ID A0A0B4LFF8_DROME Unreviewed; 2456 AA.
AC A0A0B4LFF8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Rho guanine nucleotide exchange factor 2, isoform H {ECO:0000313|EMBL:AHN56311.1};
GN Name=RhoGEF2 {ECO:0000313|EMBL:AHN56311.1,
GN ECO:0000313|FlyBase:FBgn0023172};
GN Synonyms=Dmel\CG9635 {ECO:0000313|EMBL:AHN56311.1}, DRhoGEF
GN {ECO:0000313|EMBL:AHN56311.1}, dRhoGEF {ECO:0000313|EMBL:AHN56311.1},
GN DRhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, DrhoGEF2
GN {ECO:0000313|EMBL:AHN56311.1}, dRhoGEF2 {ECO:0000313|EMBL:AHN56311.1},
GN Gef2 {ECO:0000313|EMBL:AHN56311.1}, l(2)04291
GN {ECO:0000313|EMBL:AHN56311.1}, RG2 {ECO:0000313|EMBL:AHN56311.1},
GN Rho-GEF2 {ECO:0000313|EMBL:AHN56311.1}, RhoGEF
GN {ECO:0000313|EMBL:AHN56311.1}, RhoGef2 {ECO:0000313|EMBL:AHN56311.1},
GN rhoGEF2 {ECO:0000313|EMBL:AHN56311.1}, rhogef2
GN {ECO:0000313|EMBL:AHN56311.1}, RhoGF2 {ECO:0000313|EMBL:AHN56311.1},
GN shar {ECO:0000313|EMBL:AHN56311.1}, Su(Rho1)2B
GN {ECO:0000313|EMBL:AHN56311.1}, T2 {ECO:0000313|EMBL:AHN56311.1};
GN ORFNames=CG9635 {ECO:0000313|EMBL:AHN56311.1,
GN ECO:0000313|FlyBase:FBgn0023172}, Dmel_CG9635
GN {ECO:0000313|EMBL:AHN56311.1};
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 {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AHN56311.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; AE013599; AHN56311.1; -; Genomic_DNA.
DR RefSeq; NP_001286515.1; NM_001299586.1.
DR SMR; A0A0B4LFF8; -.
DR EnsemblMetazoa; FBtr0340124; FBpp0309117; FBgn0023172.
DR GeneID; 36915; -.
DR AGR; FB:FBgn0023172; -.
DR CTD; 36915; -.
DR FlyBase; FBgn0023172; RhoGEF2.
DR VEuPathDB; VectorBase:FBgn0023172; -.
DR GeneTree; ENSGT00940000168706; -.
DR OrthoDB; 2875542at2759; -.
DR BioGRID-ORCS; 36915; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36915; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0023172; Expressed in eye disc (Drosophila) and 27 other cell types or tissues.
DR ExpressionAtlas; A0A0B4LFF8; baseline and differential.
DR GO; GO:0030478; C:actin cap; IDA:FlyBase.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:FlyBase.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0070252; P:actin-mediated cell contraction; IGI:FlyBase.
DR GO; GO:0007375; P:anterior midgut invagination; IMP:FlyBase.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007377; P:germ-band extension; IMP:FlyBase.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0007277; P:pole cell development; IMP:FlyBase.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:FlyBase.
DR GO; GO:0007374; P:posterior midgut invagination; IMP:FlyBase.
DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR CDD; cd20832; C1_ARHGEF-like; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13329; PH_RhoGEF; 1.
