RBP9X_DROME
ID RBP9X_DROME Reviewed; 962 AA.
AC Q4Z8K6; A1Z895; A1Z896; A8E757; Q6NN33; Q8T0U5; Q960F3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ran-binding proteins 9/10 homolog;
DE AltName: Full=Ran-binding protein M;
GN Name=RanBPM; ORFNames=CG42236;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
RX PubMed=18762575; DOI=10.1083/jcb.200711046;
RA Dansereau D.A., Lasko P.;
RT "RanBPM regulates cell shape, arrangement, and capacity of the female
RT germline stem cell niche in Drosophila melanogaster.";
RL J. Cell Biol. 182:963-977(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-445 (ISOFORMS A/D), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-962 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
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 [6]
RP FUNCTION.
RX PubMed=16055650; DOI=10.1101/gad.1320705;
RA Baeg G.-H., Zhou R., Perrimon N.;
RT "Genome-wide RNAi analysis of JAK/STAT signaling components in
RT Drosophila.";
RL Genes Dev. 19:1861-1870(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-393 AND SER-395, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: May be involved in JAK/STAT signaling. Isoform D is required
CC for the proper arrangement of niche cells and is autonomously required
CC for proper niche cell size, isoform C negatively regulates the adhesive
CC properties of the niche. The germline stem cell (GSC) niche in ovaries
CC is made up of two somatic cell types: 8-9 cells in a single-filed array
CC make up the terminal filament (TF), and a tight cluster of 5 or 6 cap
CC cells (CpC). Regulating the size and adhesive properties of the CpCs is
CC an important component of the mechanism that controls their capacity to
CC support stem cells, isoform C and isoform D are important factors in
CC mediating this regulation. In contrast, isoform C acts as a positive
CC regulator of cell adhesion in follicle cell epithelium.
CC {ECO:0000269|PubMed:16055650, ECO:0000269|PubMed:18762575}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18762575}. Membrane
CC {ECO:0000269|PubMed:18762575}. Nucleus {ECO:0000269|PubMed:18762575}.
CC Note=Distribution varies depending on cell type and developmental
CC stage. At late embryogenesis expression is enriched in the nuclei of
CC follicle cells and germline cells and at the nurse cell membranes. In
CC pupal ovaries, expression is seen in niche cells at the cell periphery.
CC In adult ovaries expression is in the nuclei and cytoplasm of the CpCs
CC and TF cells of the niche.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=D; Synonyms=Long RanBPM;
CC IsoId=Q4Z8K6-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q4Z8K6-2; Sequence=VSP_028297;
CC Name=C; Synonyms=Short RanBPM;
CC IsoId=Q4Z8K6-3; Sequence=VSP_028296, VSP_028297;
CC -!- TISSUE SPECIFICITY: Expressed in the GSCs and in dividing cysts.
CC Expression is reduced in the germline as individual egg chambers are
CC formed. Isoform C is expressed in all somatic and germline cells of the
CC ovary. Isoform D is expressed in the GSC niche.
CC {ECO:0000269|PubMed:18762575}.
CC -!- DISRUPTION PHENOTYPE: Lack of isoform D causes an increase in niche
CC cell size and abnormal terminal filament organization. This in turn
CC increases niche capacity by increasing the potential contact surface
CC between CpCs and stem cells. Lack of isoform C causes defects in the
CC organization of the follicle cell layer and defects in dorsal appendage
CC morphogenesis. {ECO:0000269|PubMed:18762575}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93515.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAL39193.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAR99122.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAX84045.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABV82381.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY973544; AAX84045.1; ALT_FRAME; mRNA.
DR EMBL; AY973545; AAX84046.1; -; mRNA.
DR EMBL; AY973546; AAX84047.1; -; mRNA.
DR EMBL; AE013599; AAF58795.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68758.1; -; Genomic_DNA.
DR EMBL; AE013599; ABC66064.1; -; Genomic_DNA.
DR EMBL; BT011464; AAR99122.1; ALT_FRAME; mRNA.
DR EMBL; BT030999; ABV82381.1; ALT_SEQ; mRNA.
DR EMBL; AY052091; AAK93515.1; ALT_SEQ; mRNA.
DR EMBL; AY069048; AAL39193.1; ALT_INIT; mRNA.
DR RefSeq; NP_001033938.1; NM_001038849.2. [Q4Z8K6-1]
DR RefSeq; NP_610585.2; NM_136741.3. [Q4Z8K6-3]
DR RefSeq; NP_724932.1; NM_165770.3. [Q4Z8K6-2]
DR AlphaFoldDB; Q4Z8K6; -.
