DNLI3_HUMAN
ID DNLI3_HUMAN Reviewed; 1009 AA.
AC P49916; E5KLB5; E5KLB6; Q16714; Q6NVK3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=DNA ligase 3;
DE EC=6.5.1.1 {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:20518483};
DE AltName: Full=DNA ligase III;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 3;
DE Flags: Precursor;
GN Name=LIG3;
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 3), AND INTERACTION WITH XRCC1.
RC TISSUE=Prostate;
RX PubMed=7760816; DOI=10.1128/mcb.15.6.3206;
RA Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C., Yu G.-L.,
RA Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E., Haseltine W.A.,
RA Lindahl T.;
RT "Molecular cloning and expression of human cDNAs encoding a novel DNA
RT ligase IV and DNA ligase III, an enzyme active in DNA repair and
RT recombination.";
RL Mol. Cell. Biol. 15:3206-3216(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=7565692; DOI=10.1128/mcb.15.10.5412;
RA Chen J., Tomkinson A.E., Ramos W., Mackey Z.B., Danehower S., Walter C.A.,
RA Schultz R.A., Besterman J.M., Husain I.;
RT "Mammalian DNA ligase III: molecular cloning, chromosomal localization, and
RT expression in spermatocytes undergoing meiotic recombination.";
RL Mol. Cell. Biol. 15:5412-5422(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-768.
RX PubMed=20843780; DOI=10.1093/nar/gkq750;
RA Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
RA Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M.,
RA Speed T.P., Scharfe C.;
RT "Identification of rare DNA variants in mitochondrial disorders with
RT improved array-based sequencing.";
RL Nucleic Acids Res. 39:44-58(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-867.
RG NIEHS SNPs program;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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] (ISOFORM 1).
RC TISSUE=Pancreas;
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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP INITIATION.
RX PubMed=10207110; DOI=10.1128/mcb.19.5.3869;
RA Lakshmipathy U., Campbell C.;
RT "The human DNA ligase III gene encodes nuclear and mitochondrial
RT proteins.";
RL Mol. Cell. Biol. 19:3869-3876(1999).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-216; SER-242 AND
RP SER-913, AND 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 [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24674627; DOI=10.1016/j.dnarep.2014.01.015;
RA Akbari M., Keijzers G., Maynard S., Scheibye-Knudsen M., Desler C.,
RA Hickson I.D., Bohr V.A.;
RT "Overexpression of DNA ligase III in mitochondria protects cells against
RT oxidative stress and improves mitochondrial DNA base excision repair.";
RL DNA Repair 16:44-53(2014).
RN [19]
RP STRUCTURE BY NMR OF 924-1009.
RX PubMed=11281714; DOI=10.1006/prep.2001.1391;
RA Thornton K.H., Krishnan V.V., West M.G., Popham J., Ramirez M.,
RA Thelen M.P., Cosman M.;
RT "Expression, purification, and biophysical characterization of the BRCT
RT domain of human DNA ligase IIIalpha.";
RL Protein Expr. Purif. 21:401-411(2001).
RN [20]
RP STRUCTURE BY NMR OF 1-204 IN COMPLEX WITH ZINC.
RX PubMed=15288782; DOI=10.1016/j.jmb.2004.06.035;
RA Kulczyk A.W., Yang J.C., Neuhaus D.;
RT "Solution structure and DNA binding of the zinc-finger domain from DNA
RT ligase IIIalpha.";
RL J. Mol. Biol. 341:723-738(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 257-833 IN COMPLEX WITH DNA AND
RP AMP, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF
RP LYS-410 AND ARG-414.
RX PubMed=20518483; DOI=10.1021/bi100503w;
RA Cotner-Gohara E., Kim I.K., Hammel M., Tainer J.A., Tomkinson A.E.,
RA Ellenberger T.;
RT "Human DNA ligase III recognizes DNA ends by dynamic switching between two
RT DNA-bound states.";
RL Biochemistry 49:6165-6176(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 924-1009 IN COMPLEX WITH XRCC1,
RP AND INTERACTION WITH XRCC1.
