MMD4_DROME
ID MMD4_DROME Reviewed; 610 AA.
AC Q86B87; A1A725; A8JR64; A8JR66; P91932; Q24099; Q24100; Q24101; Q24482;
AC Q24483; Q86B84; Q86B85; Q86B86; Q8IN28; Q8IN29; Q8IN30; Q8IN31; Q8IN32;
AC Q8IN33; Q8IN34; Q8WTI9; Q8WTJ0; Q8WTJ1; Q95R78; Q95ZF4; Q95ZF5; Q95ZF6;
AC Q95ZF7; Q95ZF8; Q9N6U6; Q9N6U7; Q9N6U8; Q9N6U9; Q9N6V0; Q9N6V1; Q9N6V2;
AC Q9N6V3; Q9N6V4; Q9N6V5; Q9N6V6; Q9N6V7; Q9N6V8; Q9N6V9; Q9N6W0; Q9N6W1;
AC Q9N6W2; Q9N6W3; Q9N6W4; Q9N6W5; Q9VDA9; Q9VDB2; Q9VDB3; Q9VDB4; Q9VDB5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Modifier of mdg4;
GN Name=mod(mdg4) {ECO:0000312|FlyBase:FBgn0002781};
GN Synonyms=bpd, doom {ECO:0000312|FlyBase:FBgn0002781},
GN E(var)3-93D {ECO:0000312|FlyBase:FBgn0002781};
GN ORFNames=CG32491 {ECO:0000312|FlyBase:FBgn0002781};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS C AND MOD2.2), FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:8248257};
RC TISSUE=Embryo {ECO:0000269|PubMed:8248257};
RX PubMed=8248257; DOI=10.1073/pnas.90.23.11376;
RA Dorn R., Krauss V., Reuter G., Saumweber H.;
RT "The enhancer of position-effect variegation of Drosophila, E(var)3-93D,
RT codes for a chromatin protein containing a conserved domain common to
RT several transcriptional regulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11376-11380(1993).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MOD1.8; MOD1.9 AND MOD2.2), FUNCTION,
RP AND INTERACTION WITH SU(HW).
RX PubMed=7664338; DOI=10.1016/0092-8674(95)90031-4;
RA Gerasimova T.I., Gdula D.A., Gerasimov D.V., Simonova O., Corces V.G.;
RT "A Drosophila protein that imparts directionality on a chromatin insulator
RT is an enhancer of position-effect variegation.";
RL Cell 82:587-597(1995).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H), AND FUNCTION.
RC STRAIN=Canton-S {ECO:0000269|PubMed:9111355};
RX PubMed=9111355; DOI=10.1128/mcb.17.5.2835;
RA Harvey A.J., Bidwai A.P., Miller L.K.;
RT "Doom, a product of the Drosophila mod(mdg4) gene, induces apoptosis and
RT binds to baculovirus inhibitor-of-apoptosis proteins.";
RL Mol. Cell. Biol. 17:2835-2843(1997).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 53.1; 53.6; 55.6; 59.0; 62.3; B; C; D;
RP E; F; G; H; I; J; K; M; N; O; Q; R AND S), FUNCTION, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=10790390; DOI=10.1093/genetics/155.1.141;
RA Buechner K., Roth P., Schotta G., Krauss V., Saumweber H., Reuter G.,
RA Dorn R.;
RT "Genetic and molecular complexity of the position effect variegation
RT modifier mod(mdg4) in Drosophila.";
RL Genetics 155:141-157(2000).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; L; P; 53.6 AND 54.7).
RX PubMed=11493677; DOI=10.1073/pnas.151268698;
RA Dorn R., Reuter G., Loewendorf A.;
RT "Transgene analysis proves mRNA trans-splicing at the complex mod(mdg4)
RT locus in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9724-9729(2001).
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [7] {ECO:0000305}
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 [8] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 55.6; AA; E AND P).
RC STRAIN=Berkeley {ECO:0000305}; TISSUE=Embryo {ECO:0000305};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 458-610 (ISOFORM MOD2.2), AND
RP FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=11604507; DOI=10.1128/mcb.21.22.7714-7720.2001;
RA Wei W., Brennan M.D.;
RT "The gypsy insulator can act as a promoter-specific transcriptional
RT stimulator.";
RL Mol. Cell. Biol. 21:7714-7720(2001).
RN [10]
RP FUNCTION.
RX PubMed=7761470; DOI=10.1073/pnas.92.11.5184;
RA Georgiev P.G., Corces V.G.;
RT "The su(Hw) protein bound to gypsy sequences in one chromosome can repress
RT enhancer-promoter interactions in the paired gene located in the other
RT homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5184-5188(1995).
RN [11]
RP FUNCTION.
RX PubMed=8852842; DOI=10.1093/genetics/142.2.425;
RA Georgiev P.G., Kozycina M.;
RT "Interaction between mutations in the suppressor of Hairy wing and modifier
RT of mdg4 genes of Drosophila melanogaster affecting the phenotype of gypsy-
RT induced mutations.";
RL Genetics 142:425-436(1996).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9491892; DOI=10.1016/s0092-8674(00)80944-7;
RA Gerasimova T.I., Corces V.G.;
RT "Polycomb and trithorax group proteins mediate the function of a chromatin
RT insulator.";
RL Cell 92:511-521(1998).
RN [13]
RP FUNCTION.
