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Database: UniProt
Entry: RBP2_DROME
LinkDB: RBP2_DROME
Original site: 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   24-JAN-2024, entry version 61.
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   ComplexPortal; CPX-2568; Nuclear pore complex.
DR   IntAct; A0A0B4K7J2; 3.
DR   MINT; A0A0B4K7J2; -.
DR   STRING; 7227.FBpp0293235; -.
DR   PaxDb; 7227-FBpp0293235; -.
DR   EnsemblMetazoa; FBtr0084813; FBpp0084188; FBgn0039302. [A0A0B4K7J2-2]
DR   EnsemblMetazoa; FBtr0304692; FBpp0293235; FBgn0039302. [A0A0B4K7J2-1]
DR   GeneID; 43041; -.
DR   KEGG; dme:Dmel_CG11856; -.
DR   UCSC; CG11856-RA; d. melanogaster.
DR   AGR; FB:FBgn0039302; -.
DR   CTD; 43041; -.
DR   FlyBase; FBgn0039302; Nup358.
DR   VEuPathDB; VectorBase:FBgn0039302; -.
DR   eggNOG; KOG0864; Eukaryota.
DR   GeneTree; ENSGT00900000141073; -.
DR   InParanoid; A0A0B4K7J2; -.
DR   OMA; FRFVDKE; -.
DR   OrthoDB; 158765at2759; -.
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-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 cell types or 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: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:UniProtKB.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR   GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR   CDD; cd13171; RanBD1_RanBP2_insect-like; 1.
DR   CDD; cd13172; RanBD2_RanBP2_insect-like; 1.
DR   CDD; cd13173; RanBD3_RanBP2_insect-like; 1.
DR   CDD; cd13174; RanBD4_RanBP2_insect-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
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:SF169; E3 SUMO-PROTEIN LIGASE RANBP2; 1.
DR   PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
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; SSF50729; PH domain-like; 4.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 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
//
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