ID   RANB9_MOUSE             Reviewed;         653 AA.
AC   P69566; P84500; Q3V136;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Ran-binding protein 9 {ECO:0000305};
DE            Short=RanBP9;
DE   AltName: Full=B-cell antigen receptor Ig beta-associated protein 1;
DE            Short=IBAP-1;
DE   AltName: Full=Ran-binding protein M;
DE            Short=RanBPM;
GN   Name=Ranbp9 {ECO:0000312|MGI:MGI:1928741}; Synonyms=Ranbpm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX4, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Testis;
RX   PubMed=14648869; DOI=10.1002/mrd.20009;
RA   Shibata N., Tsunekawa N., Okamoto-Ito S., Akasu R., Tokumasu A., Noce T.;
RT   "Mouse RanBPM is a partner gene to a germline specific RNA helicase, mouse
RT   vasa homolog protein.";
RL   Mol. Reprod. Dev. 67:1-7(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Doi T., Watanabe T.;
RT   "B cell antigen receptor Ig beta associated protein.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-653 (ISOFORM 1), AND INTERACTION WITH
RP   NGFR.
RC   TISSUE=Brain;
RX   PubMed=12963025; DOI=10.1016/j.bbrc.2003.08.033;
RA   Bai D., Chen H., Huang B.-R.;
RT   "RanBPM is a novel binding protein for p75NTR.";
RL   Biochem. Biophys. Res. Commun. 309:552-557(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=14722085; DOI=10.1074/jbc.m313515200;
RA   Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
RA   Fabbri M., Pardi R., Bianchi E.;
RT   "RanBPM is a phosphoprotein that associates with the plasma membrane and
RT   interacts with the integrin LFA-1.";
RL   J. Biol. Chem. 279:13027-13034(2004).
RN   [6]
RP   INTERACTION WITH MKLN1, AND SUBCELLULAR LOCATION.
RX   PubMed=18710924; DOI=10.1083/jcb.200801133;
RA   Valiyaveettil M., Bentley A.A., Gursahaney P., Hussien R., Chakravarti R.,
RA   Kureishy N., Prag S., Adams J.C.;
RT   "Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator
RT   of cell morphology regulation.";
RL   J. Cell Biol. 182:727-739(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND SER-412, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   INTERACTION WITH TEX19.1.
RX   PubMed=28254886; DOI=10.1242/jcs.188763;
RA   Tarabay Y., Achour M., Teletin M., Ye T., Teissandier A., Mark M.,
RA   Bourc'his D., Viville S.;
RT   "Tex19 paralogs are new members of the piRNA pathway controlling
RT   retrotransposon suppression.";
RL   J. Cell Sci. 130:1463-1474(2017).
CC   -!- FUNCTION: May act as scaffolding protein, and as adapter protein to
CC       couple membrane receptors to intracellular signaling pathways. Acts as
CC       a mediator of cell spreading and actin cytoskeleton rearrangement. Core
CC       component of the CTLH E3 ubiquitin-protein ligase complex that
CC       selectively accepts ubiquitin from UBE2H and mediates ubiquitination
CC       and subsequent proteasomal degradation of the transcription factor
CC       HBP1. May be involved in signaling of ITGB2/LFA-1 and other integrins.
CC       Enhances HGF-MET signaling by recruiting Sos and activating the Ras
CC       pathway. Enhances dihydrotestosterone-induced transactivation activity
CC       of AR, as well as dexamethasone-induced transactivation activity of
CC       NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73
CC       isoform Alpha, probably by inhibiting its ubiquitination, and increases
CC       its proapoptotic activity. Inhibits the kinase activity of DYRK1A and
CC       DYRK1B. Inhibits FMR1 binding to RNA. {ECO:0000250|UniProtKB:Q96S59}.
CC   -!- SUBUNIT: Part of a complex consisting of RANBP9, MKLN1 and GID8.
CC       Identified in the CTLH complex that contains GID4, RANBP9 and/or
CC       RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B),
CC       GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or
CC       alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or
CC       RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5
CC       have ancillary roles. Interacts with GTP-bound Ran, AR, CDC2L1/p110C,
CC       CALB1, S100A7, USP11, SOS1 or SOS2, GID8, and FMR1. Interacts with the
CC       Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73 isoform
CC       Alpha but not with TP53. Interacts with the HGF receptor MET and the
CC       integrins ITGB1 and ITGB2, but not with ITGAL. Part of a complex
CC       consisting of RANBP9, RAN, DYRK1B and COPS5. Directly interacts with
CC       RANBP10. Interacts with YPEL5 (By similarity). Interacts with MKLN1
CC       (PubMed:18710924). Interacts with DDX4 (PubMed:14648869). Interacts
CC       with NGFR (PubMed:12963025). Interacts with Tex19.1 and, probably,
CC       Tex19.2 (PubMed:28254886). {ECO:0000250|UniProtKB:Q96S59,
CC       ECO:0000269|PubMed:12963025, ECO:0000269|PubMed:14648869,
CC       ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:28254886}.
CC   -!- INTERACTION:
CC       P69566; Q9JI18: Lrp1b; NbExp=2; IntAct=EBI-772305, EBI-8294317;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18710924}. Cell
CC       membrane {ECO:0000305|PubMed:18710924}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:18710924}; Cytoplasmic side
CC       {ECO:0000305|PubMed:18710924}. Nucleus {ECO:0000269|PubMed:18710924}.
