DOM_DROME
ID DOM_DROME Reviewed; 3198 AA.
AC Q9NDJ2; Q7YZ94; Q95TN6; Q968U6; Q9I7V8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Helicase domino;
DE EC=3.6.4.-;
GN Name=dom; ORFNames=CG9696;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=11262242; DOI=10.1242/dev.128.8.1429;
RA Ruhf M.-L., Braun A., Papoulas O., Tamkun J.W., Randsholt N., Meister M.;
RT "The domino gene of Drosophila encodes novel members of the SWI2/SNF2
RT family of DNA-dependent ATPases, which contribute to the silencing of
RT homeotic genes.";
RL Development 128:1429-1441(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING (ISOFORMS AND B).
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 782-2046 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE TIP60 COMPLEX.
RX PubMed=15528408; DOI=10.1126/science.1103455;
RA Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT "Acetylation by Tip60 is required for selective histone variant exchange at
RT DNA lesions.";
RL Science 306:2084-2087(2004).
RN [6]
RP FUNCTION.
RX PubMed=16024792; DOI=10.1128/mcb.25.15.6559-6569.2005;
RA Eissenberg J.C., Wong M., Chrivia J.C.;
RT "Human SRCAP and Drosophila melanogaster DOM are homologs that function in
RT the notch signaling pathway.";
RL Mol. Cell. Biol. 25:6559-6569(2005).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16322456; DOI=10.1126/science.1120140;
RA Xi R., Xie T.;
RT "Stem cell self-renewal controlled by chromatin remodeling factors.";
RL Science 310:1487-1489(2005).
RN [8]
RP FUNCTION.
RX PubMed=16508010; DOI=10.1128/mcb.26.6.2347-2359.2006;
RA Gause M., Eissenberg J.C., Macrae A.F., Dorsett M., Misulovin Z.,
RA Dorsett D.;
RT "Nipped-A, the Tra1/TRRAP subunit of the Drosophila SAGA and Tip60
RT complexes, has multiple roles in Notch signaling during wing development.";
RL Mol. Cell. Biol. 26:2347-2359(2006).
RN [9]
RP FUNCTION.
RX PubMed=17517653; DOI=10.1073/pnas.0610279104;
RA Lu J., Ruhf M.-L., Perrimon N., Leder P.;
RT "A genome-wide RNA interference screen identifies putative chromatin
RT regulators essential for E2F repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9381-9386(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656; SER-664; SER-666;
RP THR-729; SER-733; SER-736; SER-744 AND THR-838, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Mediates the ATP-dependent exchange of unmodified histone
CC H2AV for its phosphorylated and acetylated form H2AVK5acS138ph, leading
CC to transcriptional regulation of selected genes by chromatin
CC remodeling. Involved in Notch signaling. Represses E2F target genes.
CC Required for somatic stem cell self-renewal but not for germline stem
CC cell self-renewal. Involved in oogenesis. {ECO:0000269|PubMed:11262242,
CC ECO:0000269|PubMed:15528408, ECO:0000269|PubMed:16024792,
CC ECO:0000269|PubMed:16322456, ECO:0000269|PubMed:16508010,
CC ECO:0000269|PubMed:17517653}.
CC -!- SUBUNIT: Component of the Tip60 chromatin-remodeling complex which
CC contains Domino, Tip60, Tra1, Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3,
CC Act87E, BAP55, Mrg15, MrgBP, Gas41 and YL-1.
CC {ECO:0000269|PubMed:15528408}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:11262242}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9NDJ2-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9NDJ2-2; Sequence=VSP_029443;
CC -!- TISSUE SPECIFICITY: Isoform B is present at high levels in ovary, in
CC follicle cells, nurse cells and oocyte. Isoform B is also present in
CC germline and somatic stem cells from the germarium. Isoform A is
CC undetectable in adult ovary (at protein level).
CC {ECO:0000269|PubMed:11262242, ECO:0000269|PubMed:16322456}.
CC -!- DEVELOPMENTAL STAGE: Isoform A and isoform B are present in 0-12 hours
CC embryonic extracts. During embryonic development, isoform A expression
CC is restricted to the developing nervous system, whereas isoform B is
CC ubiquitously expressed. During postembryonic development, isoform B is
CC found in brain, imaginal disks, lymph glands and salivary glands and
CC isoform A is found in some brain regions, photoreceptor cells and
CC sensory organ precursors (at protein level).
