ID DCR1C_HUMAN Reviewed; 692 AA. AC Q96SD1; D3DRT6; Q1HCL2; Q5JSR4; Q5JSR5; Q5JSR7; Q5JSR8; Q5JSR9; Q5JSS0; AC Q5JSS7; Q6PK14; Q8N101; Q8N132; Q8TBW9; Q9BVW9; Q9HAM4; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 2. DT 27-MAR-2024, entry version 163. DE RecName: Full=Protein artemis {ECO:0000303|PubMed:11336668}; DE EC=3.1.-.- {ECO:0000269|PubMed:11955432}; DE AltName: Full=DNA cross-link repair 1C protein {ECO:0000303|PubMed:12177301}; DE AltName: Full=Protein A-SCID {ECO:0000303|PubMed:11336668}; DE AltName: Full=SNM1 homolog C {ECO:0000303|PubMed:12177301}; DE Short=hSNM1C {ECO:0000303|PubMed:12177301}; DE AltName: Full=SNM1-like protein {ECO:0000303|PubMed:12055248}; GN Name=DCLRE1C {ECO:0000312|HGNC:HGNC:17642}; GN Synonyms=ARTEMIS {ECO:0000303|PubMed:11336668}, ASCID GN {ECO:0000303|PubMed:11336668}, SCIDA, SNM1C GN {ECO:0000303|PubMed:12177301}; 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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP INVOLVEMENT IN RSSCID. RX PubMed=11336668; DOI=10.1016/s0092-8674(01)00309-9; RA Moshous D., Callebaut I., de Chasseval R., Corneo B., Cavazzana-Calvo M., RA le Deist F., Tezcan I., Sanal O., Bertrand Y., Philippe N., Fischer A., RA de Villartay J.-P.; RT "Artemis, a novel DNA double-strand break repair/V(D)J recombination RT protein, is mutated in human severe combined immune deficiency."; RL Cell 105:177-186(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR RP LOCATION, AND INVOLVEMENT IN SCIDA. RX PubMed=12055248; DOI=10.4049/jimmunol.168.12.6323; RA Li L., Moshous D., Zhou Y., Wang J., Xie G., Salido E., Hu D., RA de Villartay J.-P., Cowan M.J.; RT "A founder mutation in Artemis, an SNM1-like protein, causes SCID in RT Athabascan-speaking native Americans."; RL J. Immunol. 168:6323-6329(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ARG-171. RC TISSUE=Embryo; 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-140; ARG-153; ARG-171; RP ARG-243; CYS-320 AND MET-329. RG NIEHS SNPs program; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). 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] (ISOFORMS 3 AND 4), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 401-692 (ISOFORMS 1/2/3), AND VARIANT RP ARG-243. RC TISSUE=Cervix carcinoma, Lung carcinoma, and Skeletal muscle; 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 FUNCTION, INTERACTION WITH PRKDC, PHOSPHORYLATION BY PRKDC, AND MUTAGENESIS RP OF ASP-165. RX PubMed=11955432; DOI=10.1016/s0092-8674(02)00671-2; RA Ma Y., Pannicke U., Schwarz K., Lieber M.R.; RT "Hairpin opening and overhang processing by an Artemis/DNA-dependent RT protein kinase complex in nonhomologous end joining and V(D)J RT recombination."; RL Cell 108:781-794(2002). RN [9] RP DNA REPAIR METALLO-BETA-LACTAMASE FAMILY. RX PubMed=12177301; DOI=10.1093/nar/gkf470; RA Callebaut I., Moshous D., Mornon J.-P., de Villartay J.-P.; RT "Metallo-beta-lactamase fold within nucleic acids processing enzymes: the RT beta-CASP family."; RL Nucleic Acids Res. 30:3592-3601(2002). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-17; HIS-33; HIS-35; RP ASP-37; HIS-38; HIS-115; ASP-136; ASP-165 AND HIS-319, AND PHOSPHORYLATION RP BY PRKDC. RX PubMed=15071507; DOI=10.1038/sj.emboj.7600206; RA Pannicke U., Ma Y., Hopfner K.-P., Niewolik D., Lieber M.R., Schwarz K.; RT "Functional and biochemical dissection of the structure-specific nuclease RT ARTEMIS."; RL EMBO J. 23:1987-1997(2004). RN [11] RP FUNCTION, MUTAGENESIS OF SER-516; SER-534; SER-538; SER-548; SER-553; RP SER-561 AND SER-562, PHOSPHORYLATION BY ATM, AND PHOSPHORYLATION AT RP SER-645. RX PubMed=15468306; DOI=10.1002/eji.200425455; RA Poinsignon C., de Chasseval R., Soubeyrand S., Moshous D., Fischer A., RA Hache R.J.G., de Villartay J.