OVO_DROME
ID OVO_DROME Reviewed; 1351 AA.
AC P51521; E1JJE5; O02468; Q2PE28; Q8MPN4; Q8SX56; Q8T8L9; Q9W4F0; Q9W4F1;
AC Q9W4F2; Q9XZU4; Q9Y046;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Transcriptional regulator ovo {ECO:0000303|PubMed:7935398};
DE AltName: Full=Transcriptional repressor shavenbaby {ECO:0000303|PubMed:20647469};
DE Short=Transcriptional repressor svb {ECO:0000303|PubMed:20647469};
DE Contains:
DE RecName: Full=Transcriptional activator shavenbaby {ECO:0000303|PubMed:20647469};
DE Short=Transcriptional activator svb {ECO:0000303|PubMed:20647469};
GN Name=ovo {ECO:0000303|PubMed:7935398, ECO:0000312|FlyBase:FBgn0003028};
GN Synonyms=svb {ECO:0000303|PubMed:7935398, ECO:0000312|FlyBase:FBgn0003028};
GN ORFNames=CG6824 {ECO:0000312|FlyBase:FBgn0003028};
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] (ISOFORM D), SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=7935398; DOI=10.1128/mcb.14.10.6809-6818.1994;
RA Garfinkel M.D., Wang J., Liang Y., Mahowald A.P.;
RT "Multiple products from the shavenbaby-ovo gene region of Drosophila
RT melanogaster: relationship to genetic complexity.";
RL Mol. Cell. Biol. 14:6809-6818(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION (ISOFORMS C AND D),
RP DEVELOPMENTAL STAGE (ISOFORMS C AND D), AND MUTAGENESIS OF LYS-208; LYS-226
RP AND VAL-305.
RX PubMed=10648246; DOI=10.1242/dev.127.4.881;
RA Andrews J., Garcia-Estefania D., Delon I., Lu J., Mevel-Ninio M.T.M.,
RA Spierer A., Payre F., Pauli D., Oliver B.;
RT "OVO transcription factors function antagonistically in the Drosophila
RT female germline.";
RL Development 127:881-892(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12915226; DOI=10.1016/s0925-4773(03)00081-9;
RA Delon I., Chanut-Delalande H., Payre F.;
RT "The Ovo/Shavenbaby transcription factor specifies actin remodelling during
RT epidermal differentiation in Drosophila.";
RL Mech. Dev. 120:747-758(2003).
RN [4]
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 [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-547 (ISOFORMS B/D AND C), FUNCTION,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LYS-208;
RP LYS-226 AND VAL-305.
RX PubMed=9012532; DOI=10.1242/dev.122.12.4131;
RA Mevel-Ninio M.T.M., Fouilloux E., Guenal I., Vincent A.;
RT "The three dominant female-sterile mutations of the Drosophila ovo gene are
RT point mutations that create new translation-initiator AUG codons.";
RL Development 122:4131-4138(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-1351 (ISOFORM B), FUNCTION
RP (ISOFORM D), SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=1712294; DOI=10.1002/j.1460-2075.1991.tb07762.x;
RA Mevel-Ninio M.T.M., Terracol R., Kafatos F.C.;
RT "The ovo gene of Drosophila encodes a zinc finger protein required for
RT female germ line development.";
RL EMBO J. 10:2259-2266(1991).
RN [9]
RP PROTEIN SEQUENCE OF 446-451, FUNCTION (TRANSCRIPTIONAL ACTIVATOR
RP SHAVENBABY), SUBCELLULAR LOCATION (TRANSCRIPTIONAL ACTIVATOR SHAVENBABY;
RP ISOFORMS B; C AND D), CLEAVAGE, AND DEVELOPMENTAL STAGE (ISOFORM B).
RX PubMed=20647469; DOI=10.1126/science.1188158;
RA Kondo T., Plaza S., Zanet J., Benrabah E., Valenti P., Hashimoto Y.,
RA Kobayashi S., Payre F., Kageyama Y.;
RT "Small peptides switch the transcriptional activity of Shavenbaby during
RT Drosophila embryogenesis.";
RL Science 329:336-339(2010).
RN [10]
RP MUTAGENESIS OF LYS-208; LYS-226 AND VAL-305, AND DEVELOPMENTAL STAGE.
RX PubMed=17246162; DOI=10.1093/genetics/105.2.309;
RA Busson D., Gans M., Komitopoulou K., Masson M.;
RT "Genetic Analysis of Three Dominant Female-Sterile Mutations Located on the
RT X Chromosome of DROSOPHILA MELANOGASTER.";
RL Genetics 105:309-325(1983).
