RBP10_MOUSE
ID RBP10_MOUSE Reviewed; 620 AA.
AC Q6VN19; Q69ZJ1; Q8C328; Q8R1E6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ran-binding protein 10;
DE Short=RanBP10;
GN Name=Ranbp10; Synonyms=Kiaa1464;
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].
RX PubMed=14684163; DOI=10.1016/j.bbrc.2003.11.124;
RA Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.;
RT "A novel MET-interacting protein shares high sequence similarity with
RT RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.";
RL Biochem. Biophys. Res. Commun. 313:320-326(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-620.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 474-620.
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP FUNCTION, INTERACTION WITH RAN; TUBB1 AND TUBB5, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-301.
RX PubMed=18347012; DOI=10.1074/jbc.m709397200;
RA Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr.,
RA Shivdasani R.A.;
RT "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates
RT noncentrosomal microtubules.";
RL J. Biol. Chem. 283:14109-14119(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19801445; DOI=10.1182/blood-2009-04-216804;
RA Kunert S., Meyer I., Fleischhauer S., Wannack M., Fiedler J.,
RA Shivdasani R.A., Schulze H.;
RT "The microtubule modulator RanBP10 plays a critical role in regulation of
RT platelet discoid shape and degranulation.";
RL Blood 114:5532-5540(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-362; SER-365; SER-367;
RP SER-369; SER-451 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10] {ECO:0007744|PDB:5JIA}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 29-238, AND INTERACTION WITH
RP DDX4.
RX PubMed=27622290; DOI=10.1016/j.jmb.2016.09.004;
RA Hong S.K., Kim K.H., Song E.J., Kim E.E.;
RT "Structural Basis for the Interaction between the IUS-SPRY Domain of RanBPM
RT and DDX-4 in Germ Cell Development.";
RL J. Mol. Biol. 428:4330-4344(2016).
CC -!- FUNCTION: May act as an adapter protein to couple membrane receptors to
CC intracellular signaling pathways (Probable). Core component of the CTLH
CC E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin
CC from UBE2H and mediates ubiquitination and subsequent proteasomal
CC degradation of the transcription factor HBP1 (By similarity). Enhances
CC dihydrotestosterone-induced transactivation activity of AR, as well as
CC dexamethasone-induced transactivation activity of NR3C1, but does not
CC affect estrogen-induced transactivation (By similarity). Acts as a
CC guanine nucleotide exchange factor (GEF) for RAN GTPase
CC (PubMed:18347012). May play an essential role in hemostasis and in
CC maintaining microtubule dynamics with respect to both platelet shape
CC and function (PubMed:19801445). {ECO:0000250|UniProtKB:Q6VN20,
CC ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:19801445, ECO:0000305}.
CC -!- SUBUNIT: May form homodimers. Identified in the CTLH complex that
CC contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or
CC alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within
CC this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8,
CC WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4,
CC MKLN1, ARMC8 and YPEL5 have ancillary roles. Interacts with RAN and
CC RANBP9. Interacts with the HGF receptor MET. Interacts with AR (By
CC similarity). Interacts with TUBB1 (PubMed:18347012). Interacts with
CC YPEL5 (By similarity). May interact with TUBB5 (PubMed:18347012).
CC Interacts with DDX4 (PubMed:27622290). {ECO:0000250|UniProtKB:Q6VN20,
CC ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:27622290}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18347012}. Nucleus
CC {ECO:0000269|PubMed:18347012}. Note=Predominantly cytoplasmic.
CC Associates with cytoplasmic microtubules in mature megakaryocytes and
CC platelets.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in spleen and liver.
CC Expressed in megakaryocytes and platelets (at protein level).
CC {ECO:0000269|PubMed:18347012}.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable and show no conspicuous
CC phenotype. They have normal platelet counts and only slightly reduced
CC proplatelet formation. Resting platelets tend to have a more spherical
CC shape. Many platelets exhibit disorders in microtubule filament numbers
CC and localization. The animals show a markedly prolonged bleeding time.
CC Granule release is also reduced. {ECO:0000269|PubMed:19801445}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24698.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAR01221.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AY337314; AAR01221.1; ALT_INIT; mRNA.