RX PubMed=10363916;
RX DOI=10.1002/(sici)1097-4695(19990605)39:3<447::aid-neu10>3.0.co;2-q;
RA Gorczyca M., Popova E., Jia X.-X., Budnik V.;
RT "The gene mod(mdg4) affects synapse specificity and structure in
RT Drosophila.";
RL J. Neurobiol. 39:447-460(1999).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=11106742; DOI=10.1016/s1097-2765(00)00101-5;
RA Gerasimova T.I., Byrd K., Corces V.G.;
RT "A chromatin insulator determines the nuclear localization of DNA.";
RL Mol. Cell 6:1025-1035(2000).
RN [15]
RP CHARACTERIZATION OF MUTANT MOD(MDG4)351.
RX PubMed=11024164; DOI=10.1093/nar/28.20.3864;
RA Read D., Butte M.J., Dernburg A.F., Frasch M., Kornberg T.B.;
RT "Functional studies of the BTB domain in the Drosophila GAGA and Mod(mdg4)
RT proteins.";
RL Nucleic Acids Res. 28:3864-3870(2000).
RN [16]
RP SELF-ASSOCIATION, INTERACTION WITH SU(HW), AND SUBCELLULAR LOCATION.
RX PubMed=11350941; DOI=10.1093/emboj/20.10.2518;
RA Ghosh D., Gerasimova T.I., Corces V.G.;
RT "Interactions between the Su(Hw) and Mod(mdg4) proteins required for gypsy
RT insulator function.";
RL EMBO J. 20:2518-2527(2001).
RN [17]
RP FUNCTION.
RX PubMed=11779804; DOI=10.1093/genetics/159.4.1649;
RA Chen S., Corces V.G.;
RT "The gypsy insulator of Drosophila affects chromatin structure in a
RT directional manner.";
RL Genetics 159:1649-1658(2001).
RN [18]
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH CHI AND SU(HW).
RX PubMed=11416154; DOI=10.1128/mcb.21.14.4807-4817.2001;
RA Gause M., Morcillo P., Dorsett D.;
RT "Insulation of enhancer-promoter communication by a gypsy transposon insert
RT in the Drosophila cut gene: cooperation between suppressor of hairy-wing
RT and modifier of mdg4 proteins.";
RL Mol. Cell. Biol. 21:4807-4817(2001).
RN [19]
RP INTERACTION WITH CP190; SU(HW) AND TRL, AND SUBCELLULAR LOCATION.
RX PubMed=15574329; DOI=10.1016/j.molcel.2004.11.004;
RA Pai C.-Y., Lei E.P., Ghosh D., Corces V.G.;
RT "The centrosomal protein CP190 is a component of the gypsy chromatin
RT insulator.";
RL Mol. Cell 16:737-748(2004).
RN [20]
RP INTERACTION WITH TRL.
RX PubMed=15465920; DOI=10.1073/pnas.0403959101;
RA Melnikova L., Juge F., Gruzdeva N., Mazur A., Cavalli G., Georgiev P.G.;
RT "Interaction between the GAGA factor and Mod(mdg4) proteins promotes
RT insulator bypass in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14806-14811(2004).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16286005; DOI=10.1016/j.cell.2005.08.043;
RA Thomas S.E., Soltani-Bejnood M., Roth P., Dorn R., Logsdon J.M. Jr.,
RA McKee B.D.;
RT "Identification of two proteins required for conjunction and regular
RT segregation of achiasmate homologs in Drosophila male meiosis.";
RL Cell 123:555-568(2005).
RN [22]
RP INTERACTION WITH TOPORS, AND SUBCELLULAR LOCATION.
RX PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
RA Capelson M., Corces V.G.;
RT "The ubiquitin ligase dTopors directs the nuclear organization of a
RT chromatin insulator.";
RL Mol. Cell 20:105-116(2005).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS 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).
RN [24]
RP INTERACTION WITH TOP2, AND SUBCELLULAR LOCATION.
RX PubMed=21304601; DOI=10.1371/journal.pone.0016562;
RA Ramos E., Torre E.A., Bushey A.M., Gurudatta B.V., Corces V.G.;
RT "DNA topoisomerase II modulates insulator function in Drosophila.";
RL PLoS ONE 6:E16562-E16562(2011).
CC -!- FUNCTION: Component of the gypsy chromatin insulator complex which is
CC required for the function of the gypsy chromatin insulator and other
CC endogenous chromatin insulators. Chromatin insulators are regulatory
CC elements which establish independent domains of transcriptional
CC activity within eukaryotic genomes. Insulators have two defining
CC properties; they can block the communication between an enhancer and a
CC promoter when placed between them and can also buffer transgenes from
CC position effect variegation (PEV). Insulators are proposed to structure
CC the chromatin fiber into independent domains of differing
CC transcriptional potential by promoting the formation of distinct
CC chromatin loops. This chromatin looping may involve the formation of
CC insulator bodies, where homotypic interactions between individual
CC subunits of the insulator complex could promote the clustering of
CC widely spaced insulators at the nuclear periphery. Within the gypsy
CC insulator complex, this protein may control the nature of the
CC repressive effect of su(Hw): in the absence of mod(mdg4) protein,
CC su(Hw) exerts a bidirectional silencing effect, whereas in the presence
CC of mod(mdg4), the silencing effect is unidirectional. Isoform H is
CC specifically required to maintain the pairing of achiasmate homologs in
CC male meiosis I which is mediated by the rDNA repeats on the achiasmate
CC X-Y bivalents. Isoform H also plays a role in apoptotic regulatory
CC pathways. {ECO:0000269|PubMed:10363916, ECO:0000269|PubMed:10790390,
CC ECO:0000269|PubMed:11416154, ECO:0000269|PubMed:11604507,
CC ECO:0000269|PubMed:11779804, ECO:0000269|PubMed:16286005,
CC ECO:0000269|PubMed:7664338, ECO:0000269|PubMed:7761470,
CC ECO:0000269|PubMed:8248257, ECO:0000269|PubMed:8852842,
CC ECO:0000269|PubMed:9111355, ECO:0000269|PubMed:9491892}.