CC {ECO:0000269|PubMed:11262242}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13882.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF076776; AAF82185.1; -; mRNA.
DR EMBL; AF254373; AAK53539.1; -; mRNA.
DR EMBL; AE013599; AAM70871.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM70872.2; -; Genomic_DNA.
DR EMBL; AY058653; AAL13882.1; ALT_INIT; mRNA.
DR RefSeq; NP_524833.2; NM_080094.4. [Q9NDJ2-1]
DR RefSeq; NP_788424.1; NM_176244.3. [Q9NDJ2-2]
DR SMR; Q9NDJ2; -.
DR BioGRID; 69802; 98.
DR DIP; DIP-60953N; -.
DR IntAct; Q9NDJ2; 8.
DR STRING; 7227.FBpp0071529; -.
DR iPTMnet; Q9NDJ2; -.
DR PaxDb; Q9NDJ2; -.
DR PRIDE; Q9NDJ2; -.
DR EnsemblMetazoa; FBtr0071603; FBpp0071529; FBgn0020306. [Q9NDJ2-1]
DR EnsemblMetazoa; FBtr0071604; FBpp0071530; FBgn0020306. [Q9NDJ2-2]
DR GeneID; 45655; -.
DR KEGG; dme:Dmel_CG9696; -.
DR UCSC; CG9696-RA; d. melanogaster. [Q9NDJ2-1]
DR CTD; 45655; -.
DR FlyBase; FBgn0020306; dom.
DR VEuPathDB; VectorBase:FBgn0020306; -.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000167340; -.
DR InParanoid; Q9NDJ2; -.
DR PhylomeDB; Q9NDJ2; -.
DR SignaLink; Q9NDJ2; -.
DR BioGRID-ORCS; 45655; 0 hits in 3 CRISPR screens.
DR ChiTaRS; jumu; fly.
DR GenomeRNAi; 45655; -.
DR PRO; PR:Q9NDJ2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0020306; Expressed in egg cell and 27 other tissues.
DR ExpressionAtlas; Q9NDJ2; baseline and differential.
DR Genevisible; Q9NDJ2; DM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IPI:FlyBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:FlyBase.
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:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0070983; P:dendrite guidance; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0030097; P:hemopoiesis; TAS:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0035207; P:negative regulation of hemocyte proliferation; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0035222; P:wing disc pattern formation; IGI:FlyBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell cycle; Chromatin regulator;
KW Coiled coil; Developmental protein; Differentiation; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Oogenesis; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..3198
FT /note="Helicase domino"
FT /id="PRO_0000311238"
FT DOMAIN 507..579
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 926..1091
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1662..1812
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2136..2205
