DDX4_HUMAN
ID DDX4_HUMAN Reviewed; 724 AA.
AC Q9NQI0; A8K8Q2; B3KSF4; D6RDK4; E9PCD8; Q5M7Z3; Q86VX0; Q9NT92; Q9NYB1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX4;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q61496};
DE AltName: Full=DEAD box protein 4;
DE AltName: Full=Vasa homolog;
GN Name=DDX4; Synonyms=VASA;
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, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10920202; DOI=10.1073/pnas.160274797;
RA Castrillon D.H., Quade B.J., Wang T.Y., Quigley C., Crum C.P.;
RT "The human VASA gene is specifically expressed in the germ cell lineage.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9585-9590(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Rocha D., Affara N.;
RT "Cloning and characterization of the human VASA gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis;
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].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-724 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP FUNCTION.
RX PubMed=21034600;
RA Li H.J., Yu N., Zhang X.Y., Jin W., Li H.Z.;
RT "Spermatozoal protein profiles in male infertility with
RT asthenozoospermia.";
RL Chin. Med. J. 123:2879-2882(2010).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=21421998; DOI=10.1093/hmg/ddr114;
RA Julaton V.T., Reijo Pera R.A.;
RT "NANOS3 function in human germ cell development.";
RL Hum. Mol. Genet. 20:2238-2250(2011).
RN [11]
RP INTERACTION WITH RANBP9.
RX PubMed=27622290; DOI=10.1016/j.jmb.2016.09.004;
RA Hong S.K., Kim K.H., Song E.J., Kim E.E.;
RT "Structural Basis for the Interaction between the IUS-SPRY Domain of RanBPM
RT and DDX-4 in Germ Cell Development.";
RL J. Mol. Biol. 428:4330-4344(2016).
CC -!- FUNCTION: ATP-dependent RNA helicase required during spermatogenesis
CC (PubMed:10920202, PubMed:21034600). Required to repress transposable
CC elements and preventing their mobilization, which is essential for the
CC germline integrity (By similarity). Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC governs the methylation and subsequent repression of transposons (By
CC similarity). Involved in the secondary piRNAs metabolic process, the
CC production of piRNAs in fetal male germ cells through a ping-pong
CC amplification cycle (By similarity). Required for PIWIL2 slicing-
CC triggered piRNA biogenesis: helicase activity enables utilization of
CC one of the slice cleavage fragments generated by PIWIL2 and processing
CC these pre-piRNAs into piRNAs (By similarity).
CC {ECO:0000250|UniProtKB:Q61496, ECO:0000269|PubMed:10920202,
CC ECO:0000269|PubMed:21034600}.
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 Evidence={ECO:0000250|UniProtKB:Q61496};
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC TDRD7 and DDX4 (By similarity). Interacts with RANBP9
CC (PubMed:27622290). Interacts with RANBP10. Interacts with PIWIL2 and
CC MAEL. Interacts with ARNTL/BMAL1 and CLOCK. Interacts with Tex19.1 and,
CC probably, Tex19.2 (By similarity). {ECO:0000250|UniProtKB:Q61496,
CC ECO:0000269|PubMed:27622290}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q61496}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000250|UniProtKB:Q61496}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NQI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQI0-2; Sequence=VSP_011197;
CC Name=3;
CC IsoId=Q9NQI0-3; Sequence=VSP_046132, VSP_011197, VSP_046133;
CC Name=4;
CC IsoId=Q9NQI0-4; Sequence=VSP_047177;
CC -!- TISSUE SPECIFICITY: Expressed only in ovary and testis. Expressed in
CC migratory primordial germ cells in the region of the gonadal ridge in
CC both sexes. {ECO:0000269|PubMed:10920202}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC subfamily. {ECO:0000305}.
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DR EMBL; AY004154; AAF86585.1; -; mRNA.
DR EMBL; AF262962; AAF72705.1; -; mRNA.
DR EMBL; AK093439; BAG52716.1; -; mRNA.