RN [11]
RP FUNCTION (ISOFORM D), AND DISRUPTION PHENOTYPE (ISOFORM D).
RX PubMed=3428601; DOI=10.1101/gad.1.9.913;
RA Oliver B., Perrimon N., Mahowald A.P.;
RT "The ovo locus is required for sex-specific germ line maintenance in
RT Drosophila.";
RL Genes Dev. 1:913-923(1987).
RN [12]
RP FUNCTION (ISOFORM D).
RX PubMed=2116356; DOI=10.1093/genetics/125.3.535;
RA Oliver B., Pauli D., Mahowald A.P.;
RT "Genetic evidence that the ovo locus is involved in Drosophila germ line
RT sex determination.";
RL Genetics 125:535-550(1990).
RN [13]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE (ISOFORMS B AND D).
RX PubMed=7748792; DOI=10.1016/0925-4773(94)00305-7;
RA Mevel-Ninio M.T.M., Terracol R., Salles C., Vincent A., Payre F.;
RT "ovo, a Drosophila gene required for ovarian development, is specifically
RT expressed in the germline and shares most of its coding sequences with
RT shavenbaby, a gene involved in embryo patterning.";
RL Mech. Dev. 49:83-95(1995).
RN [14]
RP FUNCTION (ISOFORM D), AND DISRUPTION PHENOTYPE (ISOFORM D).
RX PubMed=8652413; DOI=10.1016/0925-4773(95)00477-7;
RA Staab S., Steinmann-Zwicky M.;
RT "Female germ cells of Drosophila require zygotic ovo and otu product for
RT survival in larvae and pupae respectively.";
RL Mech. Dev. 54:205-210(1996).
RN [15]
RP FUNCTION (ISOFORM D).
RX PubMed=9634487; DOI=10.1007/s004270050175;
RA Lue J., Andrews J., Pauli D., Oliver B.;
RT "Drosophila OVO zinc-finger protein regulates ovo and ovarian tumor target
RT promoters.";
RL Dev. Genes Evol. 208:213-222(1998).
RN [16]
RP FUNCTION (ISOFORM D).
RX PubMed=10525184; DOI=10.1016/s0925-4773(99)00167-7;
RA Hinson S., Pettus J., Nagoshi R.N.;
RT "Regulatory and functional interactions between ovarian tumor and ovo
RT during Drosophila oogenesis.";
RL Mech. Dev. 88:3-14(1999).
RN [17]
RP FUNCTION.
RX PubMed=10421370; DOI=10.1038/22330;
RA Payre F., Vincent A., Carreno S.;
RT "ovo/svb integrates Wingless and DER pathways to control epidermis
RT differentiation.";
RL Nature 400:271-275(1999).
RN [18]
RP DOMAIN, AND DNA-BINDING.
RX PubMed=10637336; DOI=10.1093/nar/28.3.826;
RA Lee S., Garfinkel M.D.;
RT "Characterization of Drosophila OVO protein DNA binding specificity using
RT random DNA oligomer selection suggests zinc finger degeneration.";
RL Nucleic Acids Res. 28:826-834(2000).
RN [19]
RP FUNCTION (ISOFORM D), AND DNA-BINDING.
RX PubMed=11290304; DOI=10.1242/dev.128.9.1671;
RA Lu J., Oliver B.;
RT "Drosophila OVO regulates ovarian tumor transcription by binding unusually
RT near the transcription start site.";
RL Development 128:1671-1686(2001).
RN [20]
RP FUNCTION (ISOFORM D), AND DEVELOPMENTAL STAGE (ISOFORM C AND D).
RX PubMed=12051822; DOI=10.1006/dbio.2002.0659;
RA Salles C., Mevel-Ninio M., Vincent A., Payre F.;
RT "A germline-specific splicing generates an extended ovo protein isoform
RT required for Drosophila oogenesis.";
RL Dev. Biol. 246:366-376(2002).
RN [21]
RP ALTERNATIVE PROMOTER USAGE, AND DEVELOPMENTAL STAGE (ISOFORMS C AND D).
RX PubMed=15371353; DOI=10.1534/genetics.104.033118;
RA Bielinska B., Lue J., Sturgill D., Oliver B.;
RT "Core promoter sequences contribute to ovo-B regulation in the Drosophila
RT melanogaster germline.";
RL Genetics 169:161-172(2005).