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2061..2100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2318..2362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..212
FT /evidence="ECO:0000255"
FT COILED 666..696
FT /evidence="ECO:0000255"
FT COILED 741..784
FT /evidence="ECO:0000255"
FT COILED 1951..1996
FT /evidence="ECO:0000255"
FT COMPBIAS 258..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..846
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2322..2348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 939..946
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 838
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2009..3198
FT /note="WISRNTMEQMPMWCPPTPPQDNDNDIYIDYSLSFMYELEPIAETDLPPVYVR
FT KEHKRSRTDAGYDGSRRPNKMRREDNYVPPRSLFDRPTPQLARLRRELKSQRFRGSFKP
FT NMPIPGLKPQLPTKPLTEPEAMAEWCVFEDMAILHVLVNLQGLPCSLMLLSPGQTPNWD
FT LVSEMVNFCSKTYRSARQCRWRYETHIQPREEGKVVESPKKQKKLKPTLRTEYLKSPLR
FT YLRTTQLYVSDNNASFYKTMRSRFDSIKTAYLKKAPPPKRQFSAPSLMNPKHMEVLQEF
FT GILNYDQPVSPQNIAAMKANKIREKQRGQQMSQPPVGVGVVQQMQQQSQQQQQPAPPPL
FT PQQQQPQQVVQQVQQQQQQQQQQQQQQVVQQQLPTVSNVQQTLPVQQTVELVQQQPTTT
FT TTVAVPAAGGQLQQLQIQHLTSSNVSPGQQTAILLHQPQQQLRTHPGQGGQSNTQQLVK
FT TIVGTSSSLTAGQLQQLAQQSAVASGGQSSVSVVLTTPVQTLPSVVQPQIGSGAQIVSI
FT SSQTLPVNSSPQLGSIVQTQSLPQVVSVSTLPTVGTVLTTTANQPQQQHQTTAVTTLNT
FT TMLRGQRIVSTAAGNTLQQRTTAGGQSIVSMPNLGQGASPSQFQTQLRLAAVPTSPATQ
FT TTQLVTTKGIPVSALQQGGKTTVIPVTQQSGGAHIQLYRQRSLKVLQTTTQAVPSGSAG
FT ATGATANLVQAGGTIIQASNMATHVTSQKVAVSGMPGTSTTVQAGNVVSSVQMHGQART
FT QFIKQMAAGKQQLQRQVVSADGTTTTTAAGDMLLVKRHNILAAQKAQQASGALFTTTTG
FT QQQQQQQQQGQLPVAGQPQQVTQHQIASLVKASTAAAASGSSVNAGGVTVSATNPTVQA
FT GSVNMTLPQLKPGSQIKVTMPNQMRHLQMQQQLTMPRKISRMTQLVSASGQPTATNIIT
FT TTGPQQQQQGVTVSGGGTLPTVASQQQQQQHQQKVGGGNSVQAQLLHIQNTKGLSNSVT
FT MQQIQQVMRSGQQGTLATTNLVLGKTSVGRVIPVSVASQANQRQTIQVVSAASAQALAA
FT GNLRTHVAGPSIASTLKVAAPGSAGGQTTQQTLIAALQHNQRQNASPVRLQTTAGGNLL
FT AVVQQQQQQQHTSIAGPTAGPAEVMTITQTTTTLPTVGSLQQQQQQQQQQGGISQPTTQ
FT QVRKLVQKKILIRSEKE -> NTKTDSNSNKRRLVRENRRNSAQKLSRSVSSHSTGSNN
FT KNSKSATTRGNSQNSLNQTVPVGSGISRVNRTGAGVSSSSRGKSNSTKSTGKGTDAAPQ
FT VRRQTRLHSLGAVNMASARTPPTRKTTRTALAASAAASTLEDASLIVEERPKRQSANIA
FT MSKMMKTPFKQNVPSNISIKTTPPKRGRRDSVAAAATRSKLLERRATIAAPLKHMDDES
FT DQDEEEQEEQESEEDTEGEEANATVDDDEEGEEELASLDEETIQTGSQTNDEEDDDEEE
FT VGEEGMVDIDTEDSEADVKSSSTYGTAADGKPEEAESLDGWDAHDQVQDTTMTSSTYYN
FT VSEESDTDEHHDSKAEAKEPPQNSDKSDESEAVGHTPRTRSRGTVKINLWTLDVSPVAN
FT ALNKSSANRSLKKAPRTESTPKESQSEPRRKITQPKLPKKEETNNKSNSNIGTLHRWIS
FT KSPRVMLRSTPVTAASASSSAAVSGVSGGNASSSGTAR (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11262242"
FT /id="VSP_029443"
