RASEF_DANRE
ID RASEF_DANRE Reviewed; 663 AA.
AC A5WW21; A4QP53;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ras and EF-hand domain-containing protein;
GN Name=rasef; ORFNames=si:ch211-39k3.1, zgc:162879;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds predominantly GDP, and also GTP.
CC {ECO:0000250|UniProtKB:Q8IZ41}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8IZ41}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8IZ41}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; CT573123; CAN88515.1; -; Genomic_DNA.
DR EMBL; BC139657; AAI39658.1; -; mRNA.
DR RefSeq; NP_001082896.1; NM_001089427.1.
DR AlphaFoldDB; A5WW21; -.
DR SMR; A5WW21; -.
DR STRING; 7955.ENSDARP00000093820; -.
DR PaxDb; A5WW21; -.
DR PeptideAtlas; A5WW21; -.
DR Ensembl; ENSDART00000103046; ENSDARP00000093820; ENSDARG00000074163.
DR GeneID; 572256; -.
DR KEGG; dre:572256; -.
DR ZFIN; ZDB-GENE-070424-92; zgc:162879.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000165251; -.
DR HOGENOM; CLU_023178_1_0_1; -.
DR InParanoid; A5WW21; -.
DR OMA; ASMQRKH; -.
DR OrthoDB; 1184845at2759; -.
DR PhylomeDB; A5WW21; -.
DR TreeFam; TF313106; -.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-8873719; RAB geranylgeranylation.
DR PRO; PR:A5WW21; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000074163; Expressed in early embryo and 20 other tissues.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Calcium; Coiled coil; Cytoplasm; GTP-binding; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..663
FT /note="Ras and EF-hand domain-containing protein"
FT /id="PRO_0000299579"
FT DOMAIN 1..33
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 35..70
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..297
FT /evidence="ECO:0000255"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 477..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT BINDING 580..583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT BINDING 615..616
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT CONFLICT 68
FT /note="S -> A (in Ref. 2; AAI39658)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="M -> I (in Ref. 2; AAI39658)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="E -> Q (in Ref. 2; AAI39658)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="S -> P (in Ref. 2; AAI39658)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="K -> E (in Ref. 2; AAI39658)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="N -> S (in Ref. 2; AAI39658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 75858 MW; CA4667BBB995D9FA CRC64;
MNHAELRRLF AACDGNQSGR VEYEDFTTVC RELNVPADDI RTLFNKFDLD GDGYINFNDF
SSSFQEVSEA LNLASLGNCL HSQRRAWDEF ENTLDGDVAF YLGRQWDALS ELYEGIHSTS
DELLLQQFED LIRALVTEIR EHRMESEQLE TSLRRTEEVS SSQLAEMEED LQQQLIHTER
RVREEEQKKL DESIAMLQIK HENELADLQT TIERLTKQYQ EESKLNTPRE DSVKLRAQIK
DLMEENEELR ASLMKAQMNV SILQVELDKL KNAFTDQKRQ HERESDDLKK MVMEFQSYSS
HIEMLQEMNK SLYDSNDGLR SALSQENAST KRQLSPRNEV LPRKMKPIRQ STMNQSSFTN
EEDTLALVKC WAEKYLDSGV SVQSEMDAMS GIDYDSDDSH HSVETVHHSY SCVPSELEVS
EVKPEALRSV ARSTVGSISS SLRRRLSAFP VKQNEEDLLD TQDLAPVYRL VLAGDAGSGK
SSFLLRLSLN EFRGDIQTTL GVDFQIKKML VDGEKTNLQI WDTAGQERFR SIARSYFRKA
HGVLLLYDVT SESSFLNVRE WVEQIRESTD EDIPMCIIGN KVDLRAARPE GSCVSSIHGE
KLAMNYNALF CEASAKEGTN VIEAVLHLAR EVKKHVKLGR RSESQVKLSL HKRRKTLSNC
CGV