-P.; RT "Phosphorylation of Artemis following irradiation-induced DNA damage."; RL Eur. J. Immunol. 34:3146-3155(2004). RN [12] RP FUNCTION, INTERACTION WITH PRKDC, AND MUTAGENESIS OF ASP-17; HIS-33; RP HIS-35; ASP-37; HIS-38; HIS-115; ASP-136; ASP-165 AND HIS-319. RX PubMed=14744996; DOI=10.1084/jem.20031142; RA Poinsignon C., Moshous D., Callebaut I., de Chasseval R., Villey I., RA de Villartay J.-P.; RT "The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the RT catalytic core for V(D)J recombination."; RL J. Exp. Med. 199:315-321(2004). RN [13] RP FUNCTION, AND INTERACTION WITH PRKDC. RX PubMed=15574326; DOI=10.1016/j.molcel.2004.11.017; RA Ma Y., Lu H., Tippin B., Goodman M.F., Shimazaki N., Koiwai O., RA Hsieh C.-L., Schwarz K., Lieber M.R.; RT "A biochemically defined system for mammalian nonhomologous DNA end RT joining."; RL Mol. Cell 16:701-713(2004). RN [14] RP FUNCTION, INTERACTION WITH TP53BP1, MUTAGENESIS OF ASP-37, AND RP PHOSPHORYLATION BY ATM. RX PubMed=15574327; DOI=10.1016/j.molcel.2004.10.029; RA Riballo E., Kuehne M., Rief N., Doherty A., Smith G.C.M., Recio M.-J., RA Reis C., Dahm K., Fricke A., Krempler A., Parker A.R., Jackson S.P., RA Gennery A., Jeggo P.A., Loebrich M.; RT "A pathway of double-strand break rejoining dependent upon ATM, Artemis, RT and proteins locating to gamma-H2AX foci."; RL Mol. Cell 16:715-724(2004). RN [15] RP FUNCTION, INTERACTION WITH ATM; BRCA1; THE MRN COMPLEX AND PRKDC, AND RP PHOSPHORYLATION BY ATM; ATR AND PRKDC. RX PubMed=15456891; DOI=10.1128/mcb.24.20.9207-9220.2004; RA Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., RA Legerski R.J.; RT "Artemis is a phosphorylation target of ATM and ATR and is involved in the RT G2/M DNA damage checkpoint response."; RL Mol. Cell. Biol. 24:9207-9220(2004). RN [16] RP INTERACTION WITH THE MRN COMPLEX, PHOSPHORYLATION BY ATM, AND RP PHOSPHORYLATION AT SER-645. RX PubMed=15723659; DOI=10.1111/j.1349-7006.2005.00019.x; RA Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K., RA Chessa L., Villa A., Lecis D., Delia D., Mizutani S.; RT "Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in RT response to DNA damage."; RL Cancer Sci. 96:134-141(2005). RN [17] RP FUNCTION, PHOSPHORYLATION BY PRKDC, AND PHOSPHORYLATION IN RESPONSE TO DNA RP DAMAGE. RX PubMed=15811628; DOI=10.1016/j.dnarep.2005.02.001; RA Wang J., Pluth J.M., Cooper P.K., Cowan M.J., Chen D.J., Yannone S.M.; RT "Artemis deficiency confers a DNA double-strand break repair defect and RT Artemis phosphorylation status is altered by DNA damage and cell cycle RT progression."; RL DNA Repair 4:556-570(2005). RN [18] RP FUNCTION, AND INTERACTION WITH PRKDC. RX PubMed=15936993; DOI=10.1016/j.dnarep.2005.04.013; RA Ma Y., Schwarz K., Lieber M.R.; RT "The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and gaps."; RL DNA Repair 4:845-851(2005). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] {ECO:0007744|PDB:4HTP} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 485-495 IN COMPLEX WITH LIG4, AND RP INTERACTION WITH LIG4. RX PubMed=23219551; DOI=10.1016/j.celrep.2012.11.004; RA De Ioannes P., Malu S., Cortes P., Aggarwal A.K.; RT "Structural basis of DNA ligase IV-Artemis interaction in nonhomologous RT end-joining."; RL Cell Rep. 2:1505-1512(2012). RN [22] {ECO:0007744|PDB:3W1B, ECO:0007744|PDB:3W1G} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 485-495 IN