DCR1C_HUMAN
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 03-AUG-2022, entry version 154.
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},
GN ASCID {ECO:0000303|PubMed:11336668}, SCIDA,
GN SNM1C {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]
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 [22]
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 [23]
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 [24]
RP INVOLVEMENT IN RSSCID.
RX PubMed=12569164; DOI=10.1172/jci200316774;
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 [25]
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 ATM, BRCA1, PRKDC and TP53BP1. Also exhibits
CC ATM- and phosphorylation-dependent interaction with the MRN complex,
CC composed of MRE11, RAD50, and NBN. {ECO:0000269|PubMed:11955432,
CC ECO:0000269|PubMed:14744996, ECO:0000269|PubMed:15456891,
CC ECO:0000269|PubMed:15574326, ECO:0000269|PubMed:15574327,
CC ECO:0000269|PubMed:15723659, ECO:0000269|PubMed:15936993}.
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/";
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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. [Q96SD1-3]
DR RefSeq; XP_011517918.1; XM_011519616.1. [Q96SD1-3]
DR RefSeq; XP_011517919.1; XM_011519617.1. [Q96SD1-3]
DR RefSeq; XP_011517921.1; XM_011519619.1. [Q96SD1-2]
DR RefSeq; XP_016872046.1; XM_017016557.1. [Q96SD1-3]
DR RefSeq; XP_016872047.1; XM_017016558.1. [Q96SD1-2]
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 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 AlphaFoldDB; Q96SD1; -.
DR SMR; Q96SD1; -.
DR BioGRID; 122170; 39.
DR CORUM; Q96SD1; -.
DR IntAct; Q96SD1; 22.
DR STRING; 9606.ENSP00000367527; -.
DR BindingDB; Q96SD1; -.
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; Q96SD1; -.
DR PeptideAtlas; Q96SD1; -.
DR PRIDE; Q96SD1; -.
DR ProteomicsDB; 78103; -. [Q96SD1-1]
DR ProteomicsDB; 78104; -. [Q96SD1-2]
DR ProteomicsDB; 78105; -. [Q96SD1-3]
DR ProteomicsDB; 78106; -. [Q96SD1-4]
DR Antibodypedia; 24989; 362 antibodies from 34 providers.
DR DNASU; 64421; -.
DR Ensembl; ENST00000357717.6; ENSP00000350349.2; ENSG00000152457.18. [Q96SD1-3]
DR Ensembl; ENST00000378246.6; ENSP00000367492.2; ENSG00000152457.18. [Q96SD1-3]
DR Ensembl; ENST00000378249.5; ENSP00000367496.1; ENSG00000152457.18. [Q96SD1-3]
DR Ensembl; ENST00000378254.5; ENSP00000367502.1; ENSG00000152457.18. [Q96SD1-2]
DR Ensembl; ENST00000378255.5; ENSP00000367503.1; ENSG00000152457.18. [Q96SD1-2]
DR Ensembl; ENST00000378258.5; ENSP00000367506.1; ENSG00000152457.18. [Q96SD1-2]
DR Ensembl; ENST00000378278.7; ENSP00000367527.2; ENSG00000152457.18. [Q96SD1-1]
DR Ensembl; ENST00000378289.8; ENSP00000367538.4; ENSG00000152457.18. [Q96SD1-4]
DR Ensembl; ENST00000396817.6; ENSP00000380030.2; ENSG00000152457.18. [Q96SD1-2]
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 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; CYSTHAS; -.
DR OrthoDB; 1441774at2759; -.
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; 16 hits in 1082 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 207 other tissues.
DR ExpressionAtlas; Q96SD1; baseline and differential.
DR Genevisible; Q96SD1; HS.
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' exodeoxyribonuclease 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:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
DR DisProt; DP01162; -.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 561."
FT /evidence="ECO:0000269|PubMed:15468306"
FT CONFLICT 560
FT /note="L -> V (in Ref. 1; CAC37570 and 2; AAM53255/
FT 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 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