DR EMBL; AK292417; BAF85106.1; -; mRNA.
DR EMBL; AC016632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471123; EAW54929.1; -; Genomic_DNA.
DR EMBL; BC047455; AAH47455.1; -; mRNA.
DR EMBL; BC088362; AAH88362.1; -; mRNA.
DR EMBL; AL137462; CAB70750.1; -; mRNA.
DR CCDS; CCDS3969.1; -. [Q9NQI0-1]
DR CCDS; CCDS47208.1; -. [Q9NQI0-2]
DR CCDS; CCDS54854.1; -. [Q9NQI0-4]
DR CCDS; CCDS54855.1; -. [Q9NQI0-3]
DR PIR; T46407; T46407.
DR RefSeq; NP_001136021.1; NM_001142549.1. [Q9NQI0-2]
DR RefSeq; NP_001160005.1; NM_001166533.1. [Q9NQI0-4]
DR RefSeq; NP_001160006.1; NM_001166534.1. [Q9NQI0-3]
DR RefSeq; NP_077726.1; NM_024415.2. [Q9NQI0-1]
DR AlphaFoldDB; Q9NQI0; -.
DR SMR; Q9NQI0; -.
DR BioGRID; 120009; 22.
DR IntAct; Q9NQI0; 7.
DR MINT; Q9NQI0; -.
DR STRING; 9606.ENSP00000424838; -.
DR iPTMnet; Q9NQI0; -.
DR PhosphoSitePlus; Q9NQI0; -.
DR BioMuta; DDX4; -.
DR DMDM; 20138033; -.
DR REPRODUCTION-2DPAGE; IPI00456933; -.
DR EPD; Q9NQI0; -.
DR jPOST; Q9NQI0; -.
DR MassIVE; Q9NQI0; -.
DR MaxQB; Q9NQI0; -.
DR PaxDb; Q9NQI0; -.
DR PeptideAtlas; Q9NQI0; -.
DR PRIDE; Q9NQI0; -.
DR ProteomicsDB; 14124; -.
DR ProteomicsDB; 19429; -.
DR ProteomicsDB; 82159; -. [Q9NQI0-1]
DR ProteomicsDB; 82160; -. [Q9NQI0-2]
DR ABCD; Q9NQI0; 7 sequenced antibodies.
DR Antibodypedia; 23442; 391 antibodies from 38 providers.
DR DNASU; 54514; -.
DR Ensembl; ENST00000353507.9; ENSP00000334167.7; ENSG00000152670.19. [Q9NQI0-2]
DR Ensembl; ENST00000354991.9; ENSP00000347087.5; ENSG00000152670.19. [Q9NQI0-2]
DR Ensembl; ENST00000505374.6; ENSP00000424838.1; ENSG00000152670.19. [Q9NQI0-1]
DR Ensembl; ENST00000511853.1; ENSP00000423123.1; ENSG00000152670.19. [Q9NQI0-3]
DR Ensembl; ENST00000514278.6; ENSP00000425359.2; ENSG00000152670.19. [Q9NQI0-4]
DR GeneID; 54514; -.
DR KEGG; hsa:54514; -.
DR MANE-Select; ENST00000505374.6; ENSP00000424838.1; NM_024415.3; NP_077726.1.
DR UCSC; uc003jqg.5; human. [Q9NQI0-1]
DR CTD; 54514; -.
DR DisGeNET; 54514; -.
DR GeneCards; DDX4; -.
DR HGNC; HGNC:18700; DDX4.
DR HPA; ENSG00000152670; Tissue enriched (testis).
DR MIM; 605281; gene.
DR neXtProt; NX_Q9NQI0; -.
DR OpenTargets; ENSG00000152670; -.
DR PharmGKB; PA38646; -.
DR VEuPathDB; HostDB:ENSG00000152670; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q9NQI0; -.
DR OMA; GDEDWDT; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; Q9NQI0; -.
DR TreeFam; TF300364; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q9NQI0; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR SignaLink; Q9NQI0; -.