CC -!- SUBUNIT: Can self-associate (PubMed:11350941, PubMed:11416154).
CC Interacts with Chi (PubMed:11416154). Interacts with Top2
CC (PubMed:21304601). Isoform mod2.2: Component of the gypsy chromatin
CC insulator complex, composed of Cp190, mod(mdg4) and su(Hw)
CC (PubMed:7664338, PubMed:11350941, PubMed:11416154, PubMed:15574329).
CC The gypsy chromatin insulator complex interacts with Topors via
CC mod(mdg4) and su(Hw) (PubMed:16209949). Isoform mod2.2 interacts with
CC Trl/GAGA and interaction with this protein may bypass the repressive
CC effects of the su(Hw) insulator (PubMed:15465920).
CC {ECO:0000269|PubMed:11350941, ECO:0000269|PubMed:11416154,
CC ECO:0000269|PubMed:15465920, ECO:0000269|PubMed:15574329,
CC ECO:0000269|PubMed:16209949, ECO:0000269|PubMed:21304601,
CC ECO:0000269|PubMed:7664338}.
CC -!- INTERACTION:
CC Q86B87-1; Q24478: Cp190; NbExp=4; IntAct=EBI-1433422, EBI-868840;
CC Q86B87-7; D6W4U4: UbcD6-RA; NbExp=4; IntAct=EBI-15125980, EBI-15125978;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10790390,
CC ECO:0000269|PubMed:11106742, ECO:0000269|PubMed:11350941,
CC ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16209949,
CC ECO:0000269|PubMed:16286005, ECO:0000269|PubMed:21304601,
CC ECO:0000269|PubMed:8248257, ECO:0000269|PubMed:9491892}. Chromosome
CC {ECO:0000269|PubMed:10790390, ECO:0000269|PubMed:11106742,
CC ECO:0000269|PubMed:11350941, ECO:0000269|PubMed:15574329,
CC ECO:0000269|PubMed:16209949, ECO:0000269|PubMed:16286005,
CC ECO:0000269|PubMed:21304601, ECO:0000269|PubMed:8248257,
CC ECO:0000269|PubMed:9491892}. Note=Colocalizes with other elements of
CC the gypsy chromatin insulator complex at multiple sites on polytene
CC chromosomes and at nuclear insulator bodies (PubMed:9491892,
CC PubMed:11106742, PubMed:11350941, PubMed:15574329, PubMed:16209949).
CC The unique C-termini of individual isoforms may specify binding to
CC particular chromosomal locations (PubMed:11350941). During the G2 phase
CC of male meiosis isoform H localizes to the nucleolus (PubMed:16286005).
CC It subsequently localizes to the rDNA repeats of the X-Y bivalent and
CC to multiple autosomal loci, where it remains until anaphase I
CC (PubMed:16286005). Localization to the rDNA repeats requires SA-2,
CC while localization to autosomal loci requires SA-2 and tef
CC (PubMed:16286005). {ECO:0000269|PubMed:11106742,
CC ECO:0000269|PubMed:11350941, ECO:0000269|PubMed:15574329,
CC ECO:0000269|PubMed:16209949, ECO:0000269|PubMed:16286005,
CC ECO:0000269|PubMed:9491892}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=31;
CC Name=mod2.2; Synonyms=67.2 {ECO:0000269|PubMed:10790390}, E(VAR)3-93D;
CC IsoId=Q86B87-1; Sequence=Displayed;
CC Name=53.1 {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-16; Sequence=VSP_050724;
CC Name=53.6; Synonyms=X;
CC IsoId=Q86B87-28; Sequence=VSP_010286;
CC Name=54.7; Synonyms=Y;
CC IsoId=Q86B87-23; Sequence=VSP_010287;
CC Name=55.6 {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-13; Sequence=VSP_050725;
CC Name=59.0; Synonyms=Z;
CC IsoId=Q86B87-25; Sequence=VSP_010288;
CC Name=62.3 {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-4; Sequence=VSP_050701;
CC Name=A {ECO:0000269|PubMed:11493677}; Synonyms=54.2
CC {ECO:0000269|PubMed:11493677};
CC IsoId=Q86B87-17; Sequence=VSP_050713;
CC Name=AA;
CC IsoId=Q86B87-29; Sequence=VSP_034704;
CC Name=AC;
CC IsoId=Q86B87-30; Sequence=VSP_034706;
CC Name=AB;
CC IsoId=Q86B87-31; Sequence=VSP_034705;
CC Name=B; Synonyms=54.6;
CC IsoId=Q86B87-27; Sequence=VSP_010284;
CC Name=C {ECO:0000269|PubMed:10790390, ECO:0000269|PubMed:8248257};
CC Synonyms=58.0 {ECO:0000269|PubMed:10790390}, 3
CC {ECO:0000269|PubMed:8248257};
CC IsoId=Q86B87-9; Sequence=VSP_050714;
CC Name=D; Synonyms=57.4;
CC IsoId=Q86B87-24; Sequence=VSP_010285;
CC Name=E {ECO:0000269|PubMed:10790390}; Synonyms=65.0
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-2; Sequence=VSP_050699;
CC Name=F {ECO:0000269|PubMed:10790390}; Synonyms=58.6
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-8; Sequence=VSP_050704;
CC Name=G {ECO:0000269|PubMed:10790390}; Synonyms=54.2
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-15; Sequence=VSP_050715;
CC Name=H {ECO:0000269|PubMed:10790390, ECO:0000269|PubMed:9111355};
CC Synonyms=56.3 {ECO:0000269|PubMed:10790390}, Doom, MNM;
CC IsoId=Q86B87-10; Sequence=VSP_050716;
CC Name=I {ECO:0000269|PubMed:10790390}; Synonyms=59.1
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-6; Sequence=VSP_050703;
CC Name=J {ECO:0000269|PubMed:10790390}; Synonyms=51.4
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-19; Sequence=VSP_050717;
CC Name=K {ECO:0000269|PubMed:10790390}; Synonyms=55.7
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-11; Sequence=VSP_050718;
CC Name=L {ECO:0000269|PubMed:11493677}; Synonyms=52.2
CC {ECO:0000269|PubMed:11493677};
CC IsoId=Q86B87-18; Sequence=VSP_050719;
CC Name=M {ECO:0000269|PubMed:10790390}; Synonyms=55.3
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-14; Sequence=VSP_050720;
CC Name=N {ECO:0000269|PubMed:10790390}; Synonyms=64.2
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-3; Sequence=VSP_050700;
