
DR EPD; P49184; -.
DR jPOST; P49184; -.
DR MassIVE; P49184; -.
DR MaxQB; P49184; -.
DR PaxDb; P49184; -.
DR PeptideAtlas; P49184; -.
DR PRIDE; P49184; -.
DR ProteomicsDB; 55967; -.
DR Antibodypedia; 31202; 170 antibodies from 24 providers.
DR DNASU; 1774; -.
DR Ensembl; ENST00000014935.7; ENSP00000014935.3; ENSG00000013563.14.
DR Ensembl; ENST00000309585.9; ENSP00000309168.5; ENSG00000013563.14.
DR Ensembl; ENST00000369807.6; ENSP00000358822.1; ENSG00000013563.14.
DR Ensembl; ENST00000369808.7; ENSP00000358823.3; ENSG00000013563.14.
DR Ensembl; ENST00000369809.5; ENSP00000358824.1; ENSG00000013563.14.
DR Ensembl; ENST00000393638.5; ENSP00000377255.1; ENSG00000013563.14.
DR GeneID; 1774; -.
DR KEGG; hsa:1774; -.
DR MANE-Select; ENST00000369807.6; ENSP00000358822.1; NM_001303620.2; NP_001290549.1.
DR UCSC; uc033fbh.2; human.
DR CTD; 1774; -.
DR DisGeNET; 1774; -.
DR GeneCards; DNASE1L1; -.
DR HGNC; HGNC:2957; DNASE1L1.
DR HPA; ENSG00000013563; Tissue enhanced (skeletal).
DR MalaCards; DNASE1L1; -.
DR MIM; 300081; gene.
DR neXtProt; NX_P49184; -.
DR OpenTargets; ENSG00000013563; -.
DR PharmGKB; PA27428; -.
DR VEuPathDB; HostDB:ENSG00000013563; -.
DR eggNOG; ENOG502QPNY; Eukaryota.
DR GeneTree; ENSGT00950000182846; -.
DR HOGENOM; CLU_043335_1_0_1; -.
DR InParanoid; P49184; -.
DR OMA; FHWAIAD; -.
DR OrthoDB; 1282784at2759; -.
DR PhylomeDB; P49184; -.
DR TreeFam; TF329541; -.
DR PathwayCommons; P49184; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P49184; -.
DR BioGRID-ORCS; 1774; 18 hits in 708 CRISPR screens.
DR ChiTaRS; DNASE1L1; human.
DR GeneWiki; DNASE1L1; -.
DR GenomeRNAi; 1774; -.
DR Pharos; P49184; Tbio.
DR PRO; PR:P49184; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P49184; protein.
DR Bgee; ENSG00000013563; Expressed in hindlimb stylopod muscle and 193 other tissues.
DR ExpressionAtlas; P49184; baseline and differential.
DR Genevisible; P49184; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0004536; F:deoxyribonuclease activity; TAS:ProtInc.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006308; P:DNA catabolic process; IBA:GO_Central.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR018057; Deoxyribonuclease-1_AS.
DR InterPro; IPR016202; DNase_I.
DR InterPro; IPR033125; DNASE_I_2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR PIRSF; PIRSF000988; DNase_I_euk; 1.
DR PRINTS; PR00130; DNASEI.
DR SMART; SM00476; DNaseIc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS00919; DNASE_I_1; 1.
DR PROSITE; PS00918; DNASE_I_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endonuclease; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Nuclease; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..302
FT /note="Deoxyribonuclease-1-like 1"
FT /id="PRO_0000007284"
FT ACT_SITE 97
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /evidence="ECO:0000250"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16107205"
FT DISULFID 187..224
FT /note="Essential for enzymatic activity"
FT /evidence="ECO:0000250"
FT VARIANT 122
FT /note="V -> I (in dbSNP:rs34952165)"
FT /id="VAR_048869"
FT CONFLICT 73
FT /note="L -> I (in Ref. 2; AAB00496)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="G -> D (in Ref. 2; AAB00496)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="G -> S (in Ref. 2; AAB00496)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="D -> A (in Ref. 2; AAB00495 and 3; AAA92647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33893 MW; D10CE8B470173727 CRC64;
MHYPTALLFL ILANGAQAFR ICAFNAQRLT LAKVAREQVM DTLVRILARC DIMVLQEVVD
SSGSAIPLLL RELNRFDGSG PYSTLSSPQL GRSTYMETYV YFYRSHKTQV LSSYVYNDED
DVFAREPFVA QFSLPSNVLP SLVLVPLHTT PKAVEKELNA LYDVFLEVSQ HWQSKDVILL
GDFNADCASL TKKRLDKLEL RTEPGFHWVI ADGEDTTVRA STHCTYDRVV LHGERCRSLL
HTAAAFDFPT SFQLTEEEAL NISDHYPVEV ELKLSQAHSV QPLSLTVLLL LSLLSPQLCP
AA