CC       Note=Predominantly cytoplasmic (PubMed:18710924). A phosphorylated form
CC       is associated with the plasma membrane (By similarity). Perinuclear in
CC       spermatids (PubMed:14648869). {ECO:0000250|UniProtKB:Q96S59,
CC       ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:18710924}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P69566-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P69566-2; Sequence=VSP_028266, VSP_028267;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       maturating spermatocytes. {ECO:0000269|PubMed:14648869,
CC       ECO:0000269|PubMed:14722085}.
CC   -!- DOMAIN: The SPRY domain mediates the interaction with MET, AR, and
CC       CDC2L1. {ECO:0000250|UniProtKB:Q96S59}.
CC   -!- PTM: Phosphorylated in response to stress.
CC       {ECO:0000250|UniProtKB:Q96S59}.
CC   -!- PTM: Ubiquitinated. Polyubiquitination targets the protein for rapid
CC       degradation via the ubiquitin system (By similarity).
CC       {ECO:0000250|UniProtKB:Q96S59}.
CC   -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF006465; AAD01272.1; -; mRNA.
DR   EMBL; AK132714; BAE21317.1; -; mRNA.
DR   PIR; JC8013; JC8013.
DR   RefSeq; NP_064314.2; NM_019930.2.
DR   AlphaFoldDB; P69566; -.
DR   SMR; P69566; -.
DR   BioGRID; 208133; 16.
DR   IntAct; P69566; 8.
DR   MINT; P69566; -.
DR   STRING; 10090.ENSMUSP00000130636; -.
DR   iPTMnet; P69566; -.
DR   PhosphoSitePlus; P69566; -.
DR   EPD; P69566; -.
DR   MaxQB; P69566; -.
DR   PaxDb; 10090-ENSMUSP00000130636; -.
DR   PeptideAtlas; P69566; -.
DR   ProteomicsDB; 255093; -. [P69566-1]
DR   ProteomicsDB; 255094; -. [P69566-2]
DR   Pumba; P69566; -.
DR   Antibodypedia; 24991; 310 antibodies from 35 providers.
DR   DNASU; 56705; -.
DR   Ensembl; ENSMUST00000222651.2; ENSMUSP00000152620.2; ENSMUSG00000038546.10. [P69566-2]
DR   GeneID; 56705; -.
DR   KEGG; mmu:56705; -.
DR   AGR; MGI:1928741; -.
DR   CTD; 10048; -.
DR   MGI; MGI:1928741; Ranbp9.
DR   VEuPathDB; HostDB:ENSMUSG00000038546; -.
DR   eggNOG; KOG1477; Eukaryota.
DR   GeneTree; ENSGT00940000157305; -.
DR   InParanoid; P69566; -.
DR   OrthoDB; 38145at2759; -.
DR   PhylomeDB; P69566; -.
DR   Reactome; R-MMU-373760; L1CAM interactions.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-MMU-8851805; MET activates RAS signaling.
DR   BioGRID-ORCS; 56705; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Ranbp9; mouse.
DR   PRO; PR:P69566; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P69566; Protein.
DR   Bgee; ENSMUSG00000038546; Expressed in animal zygote and 247 other cell types or tissues.
DR   ExpressionAtlas; P69566; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; ISO:MGI.
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   PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR   PANTHER; PTHR12864:SF56; RAN-BINDING PROTEIN 9; 1.
DR   Pfam; PF10607; CTLH; 2.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW   Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..653
FT                   /note="Ran-binding protein 9"
FT                   /id="PRO_0000097170"
FT   DOMAIN          72..259
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          290..322
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   DOMAIN          328..385
FT                   /note="CTLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..332
FT                   /note="Interaction with CALB1"
FT                   /evidence="ECO:0000250"
FT   REGION          386..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..653
FT                   /note="Interaction with FMR1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..26
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         330
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96S59"
FT   MOD_RES         402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..107
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028266"
FT   VAR_SEQ         108..115
FT                   /note="NNLRVHYK -> MWESSWVL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028267"
FT   CONFLICT        92
FT                   /note="R -> P (in Ref. 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   653 AA;  71012 MW;  BE810E69B238BBD5 CRC64;
     MSGQPPPPPP QQQPPPPPPP ASAAAPATAP PGLAVGPGPA AGVPVPGLAA GSSAAAPFPH
     GDSALNEQEK ELQRRLKRLY PAVDEQETPL PRSWSPKDKF SYIGLSQNNL RVHYKGHGKT
     PKDAASVRAT HPIPAACGIY YFEVKIVSKG RDGYMGIGLS AQGVNMNRLP GWDKHSYGYH
     GDDGHSFCSS GTGQPYGPTF TTGDVIGCCV NLINNTCFYT KNGHSLGIAF TDLPPNLYPT
     VGLQTPGEVV DANFGQHPFV FDIEDYMREW RTKIQAQIDR FPIGDREGEW QTMIQKMVSS
     YLVHHGYCAT AEAFARSTDQ TVLEELASIK NRQRIQKLVL AGRMGEAIET TQQLYPSLLE
     RNPNLLFTLK VRQFIEMVNG TDSEVRCLGG RSPKSQDSYP VSPRPFSSPS MSPSHGMSIH
     SLAPGKSSTA HFSGFESCSN GVISNKAHQS YCHSKHQLSS LTVPELNSLN VSRSQQVNNF
     TSNDVDMETD HYSNGVGETS SNGFLNGSSK HDHEMEDCDT EMEVDCSQLR RQLCGGSQAA
     IERMIHFGRE LQAMSEQLRR ECGKNTANKK MLKDAFSLLA YSDPWNSPVG NQLDPIQREP
     VCSALNSAIL ETHNLPKQPP LALAMGQATQ CLGLMARSGV GSCAFATVED YLH
//