CC Name=O {ECO:0000269|PubMed:10790390}; Synonyms=60.1
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-5; Sequence=VSP_050702;
CC Name=P {ECO:0000303|PubMed:10731132}; Synonyms=58.6;
CC IsoId=Q86B87-7; Sequence=VSP_050705;
CC Name=Q {ECO:0000269|PubMed:10790390}; Synonyms=46.3
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-21; Sequence=VSP_050721;
CC Name=R {ECO:0000269|PubMed:10790390}; Synonyms=52.0
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-20; Sequence=VSP_050722;
CC Name=S {ECO:0000269|PubMed:10790390}; Synonyms=55.1
CC {ECO:0000269|PubMed:10790390};
CC IsoId=Q86B87-12; Sequence=VSP_050723;
CC Name=mod1.8;
CC IsoId=Q86B87-26; Sequence=VSP_010289;
CC Name=mod1.9;
CC IsoId=Q86B87-22; Sequence=VSP_010283;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression is high in pupae and adult females but low in other stages
CC of development. {ECO:0000269|PubMed:10790390}.
CC -!- DOMAIN: Homotypic interactions mediated by the BTB (POZ) domain of this
CC protein may promote the clustering of distant insulator complexes into
CC nuclear insulator bodies.
CC -!- MISCELLANEOUS: [Isoform mod2.2]: C-terminal exons are translated from
CC the opposite DNA strand. This may be due to a trans-splicing event.
CC -!- MISCELLANEOUS: [Isoform 53.1]: C-terminal exons are translated from the
CC opposite DNA strand. This may be due to a trans-splicing event.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 53.6]: C-terminal exons are translated from the
CC opposite DNA strand. This may be due to a trans-splicing event.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 54.7]: C-terminal exons are translated from the
CC opposite DNA strand. This may be due to a trans-splicing event.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 55.6]: C-terminal exons are translated from the
CC opposite DNA strand. This may be due to a trans-splicing event.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 59.0]: C-terminal exons are translated from the
CC opposite DNA strand. This may be due to a trans-splicing event.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 62.3]: C-terminal exons are translated from the
CC opposite DNA strand. This may be due to a trans-splicing event.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA82990.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAL29128.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAN13870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X75498; CAA53215.1; -; Genomic_DNA.
DR EMBL; X75499; CAA53216.1; -; mRNA.
DR EMBL; U30905; AAA82988.1; -; mRNA.
DR EMBL; U30913; AAA82989.1; -; mRNA.
DR EMBL; U30914; AAA82990.1; ALT_SEQ; mRNA.
DR EMBL; U62802; AAC17459.1; -; mRNA.
DR EMBL; AJ277174; CAB85469.1; -; mRNA.
DR EMBL; AJ277175; CAB85470.1; -; mRNA.
DR EMBL; AJ277176; CAB85471.1; -; mRNA.
DR EMBL; AJ277177; CAB85472.1; -; mRNA.
DR EMBL; AJ277178; CAB85473.1; -; mRNA.
DR EMBL; AJ277179; CAB85474.1; -; mRNA.
DR EMBL; AJ277180; CAB85475.1; -; mRNA.
DR EMBL; AJ277181; CAB85476.1; -; mRNA.
DR EMBL; AJ277182; CAB85477.1; -; mRNA.
DR EMBL; AJ277183; CAB85478.1; -; mRNA.
DR EMBL; AJ277184; CAB85479.1; -; mRNA.
DR EMBL; AJ277185; CAB85480.1; -; mRNA.
DR EMBL; AJ277186; CAB85481.1; -; mRNA.
DR EMBL; AJ277187; CAB85482.1; -; mRNA.
DR EMBL; AJ277188; CAB85483.1; -; mRNA.
DR EMBL; AJ277189; CAB85484.1; -; mRNA.
DR EMBL; AJ277190; CAB85485.1; -; mRNA.
DR EMBL; AJ277191; CAB85486.1; -; mRNA.
DR EMBL; AJ277192; CAB85487.1; -; mRNA.
DR EMBL; AJ277193; CAB85488.1; -; mRNA.
DR EMBL; AJ277194; CAB85489.1; -; mRNA.
DR EMBL; AJ320161; CAC51387.1; -; mRNA.
DR EMBL; AJ320162; CAC51487.1; -; mRNA.
DR EMBL; AJ320163; CAC51488.1; -; mRNA.
DR EMBL; AJ320164; CAC51489.1; -; mRNA.
DR EMBL; AJ320165; CAC51388.1; -; mRNA.
DR EMBL; AE014297; AAF55882.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55883.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55884.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55885.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55888.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13862.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13863.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13864.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13865.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13866.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13867.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13868.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13869.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13870.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014297; AAN13871.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13872.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13873.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13874.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13875.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41581.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41582.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41583.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08718.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08719.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08720.1; -; Genomic_DNA.