COMPLEX WITH LIG4, AND RP INTERACTION WITH LIG4. RX PubMed=23523427; DOI=10.1016/j.str.2013.02.014; RA Ochi T., Gu X., Blundell T.L.; RT "Structure of the catalytic region of DNA ligase IV in complex with an RT Artemis fragment sheds light on double-strand break repair."; RL Structure 21:672-679(2013). RN [23] RP VARIANTS RSSCID VAL-118 AND GLU-135. RX PubMed=12406895; DOI=10.1182/blood-2002-01-0187; RA Noordzij J.G., Verkaik N.S., van der Burg M., van Veelen L.R., RA de Bruin-Versteeg S., Wiegant W., Vossen J.M.J.J., Weemaes C.M.R., RA de Groot R., Zdzienicka M.Z., van Gent D.C., van Dongen J.J.M.; RT "Radiosensitive SCID patients with Artemis gene mutations show a complete RT B-cell differentiation arrest at the pre-B-cell receptor checkpoint in bone RT marrow."; RL Blood 101:1446-1452(2003). RN [24] RP INVOLVEMENT IN RSSCID. RX PubMed=12921762; DOI=10.1016/s1521-6616(03)00095-0; RA Kobayashi N., Agematsu K., Nagumo H., Yasui K., Katsuyama Y., Yoshizawa K., RA Ota M., Yachie A., Komiyama A.; RT "Expansion of clonotype-restricted HLA-identical maternal CD4+ T cells in a RT patient with severe combined immunodeficiency and a homozygous mutation in RT the Artemis gene."; RL Clin. Immunol. 108:159-166(2003). RN [25] RP INVOLVEMENT IN RSSCID. RX PubMed=12592555; DOI=10.1007/s00439-002-0897-x; RA Kobayashi N., Agematsu K., Sugita K., Sako M., Nonoyama S., Yachie A., RA Kumaki S., Tsuchiya S., Ochs H.D., Sugita K., Fukushima Y., Komiyama A.; RT "Novel Artemis gene mutations of radiosensitive severe combined RT immunodeficiency in Japanese families."; RL Hum. Genet. 112:348-352(2003). RN [26] RP INVOLVEMENT IN RSSCID. RX PubMed=12569164; DOI=10.1172/jci16774; RA Moshous D., Pannetier C., de Chasseval R., le Deist F., Cavazzana-Calvo M., RA Romana S., Macintyre E., Canioni D., Brousse N., Fischer A., RA Casanova J.-L., de Villartay J.-P.; RT "Partial T and B lymphocyte immunodeficiency and predisposition to lymphoma RT in patients with hypomorphic mutations in Artemis."; RL J. Clin. Invest. 111:381-387(2003). RN [27] RP VARIANT OMENN SYNDROME ASP-35. RX PubMed=15731174; DOI=10.1182/blood-2004-12-4861; RA Ege M., Ma Y., Manfras B., Kalwak K., Lu H., Lieber M.R., Schwarz K., RA Pannicke U.; RT "Omenn syndrome due to ARTEMIS mutations."; RL Blood 105:4179-4186(2005). CC -!- FUNCTION: Nuclease involved in DNA non-homologous end joining (NHEJ); CC required for double-strand break repair and V(D)J recombination CC (PubMed:11336668, PubMed:11955432, PubMed:12055248, PubMed:14744996, CC PubMed:15071507, PubMed:15574326, PubMed:15936993). Required for V(D)J CC recombination, the process by which exons encoding the antigen-binding CC domains of immunoglobulins and T-cell receptor proteins are assembled CC from individual V, (D), and J gene segments (PubMed:11336668, CC PubMed:11955432, PubMed:14744996). V(D)J recombination is initiated by CC the lymphoid specific RAG endonuclease complex, which generates site CC specific DNA double strand breaks (DSBs) (PubMed:11336668, CC PubMed:11955432, PubMed:14744996). These DSBs present two types of DNA CC end structures: hairpin sealed coding ends and phosphorylated blunt CC signal ends (PubMed:11336668, PubMed:11955432, PubMed:14744996). These CC ends are independently repaired by the non homologous end joining CC (NHEJ) pathway to form coding and signal joints respectively CC (PubMed:11336668, PubMed:11955432, PubMed:14744996). This protein CC exhibits single-strand specific 5'-3' exonuclease activity in isolation CC and acquires endonucleolytic activity on 5' and 3' hairpins and CC overhangs