ER6L2_HUMAN
ID ER6L2_HUMAN Reviewed; 1561 AA.
AC Q5T890; A4D997; B2RTP8; Q49AM9; Q5T892; Q8N663; Q8N9D0; Q9NPM7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DNA excision repair protein ERCC-6-like 2;
DE EC=3.6.4.-;
DE AltName: Full=DNA repair and recombination protein RAD26-like;
GN Name=ERCC6L2; Synonyms=C9orf102, RAD26L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1062-1561 (ISOFORM 1).
RC TISSUE=Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-365 (ISOFORM 2).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1269-1561 (ISOFORM 1).
RC TISSUE=Hippocampus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384 AND SER-1387, AND
RP IDENTIFICATION BY 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 [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP INVOLVEMENT IN BMFS2, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24507776; DOI=10.1016/j.ajhg.2014.01.007;
RA Tummala H., Kirwan M., Walne A.J., Hossain U., Jackson N., Pondarre C.,
RA Plagnol V., Vulliamy T., Dokal I.;
RT "ERCC6L2 mutations link a distinct bone-marrow-failure syndrome to DNA
RT repair and mitochondrial function.";
RL Am. J. Hum. Genet. 94:246-256(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May be involved in early DNA damage response.
CC {ECO:0000269|PubMed:24507776}.
CC -!- SUBUNIT: Isoform 2 interacts with NEK6. {ECO:0000269|PubMed:20873783}.
CC -!- INTERACTION:
CC Q5T890; Q9BWK5: CYREN; NbExp=3; IntAct=EBI-3951765, EBI-8787584;
CC Q5T890; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-3951765, EBI-2555179;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Mitochondrion. Note=Colocalizes with
CC NEK6 in the centrosome. In response to DNA damage, translocates from
CC the cytosol to mitochondria and nucleus in a reactive oxygen species
CC (ROS)-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5T890-1; Sequence=Displayed;
CC Name=2; Synonyms=RAD26L;
CC IsoId=Q5T890-2; Sequence=VSP_054668, VSP_054669;
CC Name=3;
CC IsoId=Q5T890-3; Sequence=VSP_054666, VSP_054667, VSP_054668,
CC VSP_054669;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow (at protein level).
CC {ECO:0000269|PubMed:24507776}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}.
CC -!- DISEASE: Bone marrow failure syndrome 2 (BMFS2) [MIM:615715]: An
CC autosomal recessive disorder characterized by trilineage bone marrow
CC failure, bone marrow hypocellularity, learning difficulties, and
CC microcephaly. Insufficient hematopoiesis results in peripheral blood
CC cytopenias, affecting myeloid, erythroid and megakaryocyte lines.
CC Cutaneous features and increased chromosome breakage are not features.
CC {ECO:0000269|PubMed:24507776}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22957.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB97543.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB97543.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAW92640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL159167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471174; EAW92636.1; -; Genomic_DNA.
DR EMBL; CH471174; EAW92640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC022957; AAH22957.3; ALT_INIT; mRNA.
DR EMBL; BC035183; AAH35183.1; -; mRNA.
DR EMBL; BC140702; AAI40703.1; -; mRNA.
DR EMBL; AL389953; CAB97543.1; ALT_SEQ; mRNA.
DR EMBL; AK095025; BAC04478.1; -; mRNA.
DR RefSeq; NP_001010895.1; NM_001010895.2.
DR RefSeq; NP_064592.2; NM_020207.4.
DR PDB; 6HQ9; X-ray; 1.98 A; A/B=26-92.
DR PDBsum; 6HQ9; -.
DR AlphaFoldDB; Q5T890; -.
DR SMR; Q5T890; -.
DR BioGRID; 131996; 7.
DR IntAct; Q5T890; 7.
DR STRING; 9606.ENSP00000288985; -.
DR CarbonylDB; Q5T890; -.
DR iPTMnet; Q5T890; -.
DR PhosphoSitePlus; Q5T890; -.
DR BioMuta; ERCC6L2; -.
DR DMDM; 74756405; -.
DR EPD; Q5T890; -.
DR jPOST; Q5T890; -.
DR MassIVE; Q5T890; -.
DR MaxQB; Q5T890; -.
DR PaxDb; Q5T890; -.
DR PeptideAtlas; Q5T890; -.
DR PRIDE; Q5T890; -.
DR Antibodypedia; 55361; 168 antibodies from 20 providers.
DR DNASU; 375748; -.
DR Ensembl; ENST00000665077.3; ENSP00000499371.3; ENSG00000182150.19.
DR GeneID; 375748; -.
DR KEGG; hsa:375748; -.
DR UCSC; uc004avt.5; human. [Q5T890-1]
DR CTD; 375748; -.
DR DisGeNET; 375748; -.
DR GeneCards; ERCC6L2; -.
DR HGNC; HGNC:26922; ERCC6L2.
DR HPA; ENSG00000182150; Low tissue specificity.
DR MalaCards; ERCC6L2; -.
DR MIM; 615667; gene.
DR MIM; 615715; phenotype.
DR neXtProt; NX_Q5T890; -.
DR Orphanet; 319465; Inherited acute myeloid leukemia.
DR Orphanet; 401764; Pancytopenia-developmental delay syndrome.
DR PharmGKB; PA134961240; -.
DR VEuPathDB; HostDB:ENSG00000182150; -.
DR eggNOG; KOG0387; Eukaryota.
DR HOGENOM; CLU_000315_17_10_1; -.
DR InParanoid; Q5T890; -.
DR OrthoDB; 372069at2759; -.