DR EMBL; AY061580; AAL29128.1; ALT_SEQ; mRNA.
DR EMBL; BT003484; AAO39487.1; -; mRNA.
DR EMBL; BT003579; AAO39583.1; -; mRNA.
DR EMBL; BT029698; ABL75755.1; -; mRNA.
DR EMBL; AF214648; AAL33873.1; -; Genomic_DNA.
DR EMBL; AF214649; AAL33874.1; -; Genomic_DNA.
DR EMBL; AF214650; AAL33875.1; -; Genomic_DNA.
DR RefSeq; NP_001097856.1; NM_001104386.2. [Q86B87-29]
DR RefSeq; NP_001097857.1; NM_001104387.2. [Q86B87-31]
DR RefSeq; NP_001097858.1; NM_001104388.2. [Q86B87-30]
DR RefSeq; NP_524936.2; NM_080197.3. [Q86B87-8]
DR RefSeq; NP_732619.1; NM_163877.2. [Q86B87-20]
DR RefSeq; NP_732620.1; NM_163878.2. [Q86B87-17]
DR RefSeq; NP_732621.1; NM_163879.2. [Q86B87-24]
DR RefSeq; NP_732622.1; NM_163880.2. [Q86B87-15]
DR RefSeq; NP_732623.2; NM_163881.2.
DR RefSeq; NP_732624.1; NM_163882.2. [Q86B87-10]
DR RefSeq; NP_732625.1; NM_163883.2. [Q86B87-27]
DR RefSeq; NP_732626.1; NM_163884.2. [Q86B87-6]
DR RefSeq; NP_732627.1; NM_163885.2. [Q86B87-19]
DR RefSeq; NP_732628.1; NM_163886.2. [Q86B87-7]
DR RefSeq; NP_732629.1; NM_163887.2. [Q86B87-18]
DR RefSeq; NP_732630.1; NM_163888.2. [Q86B87-11]
DR RefSeq; NP_732631.1; NM_163889.2. [Q86B87-14]
DR RefSeq; NP_732632.1; NM_163890.2. [Q86B87-2]
DR RefSeq; NP_732633.1; NM_163891.2. [Q86B87-9]
DR RefSeq; NP_732634.1; NM_163892.2. [Q86B87-12]
DR RefSeq; NP_732635.1; NM_163893.2. [Q86B87-5]
DR RefSeq; NP_732636.1; NM_163894.2. [Q86B87-3]
DR RefSeq; NP_788698.1; NM_176521.1. [Q86B87-1]
DR RefSeq; NP_788699.1; NM_176522.1. [Q86B87-25]
DR RefSeq; NP_788700.1; NM_176523.1. [Q86B87-23]
DR RefSeq; NP_788701.1; NM_176524.1. [Q86B87-28]
DR RefSeq; NP_788702.1; NM_176525.1. [Q86B87-13]
DR RefSeq; NP_788703.1; NM_176526.1. [Q86B87-4]
DR RefSeq; NP_788704.1; NM_176527.1. [Q86B87-16]
DR AlphaFoldDB; Q86B87; -.
DR SMR; Q86B87; -.
DR BioGRID; 72097; 78.
DR IntAct; Q86B87; 32.
DR MINT; Q86B87; -.
DR STRING; 7227.FBpp0083463; -.
DR iPTMnet; Q86B87; -.
DR PaxDb; Q86B87; -.
DR PeptideAtlas; Q86B87; -.
DR DNASU; 49228; -.
DR EnsemblMetazoa; FBtr0084060; FBpp0083459; FBgn0002781. [Q86B87-17]
DR EnsemblMetazoa; FBtr0084061; FBpp0083460; FBgn0002781. [Q86B87-27]
DR EnsemblMetazoa; FBtr0084062; FBpp0083461; FBgn0002781. [Q86B87-9]
DR EnsemblMetazoa; FBtr0084063; FBpp0083462; FBgn0002781. [Q86B87-24]
DR EnsemblMetazoa; FBtr0084064; FBpp0083463; FBgn0002781. [Q86B87-2]
DR EnsemblMetazoa; FBtr0084065; FBpp0083464; FBgn0002781. [Q86B87-8]
DR EnsemblMetazoa; FBtr0084066; FBpp0083465; FBgn0002781. [Q86B87-15]
DR EnsemblMetazoa; FBtr0084067; FBpp0083466; FBgn0002781. [Q86B87-10]
DR EnsemblMetazoa; FBtr0084068; FBpp0083467; FBgn0002781. [Q86B87-6]
DR EnsemblMetazoa; FBtr0084069; FBpp0083468; FBgn0002781. [Q86B87-19]
DR EnsemblMetazoa; FBtr0084070; FBpp0083469; FBgn0002781. [Q86B87-11]
DR EnsemblMetazoa; FBtr0084071; FBpp0083470; FBgn0002781. [Q86B87-18]
DR EnsemblMetazoa; FBtr0084072; FBpp0083471; FBgn0002781. [Q86B87-14]
DR EnsemblMetazoa; FBtr0084073; FBpp0083472; FBgn0002781. [Q86B87-3]
DR EnsemblMetazoa; FBtr0084074; FBpp0083473; FBgn0002781. [Q86B87-5]
DR EnsemblMetazoa; FBtr0084075; FBpp0083474; FBgn0002781. [Q86B87-7]
DR EnsemblMetazoa; FBtr0084077; FBpp0083476; FBgn0002781. [Q86B87-20]
DR EnsemblMetazoa; FBtr0084078; FBpp0083477; FBgn0002781. [Q86B87-12]
DR EnsemblMetazoa; FBtr0084079; FBpp0083478; FBgn0002781. [Q86B87-1]
DR EnsemblMetazoa; FBtr0084080; FBpp0083479; FBgn0002781. [Q86B87-16]
DR EnsemblMetazoa; FBtr0084081; FBpp0083480; FBgn0002781. [Q86B87-4]
DR EnsemblMetazoa; FBtr0084082; FBpp0083481; FBgn0002781. [Q86B87-13]
DR EnsemblMetazoa; FBtr0084083; FBpp0083482; FBgn0002781. [Q86B87-28]
DR EnsemblMetazoa; FBtr0084084; FBpp0083483; FBgn0002781. [Q86B87-23]
DR EnsemblMetazoa; FBtr0084085; FBpp0083484; FBgn0002781. [Q86B87-25]
DR EnsemblMetazoa; FBtr0114359; FBpp0112908; FBgn0002781. [Q86B87-29]
DR EnsemblMetazoa; FBtr0114360; FBpp0112909; FBgn0002781. [Q86B87-31]
DR EnsemblMetazoa; FBtr0114361; FBpp0112910; FBgn0002781. [Q86B87-30]
DR GeneID; 49228; -.