when in a complex with PRKDC (PubMed:15071507, CC PubMed:15574326, PubMed:11955432, PubMed:15936993). The latter activity CC is required specifically for the resolution of closed hairpins prior to CC the formation of the coding joint (PubMed:11955432). Also required for CC the repair of complex DSBs induced by ionizing radiation, which require CC substantial end-processing prior to religation by NHEJ CC (PubMed:15456891, PubMed:15468306, PubMed:15574327, PubMed:15811628). CC {ECO:0000269|PubMed:11336668, ECO:0000269|PubMed:11955432, CC ECO:0000269|PubMed:12055248, ECO:0000269|PubMed:14744996, CC ECO:0000269|PubMed:15071507, ECO:0000269|PubMed:15456891, CC ECO:0000269|PubMed:15468306, ECO:0000269|PubMed:15574326, CC ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15811628, CC ECO:0000269|PubMed:15936993}. CC -!- SUBUNIT: Interacts with LIG4; the interaction is direct CC (PubMed:23523427, PubMed:23219551). Interacts with ATM CC (PubMed:15456891). Interacts with BRCA1 (PubMed:15456891). Interacts CC with PRKDC (PubMed:11955432, PubMed:14744996, PubMed:15456891, CC PubMed:15936993). Interacts with TP53BP1 (PubMed:15574327). Also CC exhibits ATM- and phosphorylation-dependent interaction with the MRN CC complex, composed of MRE11, RAD50, and NBN (PubMed:15456891, CC PubMed:15723659). {ECO:0000269|PubMed:11955432, CC ECO:0000269|PubMed:14744996, ECO:0000269|PubMed:15456891, CC ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15723659, CC ECO:0000269|PubMed:15936993, ECO:0000269|PubMed:23219551, CC ECO:0000269|PubMed:23523427}. CC -!- INTERACTION: CC Q96SD1; P49917: LIG4; NbExp=16; IntAct=EBI-11694104, EBI-847896; CC Q96SD1; P78527: PRKDC; NbExp=4; IntAct=EBI-11694104, EBI-352053; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12055248, CC ECO:0000269|PubMed:15071507}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q96SD1-1; Sequence=Displayed; CC Name=2; Synonyms=SCIDA; CC IsoId=Q96SD1-2; Sequence=VSP_014888; CC Name=3; CC IsoId=Q96SD1-3; Sequence=VSP_014889, VSP_014890; CC Name=4; CC IsoId=Q96SD1-4; Sequence=VSP_014891, VSP_014892; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in the CC kidney, lung, pancreas and placenta (at the mRNA level). Expression is CC not increased in thymus or bone marrow, sites of V(D)J recombination. CC {ECO:0000269|PubMed:11336668}. CC -!- PTM: Phosphorylation on undefined residues by PRKDC may stimulate CC endonucleolytic activity on 5' and 3' hairpins and overhangs. PRKDC CC must remain present, even after phosphorylation, for efficient hairpin CC opening. Also phosphorylated by ATM in response to ionizing radiation CC (IR) and by ATR in response to ultraviolet (UV) radiation. CC {ECO:0000269|PubMed:11955432, ECO:0000269|PubMed:15071507, CC ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15468306, CC ECO:0000269|PubMed:15574327, ECO:0000269|PubMed:15723659, CC ECO:0000269|PubMed:15811628}. CC -!- DISEASE: Severe combined immunodeficiency autosomal recessive T-cell- CC negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing CC radiation (RSSCID) [MIM:602450]: A form of severe combined CC immunodeficiency, a genetically and clinically heterogeneous group of CC rare congenital disorders characterized by impairment of both humoral CC and cell-mediated immunity, leukopenia, and low or absent antibody CC levels. Patients present in infancy with recurrent, persistent CC infections by opportunistic organisms. The common characteristic of all CC types of SCID is absence of T-cell-mediated cellular immunity due to a CC defect in T-cell development. Individuals