RADIL_DANRE
ID RADIL_DANRE Reviewed; 1124 AA.
AC A7UA95;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ras-associating and dilute domain-containing protein;
GN Name=radil;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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).
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.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed and enriched in the anterior
CC part of the embryos. {ECO:0000269|PubMed:17704304}.
CC -!- DEVELOPMENTAL STAGE: Present at very low level in one-cell embryos,
CC suggesting the presence of maternally deposited transcripts. Increases
CC upon the onset of zygotic transcription (around the 1000-cell stage),
CC eventually peaking at 72 hpf. {ECO:0000269|PubMed:17704304}.
CC -!- MISCELLANEOUS: Knockdown results in multiple defects in neural crest-
CC derived lineages such as cartilage, pigment cells, and enteric neurons.
CC -!- SIMILARITY: Belongs to the RADIL family. {ECO:0000305}.
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DR EMBL; EU031809; ABU24309.1; -; mRNA.
DR RefSeq; NP_001096039.1; NM_001102569.2.
DR AlphaFoldDB; A7UA95; -.
DR SMR; A7UA95; -.
DR STRING; 7955.ENSDARP00000101722; -.
DR PaxDb; A7UA95; -.
DR PeptideAtlas; A7UA95; -.
DR GeneID; 562363; -.
DR KEGG; dre:562363; -.
DR CTD; 55698; -.
DR ZFIN; ZDB-GENE-071206-1; radil.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; A7UA95; -.
DR OrthoDB; 447883at2759; -.
DR PhylomeDB; A7UA95; -.
DR PRO; PR:A7UA95; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0051020; F:GTPase binding; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IMP:ZFIN.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell adhesion; Developmental protein; Reference proteome.
FT CHAIN 1..1124
FT /note="Ras-associating and dilute domain-containing
FT protein"
FT /id="PRO_0000355182"
FT DOMAIN 61..164
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 284..342
FT /note="FHA"
FT DOMAIN 516..809
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT DOMAIN 1027..1112
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 226..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 124934 MW; 30FE3E46D82D9483 CRC64;
MFYGSSSASM SLPSKNRLKR QSRTFTQVLY RTLSYRDRRS VTDLPEQVRD DPAELSTQSS
APGVLKIFGD EISAGANYKS VLATPRSSAQ ELIKEALERY SLNKTSACNF VLCDVIGRFE
GPDRRWRTEC LRALGNNEKP LLLQDLWKPK EGFSRRFELR RRAEVEELAA KEKDTVTADI
NAQARKLQRN RAKGTMTLQH GSSFCRSLSE TSLNLVGLPG EEPKRYYSTL PGPIRTRSAR
DSEIRKERDG GGVKHSLYQS PHLLLLQGYN QQDCLVYLLN REQHTVGQET ASARPNICLS
SPDVLPLHCR IRRAAQRRSS SDQRLLLEPV AHGNVLVNFM RIERPTPIRH GDLLSFGAHY
IFLYKDPLSA KPLPAQTLTR LRTLAKLCDG ESGGLPEKGD ACRMCGAVLH EPAASSRRSS
KAPARGSQKR KLALEFERAH EDALVNRVLT LIEPSGDDHK LTPAYLLCLC IKHSANTFPP
GSFGKLLQKI AKRIQTIAWE KTKELAQKQA QHQDPASLSL LSISDLVPDL QFIFFWMSNA
IEILYFIQQK SPAYMQTIEL MDDKAGSKES LLSATISANE EAMTILEEVI MYTFQQCVYY
ITKTLYVVLP GLLDCNPFGT EPSSEQCRRA AGVCVCAVCV MPEAVRRVVS VFQTTSDLLQ
QYQVHSEIQS QMFAYLFFFT NVSLFNQLID KGPARGWFQR SRVLQIQASV KILLDWAKGA
GHNHLAQKFF AKFCSTVTIL ASPPQQLSQM SWKALCAEHP SLKPVQLHRI LTQYQLMAEL
GPLPIWQPSS EDEAYIYRTV DLLESFENHP PIVLPSAGFK VDLESDCVED SIYRQLLYVR
HFVWGLRTKT HPSNGCTDRQ DAQREPPQPH SSPHPAPSVR GEGEGEVRSS STTLGGRGEG
AGAEDRTRDK PTHGIHYRNG SGARYANQSQ ATDSSCILTP PNTPLYPEHT YIQSNTAHYP
EHASQEHTHT HSHTKTNGCM RSTPEHKKIN GFISNGIEGP LSGCGFPFPV PVSHLGPKSD
DICSVFVVDL DKGPYGLGMG LIDGLHTPLN SPGIYIRTLI PDGPAAADGR LCIGDRILAV
NGTSLIGADY QSAVDLIRLG GGRLRFLVAK SDLEVSEKIS ASSC