DR SMR; Q4Z8K6; -.
DR BioGRID; 61920; 19.
DR IntAct; Q4Z8K6; 5.
DR STRING; 7227.FBpp0099887; -.
DR iPTMnet; Q4Z8K6; -.
DR PaxDb; Q4Z8K6; -.
DR PRIDE; Q4Z8K6; -.
DR EnsemblMetazoa; FBtr0088262; FBpp0087357; FBgn0262114. [Q4Z8K6-3]
DR EnsemblMetazoa; FBtr0088263; FBpp0087358; FBgn0262114. [Q4Z8K6-2]
DR EnsemblMetazoa; FBtr0100460; FBpp0099887; FBgn0262114. [Q4Z8K6-1]
DR GeneID; 36102; -.
DR KEGG; dme:Dmel_CG42236; -.
DR CTD; 36102; -.
DR FlyBase; FBgn0262114; RanBPM.
DR VEuPathDB; VectorBase:FBgn0262114; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000174485; -.
DR HOGENOM; CLU_009129_1_0_1; -.
DR InParanoid; Q4Z8K6; -.
DR OMA; SNGYKCQ; -.
DR PhylomeDB; Q4Z8K6; -.
DR SignaLink; Q4Z8K6; -.
DR BioGRID-ORCS; 36102; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36102; -.
DR PRO; PR:Q4Z8K6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0262114; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q4Z8K6; baseline and differential.
DR Genevisible; Q4Z8K6; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0034657; C:GID complex; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:FlyBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0007299; P:ovarian follicle cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IMP:UniProtKB.
DR CDD; cd12909; SPRY_RanBP9_10; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035782; SPRY_RanBP9/10.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..962
FT /note="Ran-binding proteins 9/10 homolog"
FT /id="PRO_0000305240"
FT DOMAIN 400..587
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 617..649
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 655..712
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..362
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:18762575, ECO:0000303|Ref.4"
FT /id="VSP_028296"
FT VAR_SEQ 834..835
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:18762575, ECO:0000303|Ref.4"
FT /id="VSP_028297"
FT CONFLICT 445
FT /note="V -> E (in Ref. 5; AAK93515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 106654 MW; 91206B4DC4D9DB30 CRC64;
MENVEEAPPL SSESNSNSNN SSASSSSHQL SQSGAMGAEI APSTSRSHSH SPTPSPPVPA
SSHDQPHPDH PSPPLNASET EARENSPHDH SPTPTFHQTA PPPTTSSTAP QRDEREQQQQ
QEAPPLQQDQ QENSPAQDQE LHPLLDQQNQ EYPAVHQDQQ AEQNQELHHI EGLIRHRESQ
NPEEHPPQAS LENRETLGRE DTNQEPDEPQ VRDPEIEPEA EPPPPLLLED LDEQDSGSQD
LNEQQPPLII DANAIAETID ANAVERIDDY EDDDEEVDEE EEVVEDRVDR AGEVASVSGA
QRLHSVAVLP RYSSASRAPR SSNNNNNNIS NHNNNNNNSN SNSLSRRTRH FYSNNGSHFS
NDMFPSHNPR SSTQTSSPRV GGRRHHSTPA ASSNSPQHQG VDPLRLLYPN VNESETPLPR
CWSPHDKCLS IGLSQNNLRV TYKGVGKQHS DAASVRTAYP IPSSCGLYYF EVRIISKGRN
GYMGIGLTAQ QFRMNRLPGW DKQSYGYHGD DGNSFSSSGN GQTYGPTFTT GDVIGCCVNF
VNNTCFYTKN GVDLGIAFRD LPTKLYPTVG LQTPGEEVDA NFGQEPFKFD KIVDMMKEMR
SNVLRKIDRY PHLLETPENL MNRLVSTYLV HNAFSKTAEA FNGYTNQTFN EDLASIKTRQ
KIIKLILTGK MSQAIEHTLR SFPGLLENNK NLWFALKCRQ FIEMINGADI ENVNNKVTAT
TQTMPTNQTS VIQSTKTFKH SKSGSGNGNV NINQTQQQNN TAIPAVIKPQ GGDRPDIKNM
LVDDNSNKCV EHDSNSMDVE MEPCQSHSNG GDSSSNGNAS AVRNSLDAID EEMDVDVSPS
SRNCGRVIEK ILEFGKELSS MGQQLEKENL MTEEERQMLE DAFSLIAYSN PWSSPLGWLL
CPSRRESVST TLNSAILESL NFERRPPLEY LVAHASELIK VIGQHSLGED AFITIDDVFP
QN