affected by RS-SCID show CC defects in the DNA repair machinery necessary for coding joint CC formation and the completion of V(D)J recombination. A subset of cells CC from such patients show increased radiosensitivity. CC {ECO:0000269|PubMed:11336668, ECO:0000269|PubMed:12406895, CC ECO:0000269|PubMed:12569164, ECO:0000269|PubMed:12592555, CC ECO:0000269|PubMed:12921762}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Severe combined immunodeficiency Athabaskan type (SCIDA) CC [MIM:602450]: A variety of SCID with sensitivity to ionizing radiation. CC A founder mutation has been detected in Athabascan-speaking native CC Americans, being inherited as an autosomal recessive trait. Affected CC individuals exhibit clinical symptoms and defects in DNA repair CC comparable to those seen in RS-SCID. {ECO:0000269|PubMed:12055248}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Omenn syndrome (OS) [MIM:603554]: Severe immunodeficiency CC characterized by the presence of activated, anergic, oligoclonal T- CC cells, hypereosinophilia, and high IgE levels. CC {ECO:0000269|PubMed:15731174}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL) CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=DCLRE1Cbase; Note=DCLRE1C mutation db; CC URL="http://structure.bmc.lu.se/idbase/DCLRE1Cbase/"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/dclre1c/"; 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; AJ296101; CAC37570.1; -; mRNA. DR EMBL; AF395747; AAM53255.1; -; mRNA. DR EMBL; AF395748; AAM53256.1; -; mRNA. DR EMBL; AF395749; AAM53257.1; -; mRNA. DR EMBL; AF395750; AAM53258.1; -; mRNA. DR EMBL; AF395751; AAM53259.1; -; mRNA. DR EMBL; AF395752; AAM53260.1; -; mRNA. DR EMBL; AK021422; BAB13820.1; -; mRNA. DR EMBL; DQ504427; ABF47101.1; -; Genomic_DNA. DR EMBL; AC069544; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL360083; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86248.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86250.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86251.1; -; Genomic_DNA. DR EMBL; BC000863; AAH00863.1; -; mRNA. DR EMBL; BC009185; AAH09185.1; -; mRNA. DR EMBL; BC022254; AAH22254.1; -; mRNA. DR CCDS; CCDS31149.1; -. [Q96SD1-1] DR CCDS; CCDS31150.1; -. [Q96SD1-2] DR CCDS; CCDS7105.1; -. [Q96SD1-3] DR RefSeq; NP_001029027.1; NM_001033855.2. [Q96SD1-1] DR RefSeq; NP_001029029.1; NM_001033857.2. [Q96SD1-2] DR RefSeq; NP_001029030.1; NM_001033858.2. [Q96SD1-2] DR RefSeq; NP_001276005.1; NM_001289076.1. [Q96SD1-3] DR RefSeq; NP_001276006.1; NM_001289077.1. [Q96SD1-2] DR RefSeq; NP_001276007.1; NM_001289078.1. [Q96SD1-3] DR RefSeq; NP_001276008.1; NM_001289079.1. [Q96SD1-2] DR RefSeq; NP_071932.2; NM_022487.3. [Q96SD1-3] DR RefSeq; XP_006717554.1; XM_006717491.3. DR RefSeq; XP_011517918.1; XM_011519616.1. DR RefSeq; XP_011517919.1; XM_011519617.1. DR RefSeq; XP_011517921.1; XM_011519619.1. DR RefSeq; XP_016872046.1; XM_017016557.1. DR RefSeq; XP_016872047.1; XM_017016558.1. DR PDB; 3W1B; X-ray; 2.40 A; B=485-495. DR PDB; 3W1G; X-ray; 2.55 A; B=485-495. DR PDB; 4HTP; X-ray; 2.25 A; C/E=485-495. DR PDB; 6TT5; X-ray; 1.50 A; AAA=1-361. DR PDB; 6WNL; X-ray; 2.37 A; A/B=2-368. DR PDB; 6WO0; X-ray; 1.97 A; A=2-368. DR PDB; 7ABS; X-ray; 1.97 A; A=2-368. DR PDB; 7AF1; X-ray; 1.70 A; A=1-361. DR PDB; 7AFS; X-ray; 1.70 A; A=1-361. DR PDB; 7AFU; X-ray; 1.56 A; A=1-361. DR PDB; 7AGI; X-ray; 1.70 A; A=1-361. DR PDB; 7APV; X-ray; 1.95 A; A=1-361. DR PDB; 7SGL; EM; 3.00 A; D=1-692. DR PDB; 7TYR; EM; 3.33 A; C=1-692. DR PDBsum; 3W1B; -. DR PDBsum; 3W1G; -. DR PDBsum; 4HTP; -. DR PDBsum; 