RN [22]
RP FUNCTION (ISOFORM B), AND DEVELOPMENTAL STAGE (ISOFORM B).
RX PubMed=21527259; DOI=10.1016/j.ydbio.2011.03.033;
RA Pueyo J.I., Couso J.P.;
RT "Tarsal-less peptides control Notch signalling through the Shavenbaby
RT transcription factor.";
RL Dev. Biol. 355:183-193(2011).
RN [23]
RP FUNCTION (ISOFORM B), SUBCELLULAR LOCATION (ISOFORM B), AND DEVELOPMENTAL
RP STAGE (ISOFORM B).
RX PubMed=25344753; DOI=10.1038/ncb3052;
RA Chanut-Delalande H., Hashimoto Y., Pelissier-Monier A., Spokony R., Dib A.,
RA Kondo T., Bohere J., Niimi K., Latapie Y., Inagaki S., Dubois L.,
RA Valenti P., Polesello C., Kobayashi S., Moussian B., White K.P., Plaza S.,
RA Kageyama Y., Payre F.;
RT "Pri peptides are mediators of ecdysone for the temporal control of
RT development.";
RL Nat. Cell Biol. 16:1035-1044(2014).
RN [24]
RP FUNCTION (ISOFORM B), INTERACTION WITH UBR3 (ISOFORM B), SUBCELLULAR
RP LOCATION (ISOFORMS B; C AND D), CLEAVAGE (ISOFORM B), UBIQUITINATION
RP (ISOFORM B), AND MUTAGENESIS OF LYS-3; LYS-8 AND LYS-28.
RX PubMed=26383956; DOI=10.1126/science.aac5677;
RA Zanet J., Benrabah E., Li T., Pelissier-Monier A., Chanut-Delalande H.,
RA Ronsin B., Bellen H.J., Payre F., Plaza S.;
RT "Pri sORF peptides induce selective proteasome-mediated protein
RT processing.";
RL Science 349:1356-1358(2015).
RN [25]
RP FUNCTION (ISOFORM B), AND DISRUPTION PHENOTYPE (ISOFORM B).
RX PubMed=28506986; DOI=10.1242/dev.150169;
RA Rizzo N.P., Bejsovec A.;
RT "SoxNeuro and Shavenbaby act cooperatively to shape denticles in the
RT embryonic epidermis of Drosophila.";
RL Development 144:2248-2258(2017).
RN [26]
RP FUNCTION (ISOFORMS C AND D), AND DEVELOPMENTAL STAGE (ISOFORMS B; C AND D).
RX PubMed=28059165; DOI=10.1038/srep40056;
RA Hayashi M., Shinozuka Y., Shigenobu S., Sato M., Sugimoto M., Ito S.,
RA Abe K., Kobayashi S.;
RT "Conserved role of Ovo in germline development in mouse and Drosophila.";
RL Sci. Rep. 7:40056-40056(2017).
CC -!- FUNCTION: Transcriptional regulator with essential functions in the
CC germline and soma (PubMed:9012532, PubMed:12915226, PubMed:10421370).
CC Plays an essential role in regulating the formation of apical cell
CC extensions such as denticles and aristae, and initiating cytoskeletal
CC remodeling during epidermal differentiation (PubMed:12915226,
CC PubMed:10421370). {ECO:0000269|PubMed:10421370,
CC ECO:0000269|PubMed:12915226, ECO:0000269|PubMed:9012532}.
CC -!- FUNCTION: [Isoform B]: Transcriptional repressor which functions in
CC postembryonic development (PubMed:21527259, PubMed:26383956). The full-
CC length unprocessed form acts as a transcriptional repressor
CC (Transcriptional repressor svb) (PubMed:26383956).
CC {ECO:0000269|PubMed:21527259, ECO:0000269|PubMed:26383956}.
CC -!- FUNCTION: [Transcriptional activator shavenbaby]: Transcriptional
CC activator which initiates trichome development and also promotes tarsal
CC joint development (PubMed:21527259, PubMed:20647469, PubMed:26383956).