RX PubMed=21652643; DOI=10.1093/nar/gkr419;
RA Cuneo M.J., Gabel S.A., Krahn J.M., Ricker M.A., London R.E.;
RT "The structural basis for partitioning of the XRCC1/DNA ligase III-? BRCT-
RT mediated dimer complexes.";
RL Nucleic Acids Res. 39:7816-7827(2011).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-717.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Isoform 3 functions as heterodimer with DNA-repair protein
CC XRCC1 in the nucleus and can correct defective DNA strand-break repair
CC and sister chromatid exchange following treatment with ionizing
CC radiation and alkylating agents. Isoform 1 is targeted to mitochondria,
CC where it functions as DNA ligase in mitochondrial base-excision DNA
CC repair (PubMed:10207110, PubMed:24674627).
CC {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10135, ECO:0000269|PubMed:10207110,
CC ECO:0000269|PubMed:20518483};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Isoform 3 interacts (via BRCT domain) with the nuclear DNA-
CC repair protein XRCC1. {ECO:0000269|PubMed:21652643,
CC ECO:0000269|PubMed:7760816}.
CC -!- INTERACTION:
CC P49916; P61244: MAX; NbExp=2; IntAct=EBI-1753381, EBI-751711;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.
CC Note=Contains an N-terminal mitochondrial transit peptide.
CC {ECO:0000269|PubMed:10207110}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000305|PubMed:10207110}. Note=Contains an N-terminal
CC mitochondrial transit peptide. {ECO:0000305|PubMed:10207110}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial
CC transit peptide. {ECO:0000269|PubMed:10207110}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus
CC {ECO:0000305|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial
CC transit peptide. {ECO:0000305|PubMed:10207110}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=P49916-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49916-2; Sequence=VSP_001302;
CC Name=3; Synonyms=Alpha;
CC IsoId=P49916-3; Sequence=VSP_057464;
CC Name=4; Synonyms=Beta;
CC IsoId=P49916-4; Sequence=VSP_057464, VSP_001302;
CC -!- TISSUE SPECIFICITY: Testis, thymus, prostate and heart.
CC -!- DOMAIN: The PARP-type zinc finger is required for DNA ligase activity.
CC {ECO:0000269|PubMed:20518483}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation of
CC isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation of
CC isoform 2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=DNA ligase entry;
CC URL="https://en.wikipedia.org/wiki/DNA_ligase";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mpg/";
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DR EMBL; X84740; CAA59230.1; -; mRNA.
DR EMBL; U40671; AAA85022.1; -; mRNA.
DR EMBL; HQ204826; ADP89974.1; -; Genomic_DNA.
DR EMBL; HQ204826; ADP89975.1; -; Genomic_DNA.
DR EMBL; HQ204827; ADP89976.1; -; Genomic_DNA.
DR EMBL; HQ204827; ADP89977.1; -; Genomic_DNA.
DR EMBL; HQ204828; ADP89978.1; -; Genomic_DNA.
DR EMBL; HQ204828; ADP89979.1; -; Genomic_DNA.
DR EMBL; HQ204829; ADP89980.1; -; Genomic_DNA.
DR EMBL; HQ204829; ADP89981.1; -; Genomic_DNA.
DR EMBL; HQ204830; ADP89982.1; -; Genomic_DNA.
DR EMBL; HQ204830; ADP89983.1; -; Genomic_DNA.
DR EMBL; HQ204831; ADP89984.1; -; Genomic_DNA.
DR EMBL; HQ204831; ADP89985.1; -; Genomic_DNA.
DR EMBL; HQ204832; ADP89986.1; -; Genomic_DNA.
DR EMBL; HQ204832; ADP89987.1; -; Genomic_DNA.
DR EMBL; HQ204833; ADP89988.1; -; Genomic_DNA.
DR EMBL; HQ204833; ADP89989.1; -; Genomic_DNA.
DR EMBL; HQ204834; ADP89990.1; -; Genomic_DNA.
DR EMBL; HQ204834; ADP89991.1; -; Genomic_DNA.
DR EMBL; HQ204835; ADP89992.1; -; Genomic_DNA.
DR EMBL; HQ204835; ADP89993.1; -; Genomic_DNA.
DR EMBL; HQ204836; ADP89994.1; -; Genomic_DNA.
DR EMBL; HQ204836; ADP89995.1; -; Genomic_DNA.
DR EMBL; HQ204837; ADP89996.1; -; Genomic_DNA.
DR EMBL; HQ204837; ADP89997.1; -; Genomic_DNA.