FT CONFLICT 1598
FT /note="V -> G (in Ref. 1; AAF82185/AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611..1612
FT /note="SS -> LL (in Ref. 1; AAF82185/AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT 1619
FT /note="Q -> P (in Ref. 1; AAF82185/AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT 1631
FT /note="P -> A (in Ref. 1; AAF82185/AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT 2157
FT /note="V -> G (in Ref. 1; AAF82185)"
FT /evidence="ECO:0000305"
FT CONFLICT 2198
FT /note="R -> P (in Ref. 1; AAF82185)"
FT /evidence="ECO:0000305"
FT CONFLICT 2340
FT /note="M -> MQQQSQQ (in Ref. 1; AAF82185)"
FT /evidence="ECO:0000305"
FT CONFLICT 2369..2371
FT /note="Missing (in Ref. 1; AAF82185)"
FT /evidence="ECO:0000305"
FT CONFLICT 2514
FT /note="T -> S (in Ref. 1; AAF82185)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2127
FT /note="P -> A (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2174
FT /note="K -> N (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2180
FT /note="N -> T (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2222
FT /note="E -> D (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2229
FT /note="E -> D (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2287
FT /note="G -> E (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2471
FT /note="V -> G (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NDJ2-2:2474
FT /note="A -> T (in Ref. 1; AAK53539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3198 AA; 350239 MW; E65C3E86E1E64AB7 CRC64;
MNEGNSAGGG HEGLSPAPPA VPDRVTPHST EISVAPANST STTVRAAGSV GAALPATRHH
QHIATQVKGI ASSSSKQQKQ LASAQLPVPL SPLPQQQQQT AEATAAAAAP AHSNVSVSSS
TIEASVLPPQ AKRQRLDDNE DRTSAASIVG PAESSNIVSS LLPASVASSS EVGGLSSTAL
QDLNALKKRI LQQKLQILRN LKERHLENVS EYFYLQNGGS MMDYPAWRKK TPTPQFISYS
NANRIDQLIH EDKPSTSAAA AAAQNQKYTT QQTDSVESSL VSGIGTGATK GAPLDGNISN
STVKTNTQSQ VPSKIGSFTE STPAATESNS STTVPGTATS GAATSTSATS AEASGNVLAV
EAEIKIPAVG ATPVAISTKL PAAVVQLTQQ GGTPLLPCNT SAGSTALRRP QGQNNASSGS
AAASGGGGSL TPTPLYTGNG PAALGGSGGL TPGTPTSGSL LSPALGGGSG TPNSAAQEFS
FKAKQEVYVM QRISELQREG LWTERRLPKL QEPSRPKAHW DYLLEEMVWL AADFAQERKW
KKNAAKKCAK MVQKYFQDKA TAAQRAEKAQ ELQLKRVASF IAREVKSFWS NVEKLVEYKH
QTKIEEKRKQ ALDQHLSFIV DQTEKFSQQL VEGMNKSVAD TPSLNSSRLT SPKRESDDDF
RPESGSEDDE ETIAKAEEDA ADVKEEVTAL AKESEMDFDD FLNDLPPGYL ENRDKLMKEE
QSSAIKTETP DDSDDSEFEA KEASDDDENT ISKQEEAEQE IDHKKEIDEL EADNDLSVEQ
LLAKYKSEQP PSPKRRKLAP RDPELDSDDD STAVDSTEES EDAATEDEED LSTVKTDTDM
EEQDEQEDGL KSLMADADAT SGAAGSGSTA GASGNKDDML NDAAALAESL QPKGNTLSST