6TT5; -. DR PDBsum; 6WNL; -. DR PDBsum; 6WO0; -. DR PDBsum; 7ABS; -. DR PDBsum; 7AF1; -. DR PDBsum; 7AFS; -. DR PDBsum; 7AFU; -. DR PDBsum; 7AGI; -. DR PDBsum; 7APV; -. DR PDBsum; 7SGL; -. DR PDBsum; 7TYR; -. DR AlphaFoldDB; Q96SD1; -. DR EMDB; EMD-25113; -. DR EMDB; EMD-26192; -. DR EMDB; EMD-26198; -. DR SMR; Q96SD1; -. DR BioGRID; 122170; 41. DR CORUM; Q96SD1; -. DR IntAct; Q96SD1; 22. DR STRING; 9606.ENSP00000367527; -. DR BindingDB; Q96SD1; -. DR GlyCosmos; Q96SD1; 1 site, 1 glycan. DR GlyGen; Q96SD1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96SD1; -. DR PhosphoSitePlus; Q96SD1; -. DR BioMuta; DCLRE1C; -. DR DMDM; 71153325; -. DR EPD; Q96SD1; -. DR jPOST; Q96SD1; -. DR MassIVE; Q96SD1; -. DR MaxQB; Q96SD1; -. DR PaxDb; 9606-ENSP00000367527; -. DR PeptideAtlas; Q96SD1; -. DR ProteomicsDB; 78103; -. [Q96SD1-1] DR ProteomicsDB; 78104; -. [Q96SD1-2] DR ProteomicsDB; 78105; -. [Q96SD1-3] DR ProteomicsDB; 78106; -. [Q96SD1-4] DR Antibodypedia; 24989; 400 antibodies from 34 providers. DR DNASU; 64421; -. DR Ensembl; ENST00000378278.7; ENSP00000367527.2; ENSG00000152457.19. [Q96SD1-1] DR Ensembl; ENST00000378289.8; ENSP00000367538.4; ENSG00000152457.19. [Q96SD1-4] DR Ensembl; ENST00000697075.1; ENSP00000513090.1; ENSG00000152457.19. [Q96SD1-1] DR GeneID; 64421; -. DR KEGG; hsa:64421; -. DR MANE-Select; ENST00000378278.7; ENSP00000367527.2; NM_001033855.3; NP_001029027.1. DR UCSC; uc001inl.5; human. [Q96SD1-1] DR AGR; HGNC:17642; -. DR CTD; 64421; -. DR DisGeNET; 64421; -. DR GeneCards; DCLRE1C; -. DR HGNC; HGNC:17642; DCLRE1C. DR HPA; ENSG00000152457; Low tissue specificity. DR MalaCards; DCLRE1C; -. DR MIM; 602450; phenotype. DR MIM; 603554; phenotype. DR MIM; 605988; gene. DR neXtProt; NX_Q96SD1; -. DR OpenTargets; ENSG00000152457; -. DR Orphanet; 39041; Omenn syndrome. DR Orphanet; 275; Severe combined immunodeficiency due to DCLRE1C deficiency. DR PharmGKB; PA27176; -. DR VEuPathDB; HostDB:ENSG00000152457; -. DR eggNOG; KOG1361; Eukaryota. DR GeneTree; ENSGT00940000157779; -. DR HOGENOM; CLU_005260_1_1_1; -. DR InParanoid; Q96SD1; -. DR OMA; NVCYSTH; -. DR OrthoDB; 23465at2759; -. DR PhylomeDB; Q96SD1; -. DR TreeFam; TF329572; -. DR PathwayCommons; Q96SD1; -. DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ). DR SignaLink; Q96SD1; -. DR SIGNOR; Q96SD1; -. DR BioGRID-ORCS; 64421; 17 hits in 1161 CRISPR screens. DR ChiTaRS; DCLRE1C; human. DR GenomeRNAi; 64421; -. DR Pharos; Q96SD1; Tbio. DR PRO; PR:Q96SD1; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q96SD1; Protein. DR Bgee; ENSG00000152457; Expressed in buccal mucosa cell and 209 other cell types or tissues. DR ExpressionAtlas; Q96SD1; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IBA:GO_Central. DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:MGI. DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central. DR GO; GO:0004519; F:endonuclease activity; TAS:Reactome. DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:MGI. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central. DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl. DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central. DR GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl. DR CDD; cd16297; artemis-SNM1C-like_MBL-fold; 1. DR DisProt; DP01162; -. DR Gene3D; 3.40.50.12650; -; 1. DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1. DR InterPro; IPR011084; DRMBL. DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro. DR PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1. DR PANTHER; PTHR23240:SF38; PROTEIN ARTEMIS; 1. DR