CC Has an essential somatic role regulating the tal-dependent formation of
CC trichomes, and initiating cytoskeletal remodeling during epidermal
CC differentiation (PubMed:20647469, PubMed:21527259, PubMed:25344753,
CC PubMed:26383956). Function with SoxN is required for correct denticle
CC morphogenesis on the embryonic epidermis (PubMed:28506986). SoxN and
CC svb appear to act both independently and in conjunction with each other
CC to activate certain genes involved in denticle morphogenesis; Svb
CC appears to be involved in regulating denticle length whereas SoxN
CC regulates the denticle base circumference (PubMed:28506986). Also
CC functions in the development of other apical cell extensions such as
CC bristles (PubMed:25344753). Also has an important role in tarsal joint
CC development, repressing expression of the N ligand Dl and defining its
CC signaling boundary (PubMed:21527259). {ECO:0000269|PubMed:20647469,
CC ECO:0000269|PubMed:21527259, ECO:0000269|PubMed:25344753,
CC ECO:0000269|PubMed:26383956, ECO:0000269|PubMed:28506986}.
CC -!- FUNCTION: [Isoform C]: Transcriptional repressor which is specifically
CC involved in female germline development, where it functions
CC antagonistically to isoform D (PubMed:10648246, PubMed:28059165).
CC Negatively regulates expression of otu and may also have autoregulatory
CC activity (PubMed:10648246). Negatively regulates expression of piwi in
CC the primordial germ cells (PGCs) (PubMed:28059165).
CC {ECO:0000269|PubMed:10648246, ECO:0000269|PubMed:28059165}.
CC -!- FUNCTION: [Isoform D]: Transcriptional activator which is specifically
CC involved in female germline development, where it functions
CC antagonistically to isoform C (PubMed:10648246, PubMed:1712294,
CC PubMed:3428601, PubMed:8652413). Necessary and sufficient for normal
CC oogenesis (PubMed:1712294, PubMed:12051822). Required in the primordial
CC germ cells (PGCs) for normal development of male and female germline
CC cells (PubMed:28059165). Plays a role in germline sex determination
CC (PubMed:2116356). Binds the promoter DNA and positively regulates the
CC transcription of the otu gene in a stage-specific manner
CC (PubMed:10525184, PubMed:11290304, PubMed:9634487). May have
CC autoregulatory activity (PubMed:11290304, PubMed:9634487).
CC {ECO:0000269|PubMed:10525184, ECO:0000269|PubMed:10648246,
CC ECO:0000269|PubMed:11290304, ECO:0000269|PubMed:12051822,
CC ECO:0000269|PubMed:1712294, ECO:0000269|PubMed:2116356,
CC ECO:0000269|PubMed:28059165, ECO:0000269|PubMed:3428601,
CC ECO:0000269|PubMed:8652413, ECO:0000269|PubMed:9634487}.
CC -!- SUBUNIT: [Isoform B]: Interacts (via N-terminus) with Ubr3; the
CC interaction is mediated by tal. {ECO:0000269|PubMed:26383956}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1712294,
CC ECO:0000269|PubMed:7935398, ECO:0000269|PubMed:9012532}. Nucleus
CC {ECO:0000269|PubMed:1712294, ECO:0000269|PubMed:7748792,
CC ECO:0000269|PubMed:7935398}.
CC -!- SUBCELLULAR LOCATION: [Transcriptional activator shavenbaby]: Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:20647469}. Note=Diffuse nucleoplasmic
CC distribution. {ECO:0000269|PubMed:20647469}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Nucleus
CC {ECO:0000269|PubMed:20647469, ECO:0000269|PubMed:25344753,
CC ECO:0000269|PubMed:26383956}. Note=Localizes to the nuclear foci.
CC {ECO:0000269|PubMed:20647469}.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Nucleus
CC {ECO:0000269|PubMed:20647469, ECO:0000269|PubMed:26383956}.
CC Note=Localizes to the nuclear foci. {ECO:0000269|PubMed:20647469}.
CC -!- SUBCELLULAR LOCATION: [Isoform D]: Cytoplasm
CC {ECO:0000269|PubMed:7748792}. Nucleus {ECO:0000269|PubMed:26383956,
CC ECO:0000269|PubMed:9012532}. Nucleus, nucleoplasm
CC {ECO:0000303|PubMed:20647469}. Note=Diffuse nucleoplasmic distribution
CC (PubMed:20647469). Expressed in germ cell nuclei throughout oocyte
CC development (PubMed:7748792). Not expressed in nuclei of stage 9
CC oocytes but is expressed in nurse cell nuclei (PubMed:7748792). In
CC stage 12 oocytes it is also detected in the ooplasm (PubMed:7748792).
