RBP2_DROME
ID RBP2_DROME Reviewed; 2718 AA.
AC A0A0B4K7J2; D3DMF2; Q8SWV7; Q9VBU7;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=E3 SUMO-protein ligase RanBP2 {ECO:0000305};
DE EC=2.3.2.- {ECO:0000250|UniProtKB:P49792};
DE AltName: Full=358 kDa nucleoporin {ECO:0000312|FlyBase:FBgn0039302};
DE AltName: Full=Nuclear pore complex protein Nup358 {ECO:0000305};
GN Name=Nup358 {ECO:0000312|FlyBase:FBgn0039302};
GN Synonyms=RanBP2 {ECO:0000303|PubMed:14729961};
GN ORFNames=CG11856 {ECO:0000312|FlyBase:FBgn0039302};
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:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|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.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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|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 [3] {ECO:0000312|EMBL:ACX61603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1729 (ISOFORM A/B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACX61603.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ACX61603.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAM11383.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1321-2718 (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11383.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM11383.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH NXT1; SBR AND RANGAP.
RX PubMed=14729961; DOI=10.1128/mcb.24.3.1155-1167.2004;
RA Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R.,
RA Bork P., Ellenberg J., Izaurralde E.;
RT "RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the
RT nuclear pore complex and functions in nuclear mRNA export.";
RL Mol. Cell. Biol. 24:1155-1167(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=17682050; DOI=10.1083/jcb.200612135;
RA Sabri N., Roth P., Xylourgidis N., Sadeghifar F., Adler J., Samakovlis C.;
RT "Distinct functions of the Drosophila Nup153 and Nup214 FG domains in
RT nuclear protein transport.";
RL J. Cell Biol. 178:557-565(2007).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HSP83, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=27979731; DOI=10.1016/j.ibmb.2016.12.005;
RA He Q., Zhang Y., Zhang X., Xu D., Dong W., Li S., Wu R.;
RT "Nucleoporin Nup358 facilitates nuclear import of Methoprene-tolerant (Met)
RT in an importin beta- and Hsp83-dependent manner.";
RL Insect Biochem. Mol. Biol. 81:10-18(2017).
RN [9]
RP FUNCTION, INTERACTION WITH PIWI, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29735528; DOI=10.1074/jbc.ac118.003264;
RA Parikh R.Y., Lin H., Gangaraju V.K.;
RT "A critical role for nucleoporin 358 (Nup358) in transposon silencing and
RT piRNA biogenesis in Drosophila.";
RL J. Biol. Chem. 293:9140-9147(2018).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=31626769; DOI=10.1016/j.cell.2019.09.022;
RA Hampoelz B., Schwarz A., Ronchi P., Bragulat-Teixidor H., Tischer C.,
RA Gaspar I., Ephrussi A., Schwab Y., Beck M.;
RT "Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis.";
RL Cell 179:671-686.E17(2019).
CC -!- FUNCTION: E3 SUMO-protein ligase (By similarity). Component of the
CC nuclear pore complex (NPC), a complex required for trafficking across
CC the nuclear envelope (PubMed:17682050). Required for nuclear import of
CC nuclear localization signal (NLS)-containing proteins in an importin
CC alpha/importin beta-dependent manner, but also for the nuclear import
CC of specific proteins such as phosphorylated Mad or the sesquiterpenoid
CC juvenile hormone receptor Met as part of the juvenile hormone signal
CC transduction pathway (PubMed:27979731, PubMed:17682050,
CC PubMed:17682050). Plays a role in nuclear mRNA export by recruiting the
CC mRNA transport complex composed of Nxt1 and sbr/Nxf1 to the NPC
CC (PubMed:14729961). Essential during germline development for transposon
CC silencing and piRNA biogenesis probably by regulating piwi localization
CC to the nucleus (PubMed:29735528). During oogenesis, required to form
CC granules that modulate the biogenesis of annulate lamellae containing
CC nuclear pore complex components (PubMed:31626769).
CC {ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:14729961,
CC ECO:0000269|PubMed:17682050, ECO:0000269|PubMed:20547758,
CC ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:29735528,
CC ECO:0000269|PubMed:31626769}.