DR BioGRID-ORCS; 54514; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; DDX4; human.
DR GenomeRNAi; 54514; -.
DR Pharos; Q9NQI0; Tbio.
DR PRO; PR:Q9NQI0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NQI0; protein.
DR Bgee; ENSG00000152670; Expressed in secondary oocyte and 88 other tissues.
DR ExpressionAtlas; Q9NQI0; baseline and differential.
DR Genevisible; Q9NQI0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0071547; C:piP-body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; ISS:UniProtKB.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR DisProt; DP01066; -. [Q9NQI0-2]
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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 Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..724
FT /note="Probable ATP-dependent RNA helicase DDX4"
FT /id="PRO_0000054977"
FT DOMAIN 319..502
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 530..675
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..247
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000269|PubMed:27622290"
FT REGION 704..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 288..316
FT /note="Q motif"
FT MOTIF 446..449
FT /note="DEAD box"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT COMPBIAS 76..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64060"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61496"
FT VAR_SEQ 1..111
FT /note="MGDEDWEAEINPHMSSYVPIFEKDRYSGENGDNFNRTPASSSEMDDGPSRRD
FT HFMKSGFASGRNFGNRDAGECNKRDNTSTMGGFGVGKSFGNRGFSNSRFEDGDSSGFWR
FT -> MGSRNLFLTNSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046132"
FT VAR_SEQ 112..131
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047177"
FT VAR_SEQ 132..166
FT /note="GYRDGNNSEASGPYRRGGRGSFRGCRGGFGLGSPN -> D (in isoform
FT 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011197"
FT VAR_SEQ 209..225
FT /note="GGYKGLNEEVITGSGKN -> D (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046133"
FT VARIANT 148
FT /note="G -> D (in dbSNP:rs2306259)"
FT /id="VAR_019574"
FT VARIANT 287
FT /note="I -> V (in dbSNP:rs2305123)"
FT /id="VAR_052159"
FT CONFLICT 240
FT /note="Q -> R (in Ref. 3; BAG52716)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="Q -> K (in Ref. 6; AAH47455)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="I -> T (in Ref. 1; AAF86585)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="Q -> R (in Ref. 1; AAF86585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 79308 MW; 6D313DD98B177067 CRC64;
MGDEDWEAEI NPHMSSYVPI FEKDRYSGEN GDNFNRTPAS SSEMDDGPSR RDHFMKSGFA
SGRNFGNRDA GECNKRDNTS TMGGFGVGKS FGNRGFSNSR FEDGDSSGFW RESSNDCEDN
PTRNRGFSKR GGYRDGNNSE ASGPYRRGGR GSFRGCRGGF GLGSPNNDLD PDECMQRTGG
LFGSRRPVLS GTGNGDTSQS RSGSGSERGG YKGLNEEVIT GSGKNSWKSE AEGGESSDTQ
GPKVTYIPPP PPEDEDSIFA HYQTGINFDK YDTILVEVSG HDAPPAILTF EEANLCQTLN
NNIAKAGYTK LTPVQKYSIP IILAGRDLMA CAQTGSGKTA AFLLPILAHM MHDGITASRF
KELQEPECII VAPTRELVNQ IYLEARKFSF GTCVRAVVIY GGTQLGHSIR QIVQGCNILC
ATPGRLMDII GKEKIGLKQI KYLVLDEADR MLDMGFGPEM KKLISCPGMP SKEQRQTLMF
SATFPEEIQR LAAEFLKSNY LFVAVGQVGG ACRDVQQTVL QVGQFSKREK LVEILRNIGD
ERTMVFVETK KKADFIATFL CQEKISTTSI HGDREQRERE QALGDFRFGK CPVLVATSVA
ARGLDIENVQ HVINFDLPST IDEYVHRIGR TGRCGNTGRA ISFFDLESDN HLAQPLVKVL
TDAQQDVPAW LEEIAFSTYI PGFSGSTRGN VFASVDTRKG KSTLNTAGFS SSQAPNPVDD
ESWD