CC {ECO:0000269|PubMed:20647469, ECO:0000269|PubMed:7748792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=B {ECO:0000312|FlyBase:FBgn0003028}; Synonyms=E
CC {ECO:0000312|FlyBase:FBgn0003028}, svb {ECO:0000303|PubMed:10648246,
CC ECO:0000303|PubMed:12051822, ECO:0000303|PubMed:26383956};
CC IsoId=P51521-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0003028};
CC IsoId=P51521-2; Sequence=VSP_015268, VSP_015270, VSP_015271;
CC Name=C {ECO:0000312|FlyBase:FBgn0003028}; Synonyms=ovoA
CC {ECO:0000303|PubMed:10648246, ECO:0000303|PubMed:12051822,
CC ECO:0000303|PubMed:20647469};
CC IsoId=P51521-3; Sequence=VSP_015267, VSP_015269;
CC Name=D {ECO:0000312|FlyBase:FBgn0003028}; Synonyms=ovoB
CC {ECO:0000303|PubMed:10648246, ECO:0000303|PubMed:12051822,
CC ECO:0000303|PubMed:20647469};
CC IsoId=P51521-4; Sequence=VSP_015268, VSP_015271;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:7935398, PubMed:9012532, PubMed:1712294, PubMed:17246162,
CC PubMed:28059165). Isoform B: Expressed in the notum from early pupation
CC to 36 h after puparium formation, disappearing once epidermal cells
CC develop apical extensions (at protein level) (PubMed:25344753). Isoform
CC B: Expressed in the trichomes of stages 11 and 12 embryos and
CC disappears by stage 15 but the cleaved transcriptional activator form
CC svb is still present (at protein level) (PubMed:20647469). Isoform B:
CC Not detected until the blastoderm stage when it is expressed in the
CC head (PubMed:7748792). Isoform B: No expression in the primordial germ
CC cells (PGCs) (PubMed:28059165). Isoform B: In stage 12 embryos,
CC expressed in the trunk, and in stage 14 embryos expressed in the region
CC of denticle belt setae and dorsal hairs (PubMed:7748792). Isoform B:
CC Not detected in the pole cells throughout embryogenesis
CC (PubMed:7748792). Isoform B: Expressed in the pupal tarsal segments in
CC several segmentally separated stripes (PubMed:21527259). Isoform D:
CC Expressed in the germinal stem cells of the germarium and later in the
CC nurse cells (at protein level) (PubMed:7748792). Isoform D: Uniformly
CC expressed in early cleavage and blastoderm stage embryos (at protein
CC level) (PubMed:7748792). Isoform D: At germ band extension (stage 8),
CC expression levels decrease rapidly and becomes localized to the pole
CC cells in the posterior midgut pocket (at protein level)
CC (PubMed:7748792). Isoform D: In stage 14 embryos, expressed in the
CC forming gonads and some dispersed cells presumed to be pole cells lost
CC during cell migration (at protein level) (PubMed:7748792). Isoform D:
CC Expressed in male and female embryos, and in the germ cell in the
CC gonads of male and female larvae (at protein level) (PubMed:7748792).
CC Isoform D: Detected in adults, and in males is expressed in the apical
CC part of each testis (at protein level) (PubMed:7748792). Isoform D:
CC Expressed during early oogenesis in all female germline cells with
CC slightly lower expression in early egg chambers (stages 2-4)
CC (PubMed:10648246, PubMed:15371353). Isoform D: Weakly expressed in the
CC apex of the testis (PubMed:12051822, PubMed:15371353). Isoform D:
CC Expression levels in PGCs remain constant from stage 4 to stage 11, but
CC decrease from stage 12 to stage 17 (PubMed:28059165). Isoform C: Weakly
CC expressed in female germline stem cells and dividing cystocytes, and is
CC very weak in early to middle stages of egg chamber differentiation
CC (PubMed:10648246, PubMed:15371353). Isoform C: Expression levels are
CC highest from middle to late stages of egg maturity but this is still
CC relatively weak compared to isoform D (PubMed:10648246). Isoform C:
CC Expressed in PGCs throughout embryogenesis but at a much lower level
CC than isoform D (PubMed:28059165). Isoform C: Weakly expressed in the
CC apex of the testis (PubMed:12051822, PubMed:15371353).
CC {ECO:0000269|PubMed:10648246, ECO:0000269|PubMed:12051822,
CC ECO:0000269|PubMed:15371353, ECO:0000269|PubMed:1712294,
CC ECO:0000269|PubMed:17246162, ECO:0000269|PubMed:20647469,
CC ECO:0000269|PubMed:21527259, ECO:0000269|PubMed:25344753,
CC ECO:0000269|PubMed:28059165, ECO:0000269|PubMed:7748792,
CC ECO:0000269|PubMed:7935398, ECO:0000269|PubMed:9012532}.