CC -!- SUBUNIT: Part of the nuclear pore complex (By similarity). Forms a
CC complex with Nxt1, sbr/Nxf1 and RanGAP (PubMed:14729961). Interacts
CC (via TPR repeats) with Hsp83; the interaction is required for the
CC nuclear import of the sesquiterpenoid juvenile hormone receptor Met
CC (PubMed:27979731). Interacts (via N-terminus) with piwi
CC (PubMed:29735528). {ECO:0000250|UniProtKB:P49792,
CC ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:27979731,
CC ECO:0000269|PubMed:29735528}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P49792}. Note=Localizes to annulate lamellae,
CC stacked membrane sheets of the endoplasmic reticulum. Localizes to
CC granules which travel from nurse cells into the ooplasm through ring
CC canals connecting the cytoplasm of the two cell types.
CC {ECO:0000269|PubMed:31626769}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0039302};
CC IsoId=A0A0B4K7J2-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0039302};
CC IsoId=A0A0B4K7J2-2; Sequence=VSP_059517;
CC -!- TISSUE SPECIFICITY: Expressed in both oocytes and nurse cells (at
CC protein level). {ECO:0000269|PubMed:29735528,
CC ECO:0000269|PubMed:31626769}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (at protein level).
CC {ECO:0000269|PubMed:31626769}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown abolishes embryonic
CC development (PubMed:31626769). RNAi-mediated knockdown in the larval
CC fat body reduces the levels of importin beta and disrupts the nuclear
CC import of the sesquiterpenoid juvenile hormone receptor Met and
CC juvenile hormone signal transduction (PubMed:27979731). RNAi-mediated
CC knockdown in the germarium results in failed piwi localization to the
CC nucleus, failed transposon silencing and piRNA biogenesis, increased
CC DNA damage levels and overall defective ovaries (PubMed:29735528).
CC RNAi-mediated knockdown in egg chambers reduces numbers of annulate
CC lamellae containing nuclear pore complex components (PubMed:31626769).
CC {ECO:0000269|PubMed:27979731, ECO:0000269|PubMed:29735528,
CC ECO:0000269|PubMed:31626769}.
CC -!- SIMILARITY: Belongs to the RanBP2 E3 ligase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11383.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AFH06619.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56430.2; -; Genomic_DNA.
DR EMBL; BT100062; ACX61603.1; -; mRNA.
DR EMBL; AY095055; AAM11383.1; ALT_INIT; mRNA.
DR RefSeq; NP_001247302.1; NM_001260373.2. [A0A0B4K7J2-1]
DR RefSeq; NP_651361.2; NM_143104.3. [A0A0B4K7J2-2]
DR SMR; A0A0B4K7J2; -.
DR IntAct; A0A0B4K7J2; 3.
DR MINT; A0A0B4K7J2; -.
DR STRING; 7227.FBpp0293235; -.
DR PaxDb; A0A0B4K7J2; -.
DR EnsemblMetazoa; FBtr0084813; FBpp0084188; FBgn0039302. [A0A0B4K7J2-2]
DR EnsemblMetazoa; FBtr0304692; FBpp0293235; FBgn0039302. [A0A0B4K7J2-1]
DR GeneID; 43041; -.
DR KEGG; dme:Dmel_CG11856; -.
DR CTD; 43041; -.
DR FlyBase; FBgn0039302; Nup358.
DR VEuPathDB; VectorBase:FBgn0039302; -.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00900000141073; -.
DR OMA; FRFVDKE; -.
DR PhylomeDB; A0A0B4K7J2; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR SignaLink; A0A0B4K7J2; -.
DR BioGRID-ORCS; 43041; 2 hits in 3 CRISPR screens.
DR ChiTaRS; Nup358; fly.
DR GenomeRNAi; 43041; -.
DR PRO; PR:A0A0B4K7J2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039302; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; A0A0B4K7J2; baseline and differential.
DR Genevisible; Q9VBU7; DM.