DR CDD; cd08756; RGS_GEF_like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0B4LFF8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 260..336
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1047..1097
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1435..1630
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1775..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2151..2326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2415..2456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1422..1449
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2360..2387
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2199..2245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2246..2271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2291..2326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2417..2447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2456 AA; 269559 MW; B958C362CF326394 CRC64;
MDDPSIKKRL LDLYTDEHEY DEVQEIPEES SIQPPETSTS HTSTNGSSHS GPGTATGPGA
TSAGPSAGAP QSPVIVVDSV PELPAPKQKS VKNSKSKQKQ KQLANKSKIP RSPSLASSLS
SLASSLSGHR DRDKDRDKDR ENQNAVPPQT PPLPPSYKQN QMNGDSTAAA GGGVSAPATP
TTANNNNASH NNGSIMGGGV QLNQSDNSNP VLQAPGERSS LNLTPLSRDL SGGHTQESTT
PATTPSTPSL ALPKNFQYLT LTVRKDSNGY GMKVSGDNPV FVESVKPGGA AEIAGLVAGD
MILRVNGHEV RLEKHPTVVG LIKASTTVEL AVKRSQKLTR PSSVSVVTPS TPILSGRDRT
ASITGPQPVD SIKRREMETY KIQTLQKMLE QEKLNLERLK SDQNNPSYKL SEANIRKLRE
QLHQVGAEQQ RMSHQAESMS QSMHQHTSTP TSQQFFHPHQ QQHRFKETGP TSKGKNKFLI
SRSLIEEDVP PPLPQRNPPR QLNLDLKNGN ASPGGSHLVA PVSDLDRATS PQLNRSQQQQ
LPSSTDNSPS NAKSKRSKIK TKALSDPKMS TQMFLQMESA SAAGAAGGSI EVDGGPPPLP
PRLPGMMTED MSRGSCQNLA QPNSVGTAFN YPLVSTTTAV QNDNLNIAFP LSQRPNIVQQ
LQQYQQQQQH QMSGGQATGA LGQTPNLGKN KHRRVGSSPD NMHPRHPDRI TKTTSGSWEI
VEKDGESSPP GTPPPPYLSS SHMTVLEDPN ENNRGAAAAG PGVFIESHQF TPMAGASSPI
PISLHSSHMH AAQSNDTQKE IISMEDENSD LDEPFIDENG PFNNLTRLLE AENVTFLAIF
LNYVISNSDP APLLFYLITE LYKEGTSKDM RKWAYEIHST FLVPRAPLSW YRQDESLARE
VDNVLQLEYD KVEILRTVFL RSRKRAKDLI SEQLREFQQK RTAGLGTIYG PTDDKLAEAK
TDKLREQIID KYLMPNLHAL IEDENGSPPE DVRKVALCSA LSTVIYRIFN TRPPPSSIVE
RVHHFVSRDK SFKSRIMGKN RKMNVRGHPL VLRQYYEVTH CNHCQTIIWG VSPQGYHCTD
CKLNIHRQCS KVVDESCPGP LPQAKRLAHN DKISKFMGKI RPRTSDVIGN EKRSRQDEEL
DVELTPDRGQ ASIVRQPSDR RPDANISIRS NGNTSCNTSG LNTTDLQSSF HGSCANDSIN
PGGGAGCNMD LSTSVASTTP STSGSVAAGL SAFAELNALD TVDKEARRER YSQHPKHKSA
PVSVNRSESY KERLSNKRNR NSRRKTSDPS LSSRPNDEQL DLGLSNATYV GSSNSSLSSA
GGSESPSTSM EHFAAPGAAG GVQVPPMGLN QNQHPHLLIQ QHAQQYCQQD SFQAGLAGAA
GSSAASNSSF WNAGHPLPVA RWTLESEDED DVNEADWSSM VAAEVLAALT DAEKKRQEII
NEIYQTERNH VRTLKLLDRL FFLPLYESGL LSQDHLLLLF PPALLSLREI HGAFEQSLKQ
RRIEHNHVVN TIGDLLADMF DGQSGVVLCE FAAQFCARQQ IALEALKEKR NKDEMLQKLL
KKSESHKACR RLELKDLLPT VLQRLTKYPL LFENLYKVTV RLLPENTTEA EAIQRAVESS
KRILVEVNQA VKTAEDAHKL QNIQRKLDRS SYDKEEFKKL DLTQHHLIHD GNLTIKKNPS
VQLHGLLFEN MIVLLTKQDD KYYLKNLHTP LSITNKPVSP IMSIDADTLI RQEAADKNSF
FLIKMKTSQM LELRAPSSSE CKTWFKHFSD VAARQSKNRS KNASSNHDTS ISDPALAAIP
HSNTKESLEL STDTVQPLAA TATLTTTPLA PMLPIATVTP APATNNSNVS SLTGVQLRNP
QRDATASESD ADYVNTPKPR SSQNEVNRTM SIRSTGEPIQ KYSANGTEAN DVTLRHSQST
RESVRPGSTG EERNSTYGMV GGNSKRDSAS IVCSNNSNNT RTLLMQSPLV DPTAIQVSIS
PAHTAEPVLT PGEKLRRLDA SIRNDLLEKQ KIICDIFRLP VEHYDQIVDI AMMPEAPKDS
ADIALAAYDQ IQTLTKMLNE YMHVTPEQEV SAVSTAVCGH CHEKEKLRKK VAPSSSFSSS
PPPLPPPNRQ HAQAQAQIPP SRLMPKLQTL DLDEVAIHED DDGYCEIDEL RLPAIPSKPH
ERPTTPLAPF NTEPKTSQSV IDASKRQSTD AVPEGLLEQE PLEGDKTETK GEDNEVKTVP
SDKLSESCNE ERQCVEADIT KEVADPTTSK NEAAASVDEL PSQSREIKTA ENASKSVADK
KEDNEETIEE GVASTVDSST QTSPTESPKE TDKLTGGSSS TCGPNRIQHA SVLEPSVPCH
ALSSIVTILN EQISMLLPKI NERDMERERL RKENQHLREL LSALHDRQRV DEVKETPFDL
KKLMHAEDVE FDDDIDAISN SSLTPTPTPI PTASPSASGQ VETAEAMRIT STEDEE
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