DR EMBL; BC024698; AAH24698.1; ALT_INIT; mRNA.
DR EMBL; AK173177; BAD32455.1; -; mRNA.
DR EMBL; AK087165; BAC39817.1; -; mRNA.
DR CCDS; CCDS22613.1; -.
DR RefSeq; NP_665823.2; NM_145824.4.
DR PDB; 5JIA; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=29-238.
DR PDBsum; 5JIA; -.
DR AlphaFoldDB; Q6VN19; -.
DR SMR; Q6VN19; -.
DR BioGRID; 216672; 5.
DR IntAct; Q6VN19; 2.
DR MINT; Q6VN19; -.
DR STRING; 10090.ENSMUSP00000040045; -.
DR iPTMnet; Q6VN19; -.
DR PhosphoSitePlus; Q6VN19; -.
DR SwissPalm; Q6VN19; -.
DR EPD; Q6VN19; -.
DR MaxQB; Q6VN19; -.
DR PaxDb; Q6VN19; -.
DR PRIDE; Q6VN19; -.
DR ProteomicsDB; 253183; -.
DR Antibodypedia; 44334; 86 antibodies from 24 providers.
DR DNASU; 74334; -.
DR Ensembl; ENSMUST00000239468; ENSMUSP00000159340; ENSMUSG00000037415.
DR GeneID; 74334; -.
DR KEGG; mmu:74334; -.
DR UCSC; uc009nec.1; mouse.
DR CTD; 57610; -.
DR MGI; MGI:1921584; Ranbp10.
DR VEuPathDB; HostDB:ENSMUSG00000037415; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000158257; -.
DR InParanoid; Q6VN19; -.
DR OrthoDB; 1106989at2759; -.
DR TreeFam; TF331658; -.
DR Reactome; R-MMU-8851805; MET activates RAS signaling.
DR BioGRID-ORCS; 74334; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ranbp10; mouse.
DR PRO; PR:Q6VN19; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6VN19; protein.
DR Bgee; ENSMUSG00000037415; Expressed in fetal liver hematopoietic progenitor cell and 243 other tissues.
DR ExpressionAtlas; Q6VN19; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP: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 Pfam; PF10607; CLTH; 1.
DR Pfam; PF08513; LisH; 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 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT CHAIN 2..620
FT /note="Ran-binding protein 10"
FT /id="PRO_0000305238"
FT DOMAIN 35..222
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 253..285
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 291..348
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VN20"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 301
FT /note="L->I: Complete loss RAN-GEF activity. Partial loss
FT of RAN-binding."
FT /evidence="ECO:0000269|PubMed:18347012"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:5JIA"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5JIA"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5JIA"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5JIA"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 101..112
FT /evidence="ECO:0007829|PDB:5JIA"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5JIA"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5JIA"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5JIA"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:5JIA"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:5JIA"
SQ SEQUENCE 620 AA; 67188 MW; 6A22ADAECC7B57F5 CRC64;
MAAATADPGA GNPQAGDSSG GDSGGGLPSP GEQELSRRLQ RLYPAVNQHE TPLPRSWSPK
DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC GIYYFEVKIV SKGRDGYMGI
GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF CSSGTGQPYG PTFTTGDVIG CCVNLINGTC
FYTKNGHSLG IAFTDLPANL YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT
VHGFPISARL GEWQAVLQNM VSSYLVHHGY CSTATAFARM TETPIQEEQA SIKNRQKIQK
LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS LSSRSPKSQD
SYPGSPSLSP RHGPSSSHIH NTGADSPSCS NGVASTKNKQ NHSKYPAPSS SSSSSSSSSS
SSPSSVNYSE SNSTDSTKSQ PHSSTSNQET SDSEMEMEAE HYPNGVLESV STRIVNGAYK
HDDLQTDESS MDDGHPRRQL CGGNQAATER IILFGRELQA LSEQLGREYG KNLAHTEMLQ
DAFSLLAYSD PWSCPVGHQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR
LMARAGLGSC SFARVDDYLH