DR GO; GO:0005642; C:annulate lamellae; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; ISS:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0035626; P:juvenile hormone mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:FlyBase.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0010528; P:regulation of transposition; IMP:UniProtKB.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23138; PTHR23138; 4.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Metal-binding; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transferase; Translocation;
KW Transport; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..2718
FT /note="E3 SUMO-protein ligase RanBP2"
FT /id="PRO_0000443733"
FT REPEAT 26..58
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 59..94
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 808..809
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 1028..1029
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 1035..1036
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 1104..1105
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 1252..1253
FT /note="5"
FT /evidence="ECO:0000305"
FT DOMAIN 1309..1445
FT /note="RanBD1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 1506..1507
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 1539..1540
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 1547..1548
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1552..1553
FT /note="9"
FT /evidence="ECO:0000305"
FT DOMAIN 1605..1742
FT /note="RanBD1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 1763..1764
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1826..1827
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1842..1843
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1874..1875
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1883..1884
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1942..1943
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1944..1945
FT /note="16"
FT /evidence="ECO:0000305"
FT DOMAIN 2019..2151
FT /note="RanBD1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2260..2261
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 2313..2314
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 2332..2333
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 2352..2353
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 2360..2361
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 2366..2367
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 2393..2394
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 2399..2400
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 2415..2416
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 2421..2422
FT /note="26"
FT /evidence="ECO:0000305"
FT DOMAIN 2556..2699
FT /note="RanBD1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2580..2581
FT /note="27"
FT /evidence="ECO:0000305"
FT ZN_FING 1770..1799
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1890..1919
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..200
FT /note="Sufficient for interaction with piwi"
FT /evidence="ECO:0000269|PubMed:29735528"
FT REGION 1..100
FT /note="Sufficient for interaction with Hsp83"
FT /evidence="ECO:0000269|PubMed:27979731"
FT REGION 796..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..2581
