DDX10_HUMAN
ID DDX10_HUMAN Reviewed; 875 AA.
AC Q13206; B2RCQ3; Q5BJD8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX10;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 10;
GN Name=DDX10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8660968; DOI=10.1006/geno.1996.0184;
RA Savitsky K., Ziv Y., Bar-Shira A., Gilad S., Tagle D.A., Smith S.,
RA Uziel T., Sfez S., Nahmias J., Sartiel A., Eddy R.L., Shows T.B.,
RA Collins F.S., Shiloh Y., Rotman G.;
RT "A human gene (DDX10) encoding a putative DEAD-box RNA helicase at 11q22-
RT q23.";
RL Genomics 33:199-206(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M.;
RT "Molecular analysis of the chromosomal breakpoints and identification of
RT the repetitive sequences near the breakpoints of NUP98 in therapy-related
RT leukemia with inv(11)(p15q22).";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539 AND SER-831, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-539; THR-577 AND
RP SER-831, 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-649, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 47-280 IN COMPLEX WITH ADP.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-566.
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: Putative ATP-dependent RNA helicase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- TISSUE SPECIFICITY: High in testis but widely expressed.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DDX10ID35.html";
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DR EMBL; U28042; AAC50823.1; -; mRNA.
DR EMBL; AB040537; BAB18536.1; -; mRNA.
DR EMBL; AK315216; BAG37650.1; -; mRNA.
DR EMBL; CH471065; EAW67122.1; -; Genomic_DNA.
DR EMBL; BC091521; AAH91521.1; -; mRNA.
DR EMBL; BC093654; AAH93654.1; -; mRNA.
DR EMBL; BC093656; AAH93656.1; -; mRNA.
DR CCDS; CCDS8342.1; -.
DR RefSeq; NP_004389.2; NM_004398.3.
DR PDB; 2PL3; X-ray; 2.15 A; A=47-280.
DR PDBsum; 2PL3; -.
DR AlphaFoldDB; Q13206; -.
DR SMR; Q13206; -.
DR BioGRID; 108027; 192.
DR IntAct; Q13206; 52.
DR MINT; Q13206; -.
DR STRING; 9606.ENSP00000314348; -.
DR iPTMnet; Q13206; -.
DR PhosphoSitePlus; Q13206; -.
DR BioMuta; DDX10; -.
DR DMDM; 76803554; -.
DR SWISS-2DPAGE; Q13206; -.
DR EPD; Q13206; -.
DR jPOST; Q13206; -.
DR MassIVE; Q13206; -.
DR MaxQB; Q13206; -.
DR PaxDb; Q13206; -.
DR PeptideAtlas; Q13206; -.
DR PRIDE; Q13206; -.
DR ProteomicsDB; 59224; -.
DR Antibodypedia; 1401; 50 antibodies from 17 providers.
DR DNASU; 1662; -.
DR Ensembl; ENST00000322536.8; ENSP00000314348.3; ENSG00000178105.12.
DR GeneID; 1662; -.
DR KEGG; hsa:1662; -.
DR MANE-Select; ENST00000322536.8; ENSP00000314348.3; NM_004398.4; NP_004389.2.
DR UCSC; uc001pkm.4; human.
DR CTD; 1662; -.
DR DisGeNET; 1662; -.
DR GeneCards; DDX10; -.
DR HGNC; HGNC:2735; DDX10.
DR HPA; ENSG00000178105; Low tissue specificity.
DR MIM; 601235; gene.
DR neXtProt; NX_Q13206; -.
DR OpenTargets; ENSG00000178105; -.
DR PharmGKB; PA27200; -.
DR VEuPathDB; HostDB:ENSG00000178105; -.
DR eggNOG; KOG0343; Eukaryota.
DR GeneTree; ENSGT00550000074980; -.
DR InParanoid; Q13206; -.
DR OMA; FLWRQKQ; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q13206; -.
DR TreeFam; TF315215; -.
DR PathwayCommons; Q13206; -.
DR SignaLink; Q13206; -.
DR BioGRID-ORCS; 1662; 775 hits in 1075 CRISPR screens.
DR ChiTaRS; DDX10; human.
DR EvolutionaryTrace; Q13206; -.
DR GeneWiki; DDX10; -.
DR GenomeRNAi; 1662; -.
DR Pharos; Q13206; Tbio.
DR PRO; PR:Q13206; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13206; protein.
DR Bgee; ENSG00000178105; Expressed in sural nerve and 175 other tissues.
DR ExpressionAtlas; Q13206; baseline and differential.
DR Genevisible; Q13206; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase;
KW Isopeptide bond; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..875
FT /note="Probable ATP-dependent RNA helicase DDX10"
FT /id="PRO_0000055083"
FT DOMAIN 100..274
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 287..448
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..97
FT /note="Q motif"
FT MOTIF 222..225
FT /note="DEAD box"
FT COMPBIAS 20..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 555
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y44"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 566
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035840"
FT CONFLICT 647
FT /note="D -> A (in Ref. 1; AAC50823)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="E -> D (in Ref. 1; AAC50823)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="K -> N (in Ref. 1; AAC50823)"
FT /evidence="ECO:0000305"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:2PL3"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:2PL3"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:2PL3"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:2PL3"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:2PL3"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2PL3"
SQ SEQUENCE 875 AA; 100888 MW; B61BF325921C62FD CRC64;
MGKTANSPGS GARPDPVRSF NRWKKKHSHR QNKKKQLRKQ LKKPEWQVER ESISRLMQNY
EKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI GLALQGKDVL GAAKTGSGKT
LAFLVPVLEA LYRLQWTSTD GLGVLIISPT RELAYQTFEV LRKVGKNHDF SAGLIIGGKD
LKHEAERINN INILVCTPGR LLQHMDETVS FHATDLQMLV LDEADRILDM GFADTMNAVI
ENLPKKRQTL LFSATQTKSV KDLARLSLKN PEYVWVHEKA KYSTPATLEQ NYIVCELQQK
ISVLYSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGV SILALHGRQQ QMRRMEVYNE
FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI HRAGRTARYK EDGEALLILL
PSEKAMVQQL LQKKVPVKEI KINPEKLIDV QKKLESILAQ DQDLKERAQR CFVSYVRSVY
LMKDKEVFDV SKLPIPEYAL SLGLAVAPRV RFLQKMQKQP TKELVRSQAD KVIEPRAPSL
TNDEVEEFRA YFNEKMSILQ KGGKRLEGTE HRQDNDTGNE EQEEEEDDEE EMEEKLAKAK
GSQAPSLPNT SEAQKIKEVP TQFLDRDEEE EDADFLKVKR HNVFGLDLKD EKTLQKKEPS
KSSIKKKMTK VAEAKKVMKR NFKVNKKITF TDEGELVQQW PQMQKSAIKD AEEDDDTGGI
NLHKAKERLQ EEDKFDKEEY RKKIKAKHRE KRLKEREARR EANKRQAKAK DEEEAFLDWS
DDDDDDDDGF DPSTLPDPDK YRSSEDSDSE DMENKISDTK KKQGMKKRSN SEVEDVGPTS
HNRKKARWDT LEPLDTGLSL AEDEELVLHL LRSQS