NVVTPVPFLL KHSLREYQHI GLDWLVTMNE RKLNGILADE MGLGKTIQTI ALLAHLACAK
GNWGPHLIVV PSSVMLNWEM EFKKWCPGFK ILTYYGSQKE RKLKRVGWTK PNAFHVCITS
YKLVVQDQQS FRRKKWKYLI LDEAQNIKNF KSQRWQLLLN FSTERRLLLT GTPLQNDLME
LWSLMHFLMP YVFSSHREFK EWFSNPMTGM IEGNMEYNET LITRLHKVIR PFLLRRLKKE
VEKQMPKKYE HVITCRLSNR QRYLYEDFMS RAKTRETLQT GNLLSVINVL MQLRKVCNHP
NMFEARPTIS PFQMDGITFH TPRLVCDIME YDPFTQINLE TLNLLLLHLE QTMTAYVSHK
SRLLAPPRKL IEDIDTAPLP APRCPNGKYR FHIRVRSAEL AQRIKLNAVK VGASPAMRLE
GSKIMPMRNL LPSGRVLKRV SASINPVNMA LKPVVINSVV TTTSSSTTAS SPTGALSVLS
NSKLLGARSQ INAPTPAKVA KTMQDGKPFF YLTPATNSGA AGARLTLTSK TTASASTTTS
RTTVTASTTS GQQLIRDPIV KDLATHVKST VQKQSIANGK TEPEEETEAE DPYKVQELIQ
MRKEQRLAAL KRMAMINRRR TDATPIYGED CREAIQRCMQ ATRSLKRSTW QTRGYANCCT
AMAHRNGWSL NHLLKSFEER CADLKPVFAN FVIYVPSVCA PRIRRYVQNL SSTHWQHEQR
IENIVDQALR PKLALLHPII SEMTTKFPDP RLIQYDCGKL QTMDRLLRQL KVNGHRVLIF
TQMTKMLDVL EAFLNYHGHI YLRLDGSTRV EQRQILMERF NGDKRIFCFI LSTRSGGVGI
NLTGADTVIF YDSDWNPTMD AQAQDRCHRI GQTRDVHIYR LVSERTIEVN ILKKANQKRM
LSDMAIEGGN FTTTYFKSST IKDLFTMEQS EQDESSQEKS ENKDRIVATT TLSDTPSTVV
ETEKQSLRAF EHALAAAEDE QDVQATKTAK AEVAADLAEF DENIPIATED PNAEGGPQVE
LSKADLEMQN LVKQLSPIER YAMRFVEETG AAWTAEQLRA AEAELEAQKR EWEANRLAAM
HKEEELLKQE TEAEEMLTYS RKDSSNQVWI SRNTMEQMPM WCPPTPPQDN DNDIYIDYSL
SFMYELEPIA ETDLPPVYVR KEHKRSRTDA GYDGSRRPNK MRREDNYVPP RSLFDRPTPQ
LARLRRELKS QRFRGSFKPN MPIPGLKPQL PTKPLTEPEA MAEWCVFEDM AILHVLVNLQ
GLPCSLMLLS PGQTPNWDLV SEMVNFCSKT YRSARQCRWR YETHIQPREE GKVVESPKKQ
KKLKPTLRTE YLKSPLRYLR TTQLYVSDNN ASFYKTMRSR FDSIKTAYLK KAPPPKRQFS
APSLMNPKHM EVLQEFGILN YDQPVSPQNI AAMKANKIRE KQRGQQMSQP PVGVGVVQQM
QQQSQQQQQP APPPLPQQQQ PQQVVQQVQQ QQQQQQQQQQ QQVVQQQLPT VSNVQQTLPV
QQTVELVQQQ PTTTTTVAVP AAGGQLQQLQ IQHLTSSNVS PGQQTAILLH QPQQQLRTHP
GQGGQSNTQQ LVKTIVGTSS SLTAGQLQQL AQQSAVASGG QSSVSVVLTT PVQTLPSVVQ
PQIGSGAQIV SISSQTLPVN SSPQLGSIVQ TQSLPQVVSV STLPTVGTVL TTTANQPQQQ
HQTTAVTTLN TTMLRGQRIV STAAGNTLQQ RTTAGGQSIV SMPNLGQGAS PSQFQTQLRL
AAVPTSPATQ TTQLVTTKGI PVSALQQGGK TTVIPVTQQS GGAHIQLYRQ RSLKVLQTTT
QAVPSGSAGA TGATANLVQA GGTIIQASNM ATHVTSQKVA VSGMPGTSTT VQAGNVVSSV
QMHGQARTQF IKQMAAGKQQ LQRQVVSADG TTTTTAAGDM LLVKRHNILA AQKAQQASGA
LFTTTTGQQQ QQQQQQGQLP VAGQPQQVTQ HQIASLVKAS TAAAASGSSV NAGGVTVSAT
NPTVQAGSVN MTLPQLKPGS QIKVTMPNQM RHLQMQQQLT MPRKISRMTQ LVSASGQPTA
TNIITTTGPQ QQQQGVTVSG GGTLPTVASQ QQQQQHQQKV GGGNSVQAQL LHIQNTKGLS
NSVTMQQIQQ VMRSGQQGTL ATTNLVLGKT SVGRVIPVSV ASQANQRQTI QVVSAASAQA
LAAGNLRTHV AGPSIASTLK VAAPGSAGGQ TTQQTLIAAL QHNQRQNASP VRLQTTAGGN
LLAVVQQQQQ QQHTSIAGPT AGPAEVMTIT QTTTTLPTVG SLQQQQQQQQ QQGGISQPTT
QQVRKLVQKK ILIRSEKE