FT /note="27 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 937..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1738..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2154..2204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2239..2273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2320..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..1997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2158..2176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2326..2346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2197..2219
FT /note="Missing (in isoform A)"
FT /id="VSP_059517"
SQ SEQUENCE 2718 AA; 298931 MW; 9921196A7C964A7C CRC64;
MFTTRKEVDA HVHKMLGKLQ PGRERDIKGL AVARLYMKVQ EYPKAIEYLN GYLRVRDDAV
GHNMIATCYS RLNPPDVTEA LQHYQRSIQI DPRQSEVVID ACELLVKENN ASITECARYW
LDQANSLDLS GNKQVFNLRM RVNLADSNGE RDDTSGGDGE QNTLEILMYK ELQARPQDVN
IRIQLLRSYV EKMKIDQAFN YALKTELESK NCTSQSNEWY EQIWMVLFKI EMAKDVKKNW
RFWHFALHTL DRLVQLSLEG SGLADSSKQL FRLDQYLFKF STSIERSGDA PQRDLHQACI
DHFTGQLLLH AVTLIFKREV LANKNKWMST LRSALPLLLL GYQVRPIDDS STNQWIKHCD
AEQKQLIQMW RPQGAFRCAQ LGRTLLGCLD RSQMEIKNDR ENAEFDENKN SGNSMPGLFA
DSEELLASAH QQCLDKSWRS QIYQQLFTHA EHKLKDTSSH LVRNLRLQLP LFEWPNLAHI
ENYELQALVL PPHSLAQHVY LALGTDPNKL GDAPRVVFYE GFQRDVKQNL NYCGQDSISQ
VDVDLYLYAT TIQTRRKLQI QREVYDSSNL GNRNAAARPH MMPFANLVGQ LGAPEQSNWW
DLVVRLNSNQ LITEGNRAEQ RAQLQHGLEA VRGVNGPKAD AIIIFQLGKI LNSRSDRSSL
EARIDTLYRQ GFSILRHQHN QQMESYVRVF KYGSAGSTAA WQDLQSLAEE AVTYFSEKMF
RIGQYEQFLD EVRGLHLPMA YFLQSEACHH LEESSKLPRT SRDRYSERRR ECLQKTQKLI
KNDDKHPLIA AMHRHQQDRN SRGIDNSFGS PDVHNNSSAY EDAEDDFYSH AAFSANRSRR
QLEVTPVTPI VMAQPSQEME QAVKQISKSL CVLKDDVSVG MEAMRQDIKV LTEKFTGLED
LLKKIKISSR DTPTRDVDPA AALGLDDLFI IEDALAEHQQ QQQHQQQQSH NQGAIHPVVP
NPYTSGFYNG MPNTPSAQER FLQGPYGSPM FNQNQMYNYY AAQAQAQAQA QFLRTPPAPG
SIPPPNMFGP RNPNFGLPSM FPPPTVPSVA PYIDAMGNFT QPPPSLIPPP AQPAAPPAPL
NILESKPVVA LPTPGFFNTT TPVFGASPIQ VPQSKPLTVP TVPIPSTAPA PPIAGTVNPP
ATTAVPPPVH IPQVAPSVPA QPPAPAPVSV PSMFNRALNN QPVEKEPPAN VVITSSDPLP
KPTTASVQPT LSVTIPAQHI KPSLVQAPEQ PAQSAQPAQP SVSGVGSLSF NFGSKSSESP
FSFKTQVAKA AAEKQKEQEE AEQNQSGATD PNKTLPQDTS ADDYDPRPDF KPIIPLPDEV
EVRTGEEGED IKFTSRAKLF RYVDKEWKER GTGVIKILCD KATGVSRVLM RRDQTHKVCA
NHTITADITI NVANQDKDKK SLLWAANDFA DEQVTLERFL VRFKTGELAE EFRVAFTKAS
EAAKSKETVK PTVNTAEKGS TATAPAAFKS FVTSTPAANS LINKPQEQTK TQPNPDPPAT
AAKSLFGTLS VSAAPATSAP ASATPFASFS FTPNGSSGFG TSTASPFGNL SFGTASAVGS
GNNTTLFTTA LIKDNTVQGK TLQQESQLNK SNSSDAEEEY VPTAQFVPVI ALPDIVEVVT
GEENEDVLFE HRAKLLRWDK EANEWKERGL GNMKLLRDRT DPNKVRLLMR REQVHKLCCN
QRLLPETKFT YATNCKAAVT WGAQDYSDEE LTTALLAVRF KSQDICQQFL EAVQKAQQSI
GNEPKKEEVP SAAGEKEKPI KGFGDAFKPK AGSWNCQACY TNNGQDQLYC LACQEPKDAT
VPPKQSGLDQ GNALNLTTSS SNKFSFGFAS SATLPATGGF SFGGATQPKE KPAVAVVTAS
ASAPTSVQTA ALGFGKSSMT SGFGDAFKPA VGSWSCSACY VNNPGESLYC SACDAPKNDT
VPQKEKSLGS GLNLPPTSKF SFGFGAAAAG DKDQAGDGAT FNFAAMPAAV APTTSIGSSS
FTFSMTKPKP DQQQPNSTAA KEDEDNDSQE VEEEENNTYF SPVIPLPDKI DVKTGEEDEE
LLYVHKAKLY RLNESDWKER GLGDVKILRH RQTKKLRVVM RREQVFKICL NHVLNENVVY
REKTETSWMF AVHDFSEGES VLERFTLRFK NKEVAQGFME AIKNALNETA KPIEDSPVVG
SVSQSTEANK PSQKNDGAAK SRGGESEVLD VGKTSSVRPT THEVIPPLPM TLPLLTLPQP
LAKPNDYQTP ATILFKGSSL SRNNSSASEA SKTPSSAFIF GSTDKSEPGK DAGPLANLQK
LASGEGQGNV LGSIFRSGSS NENSSDGSVK FFFGGGNKAA EQQKKDSSES VFGGNKADSQ
SPATQEAPKL AFGGIAAPVF GDANPFGGHK VNLQKSDGKE EPKSIIGGTP LLFGGSNAFG
IPKIETQSPA KDFVFGSAPA FGQMATFSFT AAKNEKEKDI TSNNTTDLKA EGKEKKELVP
ETTSTFADLA KTGSTFADLA SNPGGTFADL ANKTGNDFAN LSANSQGTTV GFNKSAGGGF
YNLTHQNAFK NFESPQATEE CDDDGDATTD DNYDPHYDAI VELPDEIVVT TGEENETKLF
GERAKLYRYD AESKQWKERG VGEIKVLEHP ELQTFRLIMR QEQIHKLVLN MNISASLQMD
YMNAQMKSFL WAGYNYAVDA EGKVDTEGVL ERLACRFAKE EIASEFLNTV NSCIKRAKAL
QGDEENKNDD APEEQASS