DR EMBL; HQ204838; ADP89998.1; -; Genomic_DNA.
DR EMBL; HQ204838; ADP89999.1; -; Genomic_DNA.
DR EMBL; HQ204839; ADP90000.1; -; Genomic_DNA.
DR EMBL; HQ204839; ADP90001.1; -; Genomic_DNA.
DR EMBL; HQ204840; ADP90002.1; -; Genomic_DNA.
DR EMBL; HQ204840; ADP90003.1; -; Genomic_DNA.
DR EMBL; HQ204841; ADP90004.1; -; Genomic_DNA.
DR EMBL; HQ204841; ADP90005.1; -; Genomic_DNA.
DR EMBL; HQ204842; ADP90006.1; -; Genomic_DNA.
DR EMBL; HQ204842; ADP90007.1; -; Genomic_DNA.
DR EMBL; HQ204843; ADP90008.1; -; Genomic_DNA.
DR EMBL; HQ204843; ADP90009.1; -; Genomic_DNA.
DR EMBL; HQ204844; ADP90010.1; -; Genomic_DNA.
DR EMBL; HQ204844; ADP90011.1; -; Genomic_DNA.
DR EMBL; HQ204845; ADP90012.1; -; Genomic_DNA.
DR EMBL; HQ204845; ADP90013.1; -; Genomic_DNA.
DR EMBL; HQ204846; ADP90014.1; -; Genomic_DNA.
DR EMBL; HQ204846; ADP90015.1; -; Genomic_DNA.
DR EMBL; HQ204847; ADP90016.1; -; Genomic_DNA.
DR EMBL; HQ204847; ADP90017.1; -; Genomic_DNA.
DR EMBL; HQ204848; ADP90018.1; -; Genomic_DNA.
DR EMBL; HQ204848; ADP90019.1; -; Genomic_DNA.
DR EMBL; HQ204849; ADP90020.1; -; Genomic_DNA.
DR EMBL; HQ204849; ADP90021.1; -; Genomic_DNA.
DR EMBL; HQ204850; ADP90022.1; -; Genomic_DNA.
DR EMBL; HQ204850; ADP90023.1; -; Genomic_DNA.
DR EMBL; HQ204851; ADP90024.1; -; Genomic_DNA.
DR EMBL; HQ204851; ADP90025.1; -; Genomic_DNA.
DR EMBL; HQ204852; ADP90026.1; -; Genomic_DNA.
DR EMBL; HQ204852; ADP90027.1; -; Genomic_DNA.
DR EMBL; HQ204853; ADP90028.1; -; Genomic_DNA.
DR EMBL; HQ204853; ADP90029.1; -; Genomic_DNA.
DR EMBL; HQ204854; ADP90030.1; -; Genomic_DNA.
DR EMBL; HQ204854; ADP90031.1; -; Genomic_DNA.
DR EMBL; HQ204855; ADP90032.1; -; Genomic_DNA.
DR EMBL; HQ204855; ADP90033.1; -; Genomic_DNA.
DR EMBL; HQ204856; ADP90034.1; -; Genomic_DNA.
DR EMBL; HQ204856; ADP90035.1; -; Genomic_DNA.
DR EMBL; HQ204857; ADP90036.1; -; Genomic_DNA.
DR EMBL; HQ204857; ADP90037.1; -; Genomic_DNA.
DR EMBL; HQ204858; ADP90038.1; -; Genomic_DNA.
DR EMBL; HQ204858; ADP90039.1; -; Genomic_DNA.
DR EMBL; HQ204859; ADP90040.1; -; Genomic_DNA.
DR EMBL; HQ204859; ADP90041.1; -; Genomic_DNA.
DR EMBL; HQ204860; ADP90042.1; -; Genomic_DNA.
DR EMBL; HQ204860; ADP90043.1; -; Genomic_DNA.
DR EMBL; HQ204861; ADP90044.1; -; Genomic_DNA.
DR EMBL; HQ204861; ADP90045.1; -; Genomic_DNA.
DR EMBL; HQ204862; ADP90046.1; -; Genomic_DNA.
DR EMBL; HQ204862; ADP90047.1; -; Genomic_DNA.
DR EMBL; HQ204863; ADP90048.1; -; Genomic_DNA.