Pfam; PF07522; DRMBL; 1. DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1. DR Genevisible; Q96SD1; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Disease variant; KW DNA damage; DNA recombination; DNA repair; Endonuclease; Exonuclease; KW Hydrolase; Immunity; Magnesium; Nuclease; Nucleus; Phosphoprotein; KW Reference proteome; SCID. FT CHAIN 1..692 FT /note="Protein artemis" FT /id="PRO_0000209122" FT REGION 504..555 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 640..664 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 640..654 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 380 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8K4J0" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8K4J0" FT MOD_RES 645 FT /note="Phosphoserine; by ATM" FT /evidence="ECO:0000269|PubMed:15468306, FT ECO:0000269|PubMed:15723659" FT VAR_SEQ 1..120 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12055248" FT /id="VSP_014888" FT VAR_SEQ 1..115 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12055248, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_014889" FT VAR_SEQ 116..121 FT /note="CPGSVM -> MKHQER (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12055248, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_014890" FT VAR_SEQ 386..434 FT /note="EEEDDYLFDDPLPIPLRHKVPYPETFHPEVFSMTAVSEKQPEKLRQTPG -> FT GSHSVTQARMRWCHHDSLYPLTPGIKRSSCLSLLTSWITGAYRHAQLMI (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014891" FT VAR_SEQ 435..692 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014892" FT VARIANT 35 FT /note="H -> D (in Omenn syndrome; dbSNP:rs121908159)" FT /evidence="ECO:0000269|PubMed:15731174" FT /id="VAR_023077" FT VARIANT 118 FT /note="G -> V (in RSSCID)" FT /evidence="ECO:0000269|PubMed:12406895" FT /id="VAR_023078" FT VARIANT 135 FT /note="G -> E (in RSSCID)" FT /evidence="ECO:0000269|PubMed:12406895" FT /id="VAR_023079" FT VARIANT 140 FT /note="A -> V (in dbSNP:rs41297016)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_060689" FT VARIANT 153 FT /note="G -> R (in dbSNP:rs41297018)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_060690" FT VARIANT 171 FT /note="P -> R (in dbSNP:rs35441642)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4" FT /id="VAR_048892" FT VARIANT 243 FT /note="H -> R (in dbSNP:rs12768894)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4" FT /id="VAR_048893" FT VARIANT 320 FT /note="S -> C (in dbSNP:rs41298896)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_048894" FT VARIANT 329 FT /note="L -> M (in dbSNP:rs41299658)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_060691" FT MUTAGEN 17 FT /note="D->N,A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 33 FT /note="H->A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 35 FT /note="H->A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 37 FT /note="D->N,A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507, ECO:0000269|PubMed:15574327" FT MUTAGEN 38 FT /note="H->A: Reduces PRKDC-dependent endonuclease activity, FT although V(D)J recombination is largely normal." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 115 FT /note="H->A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 136 FT /note="D->N,A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 165 FT /note="D->N,A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:11955432, FT ECO:0000269|PubMed:14744996, ECO:0000269|PubMed:15071507" FT MUTAGEN 319 FT /note="H->A: Abolishes PRKDC-dependent endonuclease FT activity and V(D)J recombination." FT /evidence="ECO:0000269|PubMed:14744996, FT ECO:0000269|PubMed:15071507" FT MUTAGEN 516 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-534; A-538; A-548; A-553; A-561 and FT A-562." FT /evidence="ECO:0000269|PubMed:15468306" FT MUTAGEN 534 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-516; A-538; A-548; A-553; A-561 and FT A-562." FT /evidence="ECO:0000269|PubMed:15468306" FT MUTAGEN 538 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-516; A-534; A-548; A-553; A-561 and FT A-562." FT /evidence="ECO:0000269|PubMed:15468306" FT MUTAGEN 548 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-516; A-534; A-538; A-553; A-561 and FT A-562." FT /evidence="ECO:0000269|PubMed:15468306" FT MUTAGEN 553 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-516; A-534; A-538; A-548; A-561 and FT A-562." FT /evidence="ECO:0000269|PubMed:15468306" FT MUTAGEN 561 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-516; A-534; A-538; A-548; A-553 and FT A-562." FT /evidence="ECO:0000269|PubMed:15468306" FT MUTAGEN 562 FT /note="S->A: Reduced IR induced phosphorylation; when FT associated with A-516; A-534; A-538; A-548; A-553 and FT A-561." FT /evidence="ECO:0000269|PubMed:15468306" FT CONFLICT 560 FT /note="L -> V (in Ref. 1; CAC37570 and 2; FT AAM53255/AAM53256/AAM53257/AAM53258/AAM53259/AAM53260)" FT /evidence="ECO:0000305" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:6WNL" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 21..25 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:7ABS" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:7AFU" FT TURN 40..43 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 45..53 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 73..81 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:7AFU" FT TURN 98..100 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 103..112 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 179..194 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 200..204 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 213..223 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:7SGL" FT STRAND 283..290 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:7SGL" FT STRAND 303..306 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 308..315 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 322..332 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 335..340 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:7SGL" FT TURN 348..350 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 351..355 FT /evidence="ECO:0007829|PDB:7AFU" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:7AFU" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:7TYR" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:7SGL" FT HELIX 489..491 FT /evidence="ECO:0007829|PDB:4HTP" SQ SEQUENCE 692 AA; 78436 MW; 24B857F5B473637B CRC64; MSSFEGQMAE YPTISIDRFD RENLRARAYF LSHCHKDHMK GLRAPTLKRR LECSLKVYLY CSPVTKELLL TSPKYRFWKK RIISIEIETP TQISLVDEAS GEKEEIVVTL LPAGHCPGSV MFLFQGNNGT VLYTGDFRLA QGEAARMELL HSGGRVKDIQ SVYLDTTFCD PRFYQIPSRE ECLSGVLELV RSWITRSPYH VVWLNCKAAY GYEYLFTNLS EELGVQVHVN KLDMFRNMPE ILHHLTTDRN TQIHACRHPK AEEYFQWSKL PCGITSRNRI PLHIISIKPS TMWFGERSRK TNVIVRTGES SYRACFSFHS SYSEIKDFLS YLCPVNAYPN VIPVGTTMDK VVEILKPLCR SSQSTEPKYK PLGKLKRART VHRDSEEEDD YLFDDPLPIP LRHKVPYPET FHPEVFSMTA VSEKQPEKLR QTPGCCRAEC MQSSRFTNFV DCEESNSESE EEVGIPASLQ GDLGSVLHLQ KADGDVPQWE VFFKRNDEIT DESLENFPSS TVAGGSQSPK LFSDSDGEST HISSQNSSQS THITEQGSQG WDSQSDTVLL SSQERNSGDI TSLDKADYRP TIKENIPASL MEQNVICPKD TYSDLKSRDK DVTIVPSTGE PTTLSSETHI PEEKSLLNLS TNADSQSSSD FEVPSTPEAE LPKREHLQYL YEKLATGESI AVKKRKCSLL DT //