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DDX56_HUMAN
ID   DDX56_HUMAN             Reviewed;         547 AA.
AC   Q9NY93; A4D2K9; C9JV95; Q6IAE2; Q9H9I8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 193.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX56;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent 61 kDa nucleolar RNA helicase;
DE   AltName: Full=DEAD box protein 21;
DE   AltName: Full=DEAD box protein 56;
GN   Name=DDX56; Synonyms=DDX21, NOH61;
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).
RC   TISSUE=Keratinocyte;
RX   PubMed=10749921; DOI=10.1091/mbc.11.4.1153;
RA   Zirwes R.F., Eilbracht J., Kneissel S., Schmidt-Zachmann M.S.;
RT   "A novel helicase-type protein in the nucleolus: protein NOH61.";
RL   Mol. Biol. Cell 11:1153-1167(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Camargo A.A., Nunes D.N., Samaia H.B., Simpson A.J.G., Dias-Neto E.;
RT   "Sequencing of a new human DEAD-box RNA helicase.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Glial tumor;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [8]
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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix;
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   [10]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND SER-532, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [14]
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 play a role in later stages of the processing of the pre-
CC       ribosomal particles leading to mature 60S ribosomal subunits. Has
CC       intrinsic ATPase activity.
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   -!- SUBUNIT: May form homooligomeric complexes.
CC   -!- INTERACTION:
CC       Q9NY93; P38919: EIF4A3; NbExp=3; IntAct=EBI-372376, EBI-299104;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NY93-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NY93-2; Sequence=VSP_044869;
CC   -!- TISSUE SPECIFICITY: Detected in heart, brain, liver, pancreas, placenta
CC       and lung.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ131712; CAB87992.1; -; mRNA.
DR   EMBL; AF247666; AAG36876.1; -; mRNA.
DR   EMBL; AL136700; CAB66635.1; -; mRNA.
DR   EMBL; AK022774; BAB14238.1; -; mRNA.
DR   EMBL; AK315363; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CR457213; CAG33494.1; -; mRNA.
DR   EMBL; AC004938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236960; EAL23752.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW61094.1; -; Genomic_DNA.
DR   EMBL; BC001235; AAH01235.1; -; mRNA.
DR   CCDS; CCDS5492.1; -. [Q9NY93-1]
DR   CCDS; CCDS59053.1; -. [Q9NY93-2]
DR   RefSeq; NP_001244118.1; NM_001257189.1. [Q9NY93-2]
DR   RefSeq; NP_061955.1; NM_019082.3. [Q9NY93-1]
DR   AlphaFoldDB; Q9NY93; -.
DR   SMR; Q9NY93; -.
DR   BioGRID; 120075; 303.
DR   IntAct; Q9NY93; 81.
DR   MINT; Q9NY93; -.
DR   STRING; 9606.ENSP00000258772; -.
DR   iPTMnet; Q9NY93; -.
DR   MetOSite; Q9NY93; -.
DR   PhosphoSitePlus; Q9NY93; -.
DR   SwissPalm; Q9NY93; -.
DR   BioMuta; DDX56; -.
DR   DMDM; 20139238; -.
DR   SWISS-2DPAGE; Q9NY93; -.
DR   EPD; Q9NY93; -.
DR   jPOST; Q9NY93; -.
DR   MassIVE; Q9NY93; -.
DR   MaxQB; Q9NY93; -.
DR   PaxDb; Q9NY93; -.
DR   PeptideAtlas; Q9NY93; -.
DR   PRIDE; Q9NY93; -.
DR   ProteomicsDB; 11840; -.
DR   ProteomicsDB; 83197; -. [Q9NY93-1]
DR   Antibodypedia; 13419; 357 antibodies from 27 providers.
DR   DNASU; 54606; -.
DR   Ensembl; ENST00000258772.10; ENSP00000258772.5; ENSG00000136271.11. [Q9NY93-1]
DR   Ensembl; ENST00000431640.5; ENSP00000393488.1; ENSG00000136271.11. [Q9NY93-2]
DR   GeneID; 54606; -.
DR   KEGG; hsa:54606; -.
DR   MANE-Select; ENST00000258772.10; ENSP00000258772.5; NM_019082.4; NP_061955.1.
DR   UCSC; uc003tlg.5; human. [Q9NY93-1]
DR   CTD; 54606; -.
DR   DisGeNET; 54606; -.
DR   GeneCards; DDX56; -.
DR   HGNC; HGNC:18193; DDX56.
DR   HPA; ENSG00000136271; Low tissue specificity.
DR   MIM; 608023; gene.
DR   neXtProt; NX_Q9NY93; -.
DR   OpenTargets; ENSG00000136271; -.
DR   PharmGKB; PA134916346; -.
DR   VEuPathDB; HostDB:ENSG00000136271; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   GeneTree; ENSGT00550000074946; -.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; Q9NY93; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q9NY93; -.
DR   TreeFam; TF300620; -.
DR   PathwayCommons; Q9NY93; -.
DR   SignaLink; Q9NY93; -.
DR   BioGRID-ORCS; 54606; 813 hits in 1093 CRISPR screens.
DR   ChiTaRS; DDX56; human.
DR   GeneWiki; DDX56; -.
DR   GenomeRNAi; 54606; -.
DR   Pharos; Q9NY93; Tbio.
DR   PRO; PR:Q9NY93; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9NY93; protein.
DR   Bgee; ENSG00000136271; Expressed in lower esophagus mucosa and 195 other tissues.
DR   ExpressionAtlas; Q9NY93; baseline and differential.
DR   Genevisible; Q9NY93; HS.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
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:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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   Alternative splicing; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..547
FT                   /note="Probable ATP-dependent RNA helicase DDX56"
FT                   /id="PRO_0000055058"
FT   DOMAIN          38..218
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          230..424
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          506..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           7..35
FT                   /note="Q motif"
FT   MOTIF           166..169
FT                   /note="DEAD box"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         141
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         532
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         298..337
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044869"
FT   CONFLICT        30
FT                   /note="P -> S (in Ref. 5; CAG33494)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="I -> T (in Ref. 4; BAB14238)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="E -> D (in Ref. 4; AK315363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="C -> Y (in Ref. 5; CAG33494)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   547 AA;  61590 MW;  6D127CDAA73610D2 CRC64;
     MEDSEALGFE HMGLDPRLLQ AVTDLGWSRP TLIQEKAIPL ALEGKDLLAR ARTGSGKTAA
     YAIPMLQLLL HRKATGPVVE QAVRGLVLVP TKELARQAQS MIQQLATYCA RDVRVANVSA
     AEDSVSQRAV LMEKPDVVVG TPSRILSHLQ QDSLKLRDSL ELLVVDEADL LFSFGFEEEL
     KSLLCHLPRI YQAFLMSATF NEDVQALKEL ILHNPVTLKL QESQLPGPDQ LQQFQVVCET
     EEDKFLLLYA LLKLSLIRGK SLLFVNTLER SYRLRLFLEQ FSIPTCVLNG ELPLRSRCHI
     ISQFNQGFYD CVIATDAEVL GAPVKGKRRG RGPKGDKASD PEAGVARGID FHHVSAVLNF
     DLPPTPEAYI HRAGRTARAN NPGIVLTFVL PTEQFHLGKI EELLSGENRG PILLPYQFRM
     EEIEGFRYRC RDAMRSVTKQ AIREARLKEI KEELLHSEKL KTYFEDNPRD LQLLRHDLPL
     HPAVVKPHLG HVPDYLVPPA LRGLVRPHKK RKKLSSSCRK AKRAKSQNPL RSFKHKGKKF
     RPTAKPS
 
 
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