CC -!- DOMAIN: Only 3 of the 4 C2H2-type zinc-fingers are required for DNA-
CC binding. Based on its marked lack of evolutionary conservation, the
CC fourth zinc-finger is unlikely to be required.
CC {ECO:0000269|PubMed:10637336}.
CC -!- PTM: [Isoform B]: N-terminus is proteolytically cleaved and
CC ubiquitinated via a tal-dependent mechanism, leading to the proteolytic
CC degradation of the N-terminus and the production of transcriptional
CC activator shavenbaby, a truncated form with transcriptional activator
CC activity. {ECO:0000269|PubMed:20647469, ECO:0000269|PubMed:26383956}.
CC -!- DISRUPTION PHENOTYPE: Adult lethal (PubMed:12915226). In the rare adult
CC escapers, trichomes are often absent from large areas of the thorax and
CC wing, or they are sparse and atrophied (PubMed:12915226). In the
CC aristae, the central core is shorter and lateral cells either fail to
CC develop or are strongly reduced in size (PubMed:12915226). Embryos
CC display a smooth cuticle with sparse atrophied denticles
CC (PubMed:12915226). Isoform D: No visible phenotype (PubMed:3428601).
CC Isoform D: Males are viable whereas females are sterile and do not lay
CC eggs (PubMed:3428601). Isoform D: Ovaries are atrophic and slightly
CC larger than the oviducts at the posterior end of the ovaries, and egg
CC chambers and germline cells are not visible (PubMed:3428601). Isoform
CC D: In female embryos undergoing gastrulation, pole cells undergo cell
CC death and are consequently either absent or reduced in number
CC (PubMed:3428601). Isoform D: Pole cell morphology and their position in
CC the embryo is unaffected (PubMed:3428601). Isoform D: Embryonic
CC germline cells are unaffected while, in female larvae, germline cells
CC undergo cell death and by the third instar stage, the germline cells in
CC most mutants are either absent or reduced in number whereas, in the
CC remaining mutants, the number of germline cells are not affected
CC (PubMed:8652413). Isoform B: RNAi-mediated knockdown results in reduced
CC expression of miniature (m) in the developing embryo (PubMed:28506986).
CC {ECO:0000269|PubMed:12915226, ECO:0000269|PubMed:28506986,
CC ECO:0000269|PubMed:3428601, ECO:0000269|PubMed:8652413}.
CC -!- MISCELLANEOUS: [Isoform A]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305|PubMed:15371353}.
CC -!- MISCELLANEOUS: [Isoform C]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:15371353}.
CC -!- MISCELLANEOUS: [Isoform D]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:15371353}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; U11383; AAB60216.1; -; mRNA.
DR EMBL; AJ430589; CAD23207.1; -; mRNA.
DR EMBL; AJ430588; CAD23206.1; -; mRNA.
DR EMBL; AE014298; AAF46001.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF46002.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF46003.2; -; Genomic_DNA.
DR EMBL; AE014298; ABC67174.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95210.1; -; Genomic_DNA.
DR EMBL; AY094838; AAM11191.1; -; mRNA.
DR EMBL; AY119649; AAM50303.1; -; mRNA.
DR EMBL; S83520; AAB50918.1; -; Genomic_DNA.
DR EMBL; S83520; AAB50919.1; -; Genomic_DNA.
DR EMBL; X59772; CAB36921.1; ALT_SEQ; Genomic_DNA.
DR PIR; A56038; A56038.
DR PIR; S16356; S16356.
DR RefSeq; NP_001033831.1; NM_001038742.3. [P51521-4]
DR RefSeq; NP_001162673.1; NM_001169202.2. [P51521-1]
DR RefSeq; NP_525077.2; NM_080338.5. [P51521-2]
DR RefSeq; NP_726971.1; NM_167026.4. [P51521-1]
DR RefSeq; NP_726972.1; NM_167027.4. [P51521-3]
DR AlphaFoldDB; P51521; -.
DR BioGRID; 57942; 50.
DR IntAct; P51521; 20.
DR STRING; 7227.FBpp0291128; -.
DR PaxDb; P51521; -.
DR DNASU; 31429; -.
DR EnsemblMetazoa; FBtr0070738; FBpp0070706; FBgn0003028. [P51521-1]
DR EnsemblMetazoa; FBtr0070739; FBpp0070707; FBgn0003028. [P51521-3]
DR EnsemblMetazoa; FBtr0070740; FBpp0070708; FBgn0003028. [P51521-2]
DR EnsemblMetazoa; FBtr0100408; FBpp0099822; FBgn0003028. [P51521-4]
DR EnsemblMetazoa; FBtr0301914; FBpp0291128; FBgn0003028. [P51521-1]
DR GeneID; 31429; -.