DR EMBL; HQ204863; ADP90049.1; -; Genomic_DNA.
DR EMBL; HQ204864; ADP90050.1; -; Genomic_DNA.
DR EMBL; HQ204864; ADP90051.1; -; Genomic_DNA.
DR EMBL; HQ204865; ADP90052.1; -; Genomic_DNA.
DR EMBL; HQ204865; ADP90053.1; -; Genomic_DNA.
DR EMBL; AF491645; AAL91592.1; -; Genomic_DNA.
DR EMBL; AC004223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80197.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80199.1; -; Genomic_DNA.
DR EMBL; BC068005; AAH68005.1; -; mRNA.
DR CCDS; CCDS11284.2; -. [P49916-1]
DR CCDS; CCDS11285.2; -. [P49916-2]
DR PIR; I37292; I37292.
DR RefSeq; NP_002302.2; NM_002311.4. [P49916-2]
DR RefSeq; NP_039269.2; NM_013975.3. [P49916-1]
DR RefSeq; XP_016880113.1; XM_017024624.1. [P49916-1]
DR PDB; 1IMO; NMR; -; A=924-1009.
DR PDB; 1IN1; NMR; -; A=924-1009.
DR PDB; 1UW0; NMR; -; A=88-204.
DR PDB; 3L2P; X-ray; 3.00 A; A=257-833.
DR PDB; 3PC7; X-ray; 1.65 A; A/B=924-1009.
DR PDB; 3PC8; X-ray; 2.31 A; C/D=924-1008.
DR PDB; 3QVG; X-ray; 2.26 A; A/C=924-1008.
DR PDB; 6WH1; X-ray; 2.40 A; B=932-1008.
DR PDBsum; 1IMO; -.
DR PDBsum; 1IN1; -.
DR PDBsum; 1UW0; -.
DR PDBsum; 3L2P; -.
DR PDBsum; 3PC7; -.
DR PDBsum; 3PC8; -.
DR PDBsum; 3QVG; -.
DR PDBsum; 6WH1; -.
DR AlphaFoldDB; P49916; -.
DR BMRB; P49916; -.
DR SASBDB; P49916; -.
DR SMR; P49916; -.
DR BioGRID; 110168; 180.
DR CORUM; P49916; -.
DR IntAct; P49916; 64.
DR MINT; P49916; -.
DR STRING; 9606.ENSP00000367787; -.
DR BindingDB; P49916; -.
DR ChEMBL; CHEMBL4295773; -.
DR DrugBank; DB00290; Bleomycin.
DR GlyGen; P49916; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49916; -.
DR PhosphoSitePlus; P49916; -.
DR BioMuta; LIG3; -.
DR DMDM; 251757259; -.
DR EPD; P49916; -.
DR jPOST; P49916; -.
DR MassIVE; P49916; -.
DR MaxQB; P49916; -.
DR PaxDb; P49916; -.
DR PeptideAtlas; P49916; -.
DR PRIDE; P49916; -.
DR ProteomicsDB; 56181; -. [P49916-1]
DR ProteomicsDB; 56182; -. [P49916-2]
DR Antibodypedia; 1860; 341 antibodies from 34 providers.
DR CPTC; P49916; 1 antibody.
DR DNASU; 3980; -.
DR Ensembl; ENST00000262327.9; ENSP00000262327.4; ENSG00000005156.12. [P49916-2]
DR Ensembl; ENST00000378526.9; ENSP00000367787.3; ENSG00000005156.12. [P49916-1]
DR GeneID; 3980; -.
DR KEGG; hsa:3980; -.
DR MANE-Select; ENST00000378526.9; ENSP00000367787.3; NM_013975.4; NP_039269.2.
DR UCSC; uc002hij.4; human. [P49916-1]
DR CTD; 3980; -.
DR DisGeNET; 3980; -.
DR GeneCards; LIG3; -.
DR HGNC; HGNC:6600; LIG3.
DR HPA; ENSG00000005156; Low tissue specificity.
DR MIM; 600940; gene.
DR neXtProt; NX_P49916; -.
DR OpenTargets; ENSG00000005156; -.
DR Orphanet; 298; Mitochondrial neurogastrointestinal encephalomyopathy.
DR PharmGKB; PA30374; -.
DR VEuPathDB; HostDB:ENSG00000005156; -.