DR KEGG; dme:Dmel_CG32491; -.
DR UCSC; CG32491-RAA; d. melanogaster.
DR UCSC; CG32491-RAB; d. melanogaster.
DR UCSC; CG32491-RAC; d. melanogaster.
DR CTD; 49228; -.
DR FlyBase; FBgn0002781; mod(mdg4).
DR VEuPathDB; VectorBase:FBgn0002781; -.
DR eggNOG; ENOG502S6BI; Eukaryota.
DR HOGENOM; CLU_1514257_0_0_1; -.
DR InParanoid; Q86B87; -.
DR OMA; MRYDESY; -.
DR SignaLink; Q86B87; -.
DR BioGRID-ORCS; 49228; 2 hits in 3 CRISPR screens.
DR ChiTaRS; mod(mdg4); fly.
DR GenomeRNAi; 49228; -.
DR PRO; PR:Q86B87; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002781; Expressed in central nervous system and 56 other tissues.
DR ExpressionAtlas; Q86B87; baseline and differential.
DR Genevisible; Q86B87; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031208; F:POZ domain binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0007141; P:male meiosis I; IMP:FlyBase.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR007588; Znf_FLYWCH.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF04500; FLYWCH; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Chromatin regulator; Chromosome;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..610
FT /note="Modifier of mdg4"
FT /id="PRO_0000096505"
FT DOMAIN 32..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 452..512
FT /note="FLYWCH-type"
FT REGION 1..308
FT /note="Interaction with Chi"
FT REGION 1..160
FT /note="Self-association"
FT REGION 115..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..610
FT /note="Interaction with su(Hw)"
FT REGION 567..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 360..449
FT /note="Missing (in isoform mod1.9)"
FT /evidence="ECO:0000303|PubMed:7664338"
FT /id="VSP_010283"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GDATQFFFTKGQRESVK
FT LNYCGHSYVKFMENGRGTKWICATRSTTKCRARIRTTKNNYLEVLYASHNHGFPPQKKD
FT RGRASQRM (in isoform 53.1)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050724"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> EQEDDFKLHLPLLVTRR
FT KKTPGGSRKQSFDHLEVSFTRSNRGNNLLTIDGKPFTLNRRIKDVCYWECVKLRCKYIK
FT CSARVVTKSNRISALSGLHNHP (in isoform 54.7)"
FT /evidence="ECO:0000303|PubMed:11493677"
FT /id="VSP_010287"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GHLSTLRHLPVEAIFDA
FT DGKQMDFIPNIRVIRSQRKTIKLMFKKYAYSKTNEHDTTTYWHCRSRRNGRPACKARFS
FT TKKLKNGSYKVYLTQPEHNHPPKKRRL (in isoform 55.6)"
FT /evidence="ECO:0000303|PubMed:10790390, ECO:0000303|Ref.8"
FT /id="VSP_050725"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> VTQHVRNCGPQMFLISR
FT KGGTLLTINNFVYRSNLKFFGKSNNILYWECVQNRSVKCRSRLKTIGDDLYVTNDVHNH
FT MGDNKRIEAAKAAGMLIHKKLSSLTAADKIQGSWKMDTEGNPDHLPKM (in
FT isoform 59.0)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_010288"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> ESSVAIYSATSRGRMQL
FT IYGGQPFIFEKTLKLSSGEEKRFWRCNQWWNQKCRSRVFTINDVVCPLNRFHTHEEIVR
FT RKKRVRRVPPVETIAKVVATTPRHPQHQQTTQQQQEIQLTSDAIAGAILDDESPATIDV
FT SELGMHLKYEEIVADVTGIVGGTRVVSRRK (in isoform 62.3)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050701"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> EKQFEYVVSQKGHVLLL
FT HKKFPFIREKCINGKTYWRCTQYTTKTKCHGRLHVLNGKIVHIKTHNHSPLDQERKQYM
FT KLQLNNV (in isoform A)"
FT /evidence="ECO:0000303|PubMed:11493677"
FT /id="VSP_050713"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> VLTYDDRGKLVHEGFTF
FT SCYSRNPGKCLAFWRCSMYKKMHCTSALTTHIKSIKSIRGFHNHKPPERLKTFVPRVLD
FT CPPRPHKEDY (in isoform AA)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_034704"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GVIQSLKALFEGKTTGA
FT SIQYTTTQRGRVMLVYEGYRYVVNRQSLKNVFWRCSRYVKHSCRATLVTSKVQEVTLRI
FT AGTPHTHAPEVSSMDLTTDLLDEFPELQ (in isoform AB)"
FT /evidence="ECO:0000305"
FT /id="VSP_034705"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> VTFDVLTDPIVKPDQHQ
FT LMKRVRLSKSMEGVHYVRTPAGNVVLHCGEHRYLRNAAYKDKVYWKCSKWRKQCRSRVI
FT THILPNGQSRYAVSGVHNHP (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_010284"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> DGPSKDTAIPKPAEHPR
FT KPVTDSVQKSPRDADAIPLFDGSRVFVSKVALAKAYIPMPMIYTCRVMDLVIGKDKLVR
FT IAQHEETTDKDLIQDIITHVCKVFALRGNQLTPSAVQEFIDHKLSTLKLMPIKEGK