DR KEGG; dme:Dmel_CG6824; -.
DR UCSC; CG6824-RD; d. melanogaster.
DR CTD; 31429; -.
DR FlyBase; FBgn0003028; ovo.
DR VEuPathDB; VectorBase:FBgn0003028; -.
DR eggNOG; KOG3576; Eukaryota.
DR GeneTree; ENSGT00940000161363; -.
DR InParanoid; P51521; -.
DR OMA; QHATRNL; -.
DR PhylomeDB; P51521; -.
DR SignaLink; P51521; -.
DR BioGRID-ORCS; 31429; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31429; -.
DR PRO; PR:P51521; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003028; Expressed in cleaving embryo and 40 other tissues.
DR ExpressionAtlas; P51521; baseline and differential.
DR Genevisible; P51521; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:FlyBase.
DR GO; GO:0008343; P:adult feeding behavior; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0048067; P:cuticle pigmentation; IMP:FlyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0018992; P:germ-line sex determination; IMP:UniProtKB.
DR GO; GO:0016348; P:imaginal disc-derived leg joint morphogenesis; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0035316; P:non-sensory hair organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0070896; P:positive regulation of transposon integration; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR027756; Ovo-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10032; PTHR10032; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Activator; Alternative promoter usage; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW DNA-binding; Metal-binding; Nucleus; Oogenesis; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1351
FT /note="Transcriptional regulator ovo"
FT /id="PRO_0000047010"
FT CHAIN 446..1351
FT /note="Transcriptional activator shavenbaby"
FT /evidence="ECO:0000305|PubMed:20647469"
FT /id="PRO_0000441819"
FT ZN_FING 1197..1219
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1225..1247
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1253..1276
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1292..1315
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..31
FT /note="Required for Ubr3 binding and tal-dependent
FT proteolytic processing"
FT /evidence="ECO:0000269|PubMed:26383956"
FT REGION 22..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 445..446
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:20647469"
FT VAR_SEQ 1..501
FT /note="Missing (in isoform A and isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:7935398"
FT /id="VSP_015268"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10648246"
FT /id="VSP_015267"
FT VAR_SEQ 130..138
FT /note="CATGQVQNE -> MNVNKNDLQ (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10648246"
FT /id="VSP_015269"
FT VAR_SEQ 625..677
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015270"
FT VAR_SEQ 1069
FT /note="S -> SVSNPIGQPLNTQSQQQKQGQQITLMKTTRYTEFVEMVSMDVTVKPE
FT LFSELKPEMTEITAEELTLEAETTAAAAAAAAAAAAATTTSATEGTQVLAAAPAPLSSG
FT RKLRGRAKAVAYGSTMITLISTLKSSPEVPATKTVHRTTLRSLATAAAATAAGLLAPSP
FT TVSVLNESKVLQRR (in isoform A and isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:7935398"
FT /id="VSP_015271"
FT MUTAGEN 3
FT /note="K->G: Decreases but does not prevent tal-dependent
FT cleavage. Abolishes tal-dependent cleavage; when associated
FT with G-8. Abolishes tal-dependent cleavage and
FT ubiquitination by Ubr3; when associated with G-8 and G-28."
FT /evidence="ECO:0000269|PubMed:26383956"
FT MUTAGEN 8
FT /note="K->G: No effect on tal-dependent cleavage. Abolishes
FT tal-dependent cleavage; when associated with G-3. Abolishes
FT tal-dependent cleavage and ubiquitination by Ubr3; when
FT associated with G-3 and G-28."
FT /evidence="ECO:0000269|PubMed:26383956"
FT MUTAGEN 28
FT /note="K->G: Abolishes tal-dependent cleavage and
FT ubiquitination by Ubr3; when associated with G-3 and G-8."
FT /evidence="ECO:0000269|PubMed:26383956"
FT MUTAGEN 208
FT /note="K->M: In ovo-D1; dominant antimorphic mutation
FT leading to the creation of a new upstream initiation codon
FT in isoform D. Heterozygous females are sterile. The male
FT germline is unaffected."
FT /evidence="ECO:0000269|PubMed:10648246,
FT ECO:0000269|PubMed:17246162, ECO:0000269|PubMed:9012532"
FT MUTAGEN 226
FT /note="K->M: In ovo-D3; dominant antimorphic mutation
FT leading to the creation of a new upstream initiation codon
FT in isoform D. Heterozygous females are sterile. The male
FT germline is unaffected."