DR eggNOG; KOG4437; Eukaryota.
DR GeneTree; ENSGT00940000156492; -.
DR HOGENOM; CLU_011787_0_0_1; -.
DR InParanoid; P49916; -.
DR OMA; FNDISLM; -.
DR OrthoDB; 274264at2759; -.
DR PhylomeDB; P49916; -.
DR TreeFam; TF316220; -.
DR BRENDA; 6.5.1.1; 2681.
DR PathwayCommons; P49916; -.
DR Reactome; R-HSA-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR SignaLink; P49916; -.
DR SIGNOR; P49916; -.
DR BioGRID-ORCS; 3980; 101 hits in 1083 CRISPR screens.
DR ChiTaRS; LIG3; human.
DR EvolutionaryTrace; P49916; -.
DR GeneWiki; LIG3; -.
DR GenomeRNAi; 3980; -.
DR Pharos; P49916; Tbio.
DR PRO; PR:P49916; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P49916; protein.
DR Bgee; ENSG00000005156; Expressed in buccal mucosa cell and 182 other tissues.
DR ExpressionAtlas; P49916; baseline and differential.
DR Genevisible; P49916; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070421; C:DNA ligase III-XRCC1 complex; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:BHF-UCL.
DR GO; GO:0003909; F:DNA ligase activity; IDA:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006288; P:base-excision repair, DNA ligation; IDA:BHF-UCL.
DR GO; GO:0006287; P:base-excision repair, gap-filling; TAS:Reactome.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR GO; GO:0006266; P:DNA ligation; IDA:BHF-UCL.
DR GO; GO:0006302; P:double-strand break repair; IDA:BHF-UCL.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IGI:BHF-UCL.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:BHF-UCL.
DR GO; GO:0007005; P:mitochondrion organization; IDA:BHF-UCL.
DR GO; GO:0090298; P:negative regulation of mitochondrial DNA replication; IMP:CACAO.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1740.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000977; DNA_ligase_ATP-dep.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR031916; LIG3_BRCT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR Pfam; PF16759; LIG3_BRCT; 1.
DR Pfam; PF00645; zf-PARP; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF117018; SSF117018; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00574; dnl1; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 1.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; ATP-binding;
KW Cell cycle; Cell division; DNA damage; DNA recombination; DNA repair;
KW DNA replication; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..1009
FT /note="DNA ligase 3"
FT /id="PRO_0000059574"
FT DOMAIN 933..1009
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ZN_FING 93..185
FT /note="PARP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264,
FT ECO:0000269|PubMed:15288782"
FT REGION 224..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..280
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20518483"
FT REGION 318..323
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20518483"
FT REGION 388..391
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20518483"
FT REGION 421..427
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20518483"
FT REGION 842..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 508
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135,
FT ECO:0000269|PubMed:20518483"
FT BINDING 506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305, ECO:0007744|PDB:3L2P"
FT BINDING 513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305, ECO:0007744|PDB:3L2P"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 560
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 655
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305, ECO:0007744|PDB:3L2P"
FT BINDING 671
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_057464"
FT VAR_SEQ 933..1009
FT /note="VLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLGSRDK
FT NPAAQQVSPEWIWACIRKRRLVAPC -> RRPASEQRGRTVPAGRR (in isoform
FT 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7565692, ECO:0000305"
FT /id="VSP_001302"
FT VARIANT 224
FT /note="R -> W (in dbSNP:rs3744356)"
FT /id="VAR_020196"
FT VARIANT 717
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs757797167)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036513"
FT VARIANT 768
FT /note="Y -> H (in dbSNP:rs200981995)"
FT /evidence="ECO:0000269|PubMed:20843780"
FT /id="VAR_072387"
FT VARIANT 867
FT /note="R -> H (in dbSNP:rs3136025)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018807"
FT VARIANT 898
FT /note="K -> T (in dbSNP:rs4986974)"
FT /id="VAR_021938"
FT VARIANT 986
FT /note="P -> S (in dbSNP:rs4986973)"
FT /id="VAR_020197"
FT MUTAGEN 410
FT /note="K->E: Nearly abolishes ligase activity with blunt-
FT ended DNA, but not with nicked DNA."