DR TreeFam; TF351516; -.
DR PathwayCommons; Q5T890; -.
DR SignaLink; Q5T890; -.
DR BioGRID-ORCS; 375748; 18 hits in 1076 CRISPR screens.
DR ChiTaRS; ERCC6L2; human.
DR GenomeRNAi; 375748; -.
DR Pharos; Q5T890; Tbio.
DR PRO; PR:Q5T890; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T890; protein.
DR Bgee; ENSG00000182150; Expressed in epithelial cell of pancreas and 189 other tissues.
DR ExpressionAtlas; Q5T890; baseline and differential.
DR Genevisible; Q5T890; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029256; Heliccase-ass-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF14773; VIGSSK; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1561
FT /note="DNA excision repair protein ERCC-6-like 2"
FT /id="PRO_0000326086"
FT DOMAIN 146..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 523..673
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 283..286
FT /note="DEAH box"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIM3"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIM3"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054666"
FT VAR_SEQ 190..209
FT /note="MPEFLLRSMKKEPLSSTAKK -> MQKERELQETIYFKNTWPAC (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054667"
FT VAR_SEQ 712
FT /note="R -> V (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_054668"
FT VAR_SEQ 713..1561
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_054669"
FT VARIANT 592
FT /note="V -> A (in dbSNP:rs2274654)"
FT /id="VAR_039987"
FT CONFLICT 1551..1555
FT /note="DENAT -> A (in Ref. 5; BAC04478)"
FT /evidence="ECO:0000305"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6HQ9"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:6HQ9"
FT STRAND 43..56
FT /evidence="ECO:0007829|PDB:6HQ9"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6HQ9"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6HQ9"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6HQ9"
SQ SEQUENCE 1561 AA; 177127 MW; 0322C679063DD958 CRC64;
MQPGSAPPPG RMDPSAPQPR AETSGKDIWH PGERCLAPSP DNGKLCEASI KSITVDENGK
SFAVVLYADF QERKIPLKQL QEVKFVKDCP RNLIFDDEDL EKPYFPNRKF PSSSVAFKLS
DNGDSIPYTI NRYLRDYQRE GTRFLYGHYI HGGGCILGDD MGLGKTVQVI SFLAAVLHKK
GTREDIENNM PEFLLRSMKK EPLSSTAKKM FLIVAPLSVL YNWKDELDTW GYFRVTVLHG
NRKDNELIRV KQRKCEIALT TYETLRLCLD ELNSLEWSAV IVDEAHRIKN PKARVTEVMK
ALKCNVRIGL TGTILQNNMK ELWCVMDWAV PGLLGSGTYF KKQFSDPVEH GQRHTATKRE
LATGRKAMQR LAKKMSGWFL RRTKTLIKDQ LPKKEDRMVY CSLTDFQKAV YQTVLETEDV
TLILQSSEPC TCRSGQKRRN CCYKTNSHGE TVKTLYLSYL TVLQKVANHV ALLQAASTSK
QQETLIKRIC DQVFSRFPDF VQKSKDAAFE TLSDPKYSGK MKVLQQLLNH CRKNRDKVLL
FSFSTKLLDV LQQYCMASGL DYRRLDGSTK SEERLKIVKE FNSTQDVNIC LVSTMAGGLG
LNFVGANVVV LFDPTWNPAN DLQAIDRAYR IGQCRDVKVL RLISLGTVEE IMYLRQIYKQ
QLHCVVVGSE NAKRYFEAVQ GSKEHQGELF GIHNLFKFRS QGSCLTKDIL EREGQVEAGI
MTATTWLKEG PPAHKLEMPR QPDCQECRGT EQAAEPLAKE ACDLCSDFSD EEPVGATGIK
TAKNKAPDSS KASSSPGQLT LLQCGFSKLL ETKCKAVEDS DGNTASDDES SDEQPTCLST
EAKDAGCEKN QDSLGTSKHQ KLDNILNPKE KHIFYKSEKI LEQNISSKSD EKKIKNTDKH
CILQNVTESE DSDVICPTQY TTERFPDNSI RFKPPLEGSE DSETEHTVKT RNNDNSRNTD
DKRNGIISKK LSPENTTLKS ILKRKGTSDI SDESDDIEIS SKSRVRKRAS SLRFKRIKET
KKELHNSPKT MNKTNQVYAA NEDHNSQFID DYSSSDESLS VSHFSFSKQS HRPRTIRDRT
SFSSKLPSHN KKNSTFIPRK PMKCSNEKVV NQEQSYESMD KFLDGVQEVA YIHSNQNVIG
SSKAENHMSR WAAHDVFELK QFSQLPANIA VCSSKTYKEK VDADTLPHTK KGQQPSEGSI
SLPLYISNPV NQKKKKVYHT NQTTFIIGET PKGIRRKQFE EMASYFNSSS VNEFAKHITN
ATSEERQKML RDFYASQYPE VKEFFVDSVS QFNNSSFEKG EQRTRKKSDK RESLIKPRLS
DSETLSFKDS TNKISQVCSL KTYKRKSVKF QNHISYREEV FFNDAETKKS PVSSTQEIDS
GKNSQASEDT VTSRSLNSES ETRERRLENT MKDQQDLTRT GISRKEPLLK LENKKIENPV
LENTSVISLL GDTSILDDLF KSHGNSPTQL PKKVLSGPME KAKQRPKDFW DILNEQNDES
LSKLTDLAVI ETLCEKAPLA APFKRREEPA TSLWKSNEKF LWKKFSPSDT DENATNTQST
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