FT /evidence="ECO:0000269|PubMed:10648246,
FT ECO:0000269|PubMed:17246162, ECO:0000269|PubMed:9012532"
FT MUTAGEN 305
FT /note="V->M: In ovo-D2; dominant antimorphic mutation
FT leading to the creation of a new upstream initiation codon
FT in isoform D. Heterozygous females are sterile. The male
FT germline is unaffected."
FT /evidence="ECO:0000269|PubMed:10648246,
FT ECO:0000269|PubMed:17246162, ECO:0000269|PubMed:9012532"
FT CONFLICT 957..959
FT /note="Missing (in Ref. 2; CAD23206 and 3; CAD23207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018
FT /note="A -> AAAA (in Ref. 2; CAD23206 and 3; CAD23207)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055
FT /note="A -> R (in Ref. 2; CAD23206 and 3; CAD23207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1351 AA; 146788 MW; 6FB5CDF3496F08A0 CRC64;
MPKIFLIKNR LHQQQQRLLE SQNLLQHKNQ DDERLVPPLS PSGSGSGPSP TPTSQPPPEP
QGQGQQVLGQ VPDSDQQPLS LTRKRFHHRR HYFGQSRHSL DHLNQNQSPN PNANANPNQI
QNPAELEVEC ATGQVQNENF AAELLQRLTP NTATTAQNNI VNNLVNNSRA ATSVLATKDC
TIENSPISIP KNQRAEDEEE QEDQEKEKPA EREREKSDER TEQVEKEERV EREEEEDDEV
DVGVEAPRPR FYNTGVVLTQ AQRKEYPQEP KDLSLTIAKS SPASPHIHSD SESDSDSDGG
CKLIVDEKPP LPVIKPLSLR LRSTPPPADQ RPSPPPPRDP APAVRCSVIQ RAPQSQLPTS
RAGFLLPPLD QLGPEQQEPI DYHVPKRRSP SYDSDEELNA RRLERARQVR EARRRSTILA
ARVLLAQSQR LNPRLVRSLP GILAAAAGHG RNSSSSSGAA GQGFQSSGFG SQNSGSGSSS
GNQNAGSGAG SPGSGAGGGG GMGGGRDGRG NYGPNSPPTG ALPPFYESLK SGQQSTASNN
TGQSPGANHS HFNANPANFL QNAAAAAYIM SAGSGGGGCT GNGGGGASGP GGGPSANSGG
GGGGGGGNGY INCGGVGGPN NSLDGNNLLN FASVSNYNES NSKFHNHHHH HQHNNNNNNN
GGQTSMMGHP FYGGNPSAYG IILKDEPDIE YDEAKIDIGT FAQNIIQATM GSSGQFNASA
YEDAIMSDLA SSGQCPNGAV DPLQFTATLM LSSQTDHLLE QLSDAVDLSS FLQRSCVDDE
ESTSPRQDFE LVSTPSLTPD SVTPVEQHNT NTTQLDVLHE NLLTQLTHNI VRGGSNQQQQ
HHQQHGVQQQ QQQQHSVQQQ QQHNVQQQHG VQQQHVQQQP PPSYQHATRG LMMQQQPQHG
GYQQQAAIMS QQQQQLLSQQ QQQSHHQQQQ QQQHAAAYQQ HNIYAQQQQQ QQQQHHQQQQ
QQQHHHFHHQ QQQQPQPQSH HSHHHGHGHD NSNMSLPSPT AAAAAAAAAA AAAAAAAAHL
QRPMSSSSSS GGTNSSNSSG GSSNSPLLDA NAAAAAAAAL LDTKPLIQSL GLPPDLQLEF
VNGGHGIKNP LAVENAHGGH HRIRNIDCID DLSKHGHHSQ HQQQQGSPQQ QNMQQSVQQQ
SVQQQQSLQQ QQQQQHHQHH SNSSASSNAS SHGSAEALCM GSSGGANEDS SSGNNKFVCR
VCMKTFSLQR LLNRHMKCHS DIKRYLCTFC GKGFNDTFDL KRHTRTHTGV RPYKCNLCEK
SFTQRCSLES HCQKVHSVQH QYAYKERRAK MYVCEECGHT TCEPEVHYLH LKNNHPFSPA
LLKFYDKRHF KFTNSQFANN LLGQLPMPVH N
