RADIL_MOUSE
ID RADIL_MOUSE Reviewed; 1099 AA.
AC Q69Z89; Q8BNL0; Q8C549; Q8C6X2; Q8CAL1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ras-associating and dilute domain-containing protein;
GN Name=Radil; Synonyms=Kiaa1849;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreatic islet;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP FUNCTION.
RX PubMed=17704304; DOI=10.1101/gad.1561507;
RA Smolen G.A., Schott B.J., Stewart R.A., Diederichs S., Muir B.,
RA Provencher H.L., Look A.T., Sgroi D.C., Peterson R.T., Haber D.A.;
RT "A Rap GTPase interactor, RADIL, mediates migration of neural crest
RT precursors.";
RL Genes Dev. 21:2131-2136(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-245; SER-248;
RP SER-250; SER-432 AND SER-915, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, 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).
CC -!- FUNCTION: Downstream effector of Rap required for cell adhesion and
CC migration of neural crest precursors during development.
CC {ECO:0000269|PubMed:17704304}.
CC -!- SUBUNIT: Interacts with RAP1A; in a GTP-dependent manner. Does not
CC interact with members of the Ras family. Interacts (via PDZ domain)
CC with KIF14; is recruited to the microtubule network restricting its
CC interaction with activated RAP1A (By similarity).
CC {ECO:0000250|UniProtKB:Q96JH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q69Z89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69Z89-2; Sequence=VSP_016101, VSP_016103;
CC Name=3;
CC IsoId=Q69Z89-3; Sequence=VSP_016100;
CC Name=4;
CC IsoId=Q69Z89-4; Sequence=VSP_016101, VSP_016102;
CC Name=5;
CC IsoId=Q69Z89-5; Sequence=VSP_016101;
CC -!- SIMILARITY: Belongs to the RADIL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38904.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD32555.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173277; BAD32555.1; ALT_INIT; mRNA.
DR EMBL; AK038570; BAC30049.1; -; mRNA.
DR EMBL; AK052964; BAC35223.1; -; mRNA.
DR EMBL; AK079539; BAC37675.1; -; mRNA.
DR EMBL; AK083410; BAC38904.1; ALT_FRAME; mRNA.
DR EMBL; BC056483; AAH56483.1; -; mRNA.
DR CCDS; CCDS19827.1; -. [Q69Z89-5]
DR CCDS; CCDS80453.1; -. [Q69Z89-1]
DR RefSeq; NP_001297681.1; NM_001310752.1. [Q69Z89-1]
DR RefSeq; NP_848817.2; NM_178702.4. [Q69Z89-5]
DR RefSeq; XP_006504749.1; XM_006504686.2. [Q69Z89-3]
DR AlphaFoldDB; Q69Z89; -.
DR SMR; Q69Z89; -.
DR STRING; 10090.ENSMUSP00000064539; -.
DR iPTMnet; Q69Z89; -.
DR PhosphoSitePlus; Q69Z89; -.
DR jPOST; Q69Z89; -.
DR MaxQB; Q69Z89; -.
DR PaxDb; Q69Z89; -.
DR PeptideAtlas; Q69Z89; -.
DR PRIDE; Q69Z89; -.
DR ProteomicsDB; 255025; -. [Q69Z89-1]
DR ProteomicsDB; 255026; -. [Q69Z89-2]
DR ProteomicsDB; 255027; -. [Q69Z89-3]
DR ProteomicsDB; 255028; -. [Q69Z89-4]
DR ProteomicsDB; 255029; -. [Q69Z89-5]
DR Antibodypedia; 43694; 148 antibodies from 20 providers.
DR Ensembl; ENSMUST00000063635; ENSMUSP00000064539; ENSMUSG00000029576. [Q69Z89-5]
DR Ensembl; ENSMUST00000085758; ENSMUSP00000082910; ENSMUSG00000029576. [Q69Z89-1]
DR Ensembl; ENSMUST00000110784; ENSMUSP00000106411; ENSMUSG00000029576. [Q69Z89-3]
DR GeneID; 231858; -.
DR KEGG; mmu:231858; -.
DR UCSC; uc009ais.2; mouse. [Q69Z89-1]
DR UCSC; uc009aiu.2; mouse. [Q69Z89-4]
DR CTD; 55698; -.
DR MGI; MGI:2443088; Radil.
DR VEuPathDB; HostDB:ENSMUSG00000029576; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000159293; -.
DR HOGENOM; CLU_010386_0_0_1; -.