FT /evidence="ECO:0000269|PubMed:20518483"
FT MUTAGEN 414
FT /note="R->E: Abolishes ligase activity with blunt-ended
FT DNA, but not with nicked DNA."
FT /evidence="ECO:0000269|PubMed:20518483"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1UW0"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1UW0"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:1UW0"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1UW0"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1UW0"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1UW0"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1UW0"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1UW0"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 350..359
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 374..385
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 390..401
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 407..416
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 437..443
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 492..498
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 511..519
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 553..564
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 566..568
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 579..584
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 590..600
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 610..620
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 639..651
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 671..676
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 688..698
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 721..729
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 735..740
FT /evidence="ECO:0007829|PDB:3L2P"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 780..787
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 800..804
FT /evidence="ECO:0007829|PDB:3L2P"
FT STRAND 816..819
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 822..830
FT /evidence="ECO:0007829|PDB:3L2P"
FT HELIX 924..927
FT /evidence="ECO:0007829|PDB:1IMO"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:3QVG"
FT STRAND 936..938
FT /evidence="ECO:0007829|PDB:1IMO"
FT STRAND 942..944
FT /evidence="ECO:0007829|PDB:3QVG"
FT HELIX 952..961
FT /evidence="ECO:0007829|PDB:3PC7"
FT HELIX 969..974
FT /evidence="ECO:0007829|PDB:3PC7"
FT STRAND 976..980
FT /evidence="ECO:0007829|PDB:3PC7"
FT STRAND 982..984
FT /evidence="ECO:0007829|PDB:3QVG"
FT STRAND 988..991
FT /evidence="ECO:0007829|PDB:3PC7"
FT HELIX 993..1002
FT /evidence="ECO:0007829|PDB:3PC7"
SQ SEQUENCE 1009 AA; 112907 MW; 0E4057E33C3F19A6 CRC64;
MSLAFKIFFP QTLRALSRKE LCLFRKHHWR DVRQFSQWSE TDLLHGHPLF LRRKPVLSFQ
GSHLRSRATY LVFLPGLHVG LCSGPCEMAE QRFCVDYAKR GTAGCKKCKE KIVKGVCRIG
KVVPNPFSES GGDMKEWYHI KCMFEKLERA RATTKKIEDL TELEGWEELE DNEKEQITQH
IADLSSKAAG TPKKKAVVQA KLTTTGQVTS PVKGASFVTS TNPRKFSGFS AKPNNSGEAP
SSPTPKRSLS SSKCDPRHKD CLLREFRKLC AMVADNPSYN TKTQIIQDFL RKGSAGDGFH
GDVYLTVKLL LPGVIKTVYN LNDKQIVKLF SRIFNCNPDD MARDLEQGDV SETIRVFFEQ
SKSFPPAAKS LLTIQEVDEF LLRLSKLTKE DEQQQALQDI ASRCTANDLK CIIRLIKHDL
KMNSGAKHVL DALDPNAYEA FKASRNLQDV VERVLHNAQE VEKEPGQRRA LSVQASLMTP
VQPMLAEACK SVEYAMKKCP NGMFSEIKYD GERVQVHKNG DHFSYFSRSL KPVLPHKVAH
FKDYIPQAFP GGHSMILDSE VLLIDNKTGK PLPFGTLGVH KKAAFQDANV CLFVFDCIYF
NDVSLMDRPL CERRKFLHDN MVEIPNRIMF SEMKRVTKAL DLADMITRVI QEGLEGLVLK
DVKGTYEPGK RHWLKVKKDY LNEGAMADTA DLVVLGAFYG QGSKGGMMSI FLMGCYDPGS
QKWCTVTKCA GGHDDATLAR LQNELDMVKI SKDPSKIPSW LKVNKIYYPD FIVPDPKKAA
VWEITGAEFS KSEAHTADGI SIRFPRCTRI RDDKDWKSAT NLPQLKELYQ LSKEKADFTV
VAGDEGSSTT GGSSEENKGP SGSAVSRKAP SKPSASTKKA EGKLSNSNSK DGNMQTAKPS
AMKVGEKLAT KSSPVKVGEK RKAADETLCQ TKVLLDIFTG VRLYLPPSTP DFSRLRRYFV
AFDGDLVQEF DMTSATHVLG SRDKNPAAQQ VSPEWIWACI RKRRLVAPC