FT (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10790390,
FT ECO:0000303|PubMed:8248257"
FT /id="VSP_050714"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> EFDYGHGQYRGNNPQIQ
FT FSVSKRGGQLLWLDGMKFFRNNINRTNLYWRCHWYYRHTKCPVLICMSKTNSNDFRQIH
FT DHCHIRPKRKENSGTGDGPKIRTPVVSNVRSLPQSMAHMFDM (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_010285"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> VKIKMEPSPTPGHSSDA
FT AVAALAVTYLSDEESFRKPFTLPKLLDGKFYKNIQPNQKTPGAIQATCTTCHGLISGTT
FT KSTGNFLSHIKRRHKELLPLCQLYCQAKANGTVPAVKSSPPNPNHVLTSATPTPAMEMM
FT TQVAQMPPTAAYATGPTHLGMPVTVPVPVSMSLAMPISLPHVQTPQMMALMQQHQAHGA
FT VFISKDY (in isoform E)"
FT /evidence="ECO:0000303|PubMed:10790390, ECO:0000303|Ref.8"
FT /id="VSP_050699"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> VVLANDEVPNPEDVLVF
FT FTQSLRGRPAIMANGIRFLIMSENKKKILWRCSSMATKKLKCPARITMLKETPPKFIIN
FT KAEHLHAELKRNKYSSSKAQTLRDPHQMATKLDCEMEGAGGVSFDLHEEELNELTHDV
FT (in isoform F)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050704"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> ELAVFGTGQRGRTVLLF
FT QNEKFVKNRCSASRTYWICSKKDVTVCRARVVTAVDKNSQERIIKCTYEHDHSRKFPSN
FT NVNLPVLIKREKALSLDAS (in isoform G)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050715"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> DLGELNPSNLADFGNES
FT FLPKTKGKRPQNVRCGLAPDQKCVRTLDDWDRIRYDRTRSGDVLVYDGYRYDRRANYND
FT IIYWGCAKKRLSCNVYMITHKNKPTYVAISGVHNHL (in isoform H)"
FT /evidence="ECO:0000303|PubMed:10790390,
FT ECO:0000303|PubMed:9111355"
FT /id="VSP_050716"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> VCDDLDDMKGAIKHSLL
FT TFIRGQRGCKLLAFNGHNYVRNRRSNLKTYWICSKKGSTKCNARVVTNVVEGVHKIVLE
FT SCHHTCLNTERKKRLSVTNVVGKARSKSEKSVSTGFIKEEGDEDLTLELRTLNLSIEDL
FT NNLQ (in isoform I)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050703"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GSVAYYSYITGFRGSRK
FT LKIGEFSFTRNKTSGLKTYWSCARAGVHKCKARVVTAQDHDVTIKCGQHNHPPY (in
FT isoform J)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050717"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GQFIGDIPRGQWIDKHE
FT YFFLKNQKQGFNLVFNGYMYKKEASFRATVNWICSDGNGKRLNENKCSARAITKFDGGI
FT KLGKNAHNHPPRFLGGKVPAKLMPKDAFYPQY (in isoform K)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050718"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> DRKRYSKKFLNFDGPAE
FT FSLAAHRRPRLIIANKHFIVHRILGKDNLIGSWRCMYHHKGCKARATTFMVDSEVKYRS
FT TCSSHNHKNVRSQQQSLKMPWVFTD (in isoform M)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050720"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> DTEISFIRSQKKNAQLV
FT FRNYIYNKKLTQANGQTTWRCADVLKLRCKAVVITRDGHFIDARRQHNHESHASRIGQR
FT QLYKVEQELEEYIEICTSNPKISQYLGSSNIIVTAKDGKDCKLFLPAAEATEIEMQALV
FT DAAEEELDEEERHAEERIRDRQRVGRWRTEEAKHRSLLKSEHP (in isoform N)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050700"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> EDELVFIESPWSTPCLV
FT LNGYMYNCHSRKSNKQYWRCHNYSKKAHEMRCRSRCVLENGRLKSVTGGLHNHQPHTEK
FT IDKIIQRNKMAAIGTGRKLSRTHSFTQLQLQEQKQEFIDEHQLTSDAATLQLTDQELMH
FT ASMMLMHE (in isoform O)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050702"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GCDGLQGSCRDRGGQKL
FT TGANHQMHLRA (in isoform Q)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050721"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GTSHLATFSCTRKKKRK
FT LVIDRHEFVMDRKLKSSINWRCARYRSSNCKVRATTHVQKNGLEVYRLKYAKHSHL
FT (in isoform R)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050722"
FT VAR_SEQ 403..610
FT /note="AATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAS
FT TTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHF
FT MQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDE
FT IELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> GLIFKAARHIAPIQKVR
FT QVRDDKFLATIIKLEPAGRLNLKNPDNIIRTSSNEHNFVYVGLPRMKGKCVNCLKKNRT
FT GLRRINTLCNTCPGSNWMCEPCFEELHS (in isoform S)"
FT /evidence="ECO:0000303|PubMed:10790390"
FT /id="VSP_050723"
FT VAR_SEQ 404..610
FT /note="ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAST
FT TKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHFM
FT QASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDEI
FT ELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> CYQLVPNRRGGKNLIFQG
FT HMYSVERKYRNSINWVCSKNSNSVLRCPARCVTNPESGNGIKLSHRRHNHPADAFKPHK
FT RCRKRPGDRK (in isoform 53.6)"
FT /evidence="ECO:0000303|PubMed:10790390,
FT ECO:0000303|PubMed:11493677"
FT /id="VSP_010286"
FT VAR_SEQ 404..610
FT /note="ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAST
FT TKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHFM
FT QASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDEI
FT ELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> FHIDFADSKKNGGKLLVI
FT NGFRFFRNKKRGHLQYWKCRNYYKERCPAIAIHDESTLILRLCHQHQHTESNDIEIKPL
FT PGSETKLAESAEDEAQAEPEAELDNETDPDTNHEPARVPPLIMEPPPLLEIKSKLRNQD
FT F (in isoform AC)"
FT /evidence="ECO:0000305"
FT /id="VSP_034706"
FT VAR_SEQ 404..610
FT /note="ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAST
FT TKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHFM
FT QASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDEI
FT ELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> KDQNKGVLLKRTAQGEFL
FT VVNGKSYKKTRAMQYRTYFHCLTRNCPTYYVLVELSRRPRLTRHHEHAQHCLQCY (in
FT isoform L)"
FT /evidence="ECO:0000303|PubMed:11493677"
FT /id="VSP_050719"
FT VAR_SEQ 404..610
FT /note="ATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYAST
FT TKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHFM
FT QASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDEI
FT ELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> KFDYQISVDVGEATMQLA
FT NASSAGVVNSNSPFFIVSKYGTKQIMLKQHTFNRHICRDDVTYWRCSQFAVLRCRARLK
FT TKLDTLTILNSEHNHEVITKARKYGSLKRQRAEAEAAARAERRQDPLETAATSAPATTT
FT (in isoform P)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:11493677, ECO:0000303|Ref.8"
FT /id="VSP_050705"
FT VAR_SEQ 459..610
FT /note="GVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEH
FT VHFMQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQE
FT IDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK -> DPTRPQLWSSDVPD
FT QPQATLLTINNFVYRANLKFFGKSNNILYWECVKTDRLSAAVALKTIGDDLYVTNGSYS
FT AVSKCKGHLMASFHLQMCTITWATTSVLRRPRRLDADPQEVEFPHSRRQNPGFLENGHR
FT GQPRPSAQDVAASILPTQTFVFC (in isoform mod1.8)"
FT /evidence="ECO:0000303|PubMed:7664338"
FT /id="VSP_010289"
FT MUTAGEN 33
FT /note="D->N: In allele mod(mdg4)351; embryonic lethal; when
FT associated with S-92."
FT MUTAGEN 92
FT /note="G->S: In allele mod(mdg4)351; embryonic lethal; when
FT associated with N-33."
FT CONFLICT 151..152
FT /note="QQ -> HE (in Ref. 2; AAA82988/AAA82989/AAA82990 and
FT 3; AAC17459)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="G -> V (in Ref. 9; AAL33875)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="E -> K (in Ref. 1; CAA53216 and 4; CAB85487)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-5:543
FT /note="M -> I (in Ref. 4; CAB85483)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-8:521
FT /note="S -> T (in Ref. 4; CAB85480)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-9:422
FT /note="V -> A (in Ref. 1; CAA53215)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-10:447
FT /note="D -> A (in Ref. 4; CAB85478)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-11:484
FT /note="A -> P (in Ref. 4; CAB85477)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-18:469
FT /note="A -> T (in Ref. 5; CAC51387)"
FT /evidence="ECO:0000305"
FT CONFLICT Q86B87-23:458
FT /note="N -> D (in Ref. 5; CAC51489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 67171 MW; 79CC78E52D2ADAF5 CRC64;
MADDEQFSLC WNNFNTNLSA GFHESLCRGD LVDVSLAAEG QIVKAHRLVL SVCSPFFRKM
FTQMPSNTHA IVFLNNVSHS ALKDLIQFMY CGEVNVKQDA LPAFISTAES LQIKGLTDND
PAPQPPQESS PPPAAPHVQQ QQIPAQRVQR QQPRASARYK IETVDDGLGD EKQSTTQIVI
QTTAAPQATI VQQQQPQQAA QQIQSQQLQT GTTTTATLVS TNKRSAQRSS LTPASSSAGV
KRSKTSTSAN VMDPLDSTTE TGATTTAQLV PQQITVQTSV VSAAEAKLHQ QSPQQVRQEE
AEYIDLPMEL PTKSEPDYSE DHGDAAGDAE GTYVEDDTYG DMRYDDSYFT ENEDAGNQTA
ANTSGGGVTA TTSKAVVKQQ SQNYSESSFV DTSGDQGNTE AQAATSASAT KIPPRKRGRP
KTKVEDQTPK PKLLEKLQAA TLNEEASEPA VYASTTKGGV KLIFNGHLFK FSFRKADYSV
FQCCYREHGE ECKVRVVCDQ KRVFPYEGEH VHFMQASDKS CLPSQFMPGE SGVISSLSPS
KELLMKNTTK LEEADDKEDE DFEEFEIQEI DEIELDEPEK TPAKEEEVDP NDFREKIKRR
LQKALQNKKK