DR InParanoid; Q69Z89; -.
DR OMA; CIPFQNE; -.
DR OrthoDB; 447883at2759; -.
DR PhylomeDB; Q69Z89; -.
DR TreeFam; TF350641; -.
DR BioGRID-ORCS; 231858; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Radil; mouse.
DR PRO; PR:Q69Z89; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q69Z89; protein.
DR Bgee; ENSMUSG00000029576; Expressed in habenula and 170 other tissues.
DR ExpressionAtlas; Q69Z89; baseline and differential.
DR Genevisible; Q69Z89; MM.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR CDD; cd00060; FHA; 1.
DR CDD; cd15472; Myo5p-like_CBD_Rasip1; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR037983; CBD_Rasip1/Radil.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Developmental protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1099
FT /note="Ras-associating and dilute domain-containing
FT protein"
FT /id="PRO_0000050804"
FT DOMAIN 90..193
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 302..377
FT /note="FHA"
FT DOMAIN 525..792
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT DOMAIN 1000..1085
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 221..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JH8"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..269
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016100"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_016101"
FT VAR_SEQ 485..1079
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016102"
FT VAR_SEQ 1019..1099
FT /note="HTPLGAQGLYIQTLLPGSPAASDGRLSLGDQILEVNGSSLRGVSYMRAVDLI
FT RHGGKKMRFLVAKSDMETAKKIRFRNPPS -> VRTLGPQPSTPPTPTPCFCRLILYSV
FT STVEASERCPDCLMGLPLGALMEPSAFPWNIPGSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_016103"
FT CONFLICT 575
FT /note="C -> S (in Ref. 2; BAC37675)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="R -> Q (in Ref. 2; BAC38904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1099 AA; 120355 MW; CB1940EFFD10BC0D CRC64;
MGSSIFLGLQ PSPSHWLKSS VVIHEDAPTM FYGTQLIMSP PTKNKLKRQS QLLSTMLSRT
LSYKYRDLDS TFCSLGASDD PSELSTQLSA PGVLKVFGDS VCTGTHYKSV LATGSSSAQE
LVKEALERYA LDPECAGQYV LCDVVGQAGD SGQRWQAQCF RVFGDNEKPL LIQELWKPRE
GLSRRFELRK KSDVEELASR DVDTTTAGIN AQARRLQRIR AKGTPALTSE AAQSSPPTRL
RRTVSETSLS PAPSLPEAAQ RPEEPVPEAM RYSLYQCPHL LLLQGYSQQH DSLVYVLSKE
RHTVGQRTPS SKPSISLSAP DILPLHCTIR RHQSPEGGPA GTRLVLEPIT GASVSVNFSE
VGRNPVVLQH GDLLSLGLYY LLLFKDPGQA QPLPACALAR LGAAPQSCRM CGAVLRARGA
PSLPAAVVRR RSLLLEFEPD VEDTLLQRIM TLIEPGGDDH KLTPAFLLCL CIQHSAMHFQ
PGTFRHLLLK ISKRVRDTVW EKTKELAEKQ AQLQEPISWA SFPMADLVPD LQHILFWMSN
SIELLYFIQQ KSPLYVQSME EELDVTGSKE SLFSCTLTAS EEAMAALEEV VLYAFQQCVY
YLSKCLYVCL PALLECPPFQ TERRESWRSG PALPEELRRV VSVFQATLDL LQQLQMHPEV
ASQMLAYLFF FSGTLLLNQV LDKGPSLSCF HWPRGVQVCA RLQQFLEWAR SAGLGAPAER
FFRKLSCTLH LLATPRAQLI QMSWATLRVT FPALNPAQLH RLLTQYQLAS AMGPVSAWEP
GAPDGPEAFQ SEDILESYEN PPPIVLPSQG FQVDLEADCV EDSIYQHLLY IRHFLWGLRG
QASPDSGPAQ PESIEGLYHT IPEGHLEGHG CPLANRDPGR VAVETAPPHS LPVTGAPRAQ
GPPGRQPTRG DRRGSQAGSL HTDSSCMLTP PSTPLGLEPA GPSWPEPSGL CGRAVLDGQR
NGPGGLPGAV LEGDAIQDAE PPAEASSPSS SAEDFCYVFM VELERGPSGL GMGLIDGMHT
PLGAQGLYIQ TLLPGSPAAS DGRLSLGDQI LEVNGSSLRG VSYMRAVDLI RHGGKKMRFL
VAKSDMETAK KIRFRNPPS
