RASEF_CAEBR
ID RASEF_CAEBR Reviewed; 634 AA.
AC Q619T5; A8XJC9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ras and EF-hand domain-containing protein homolog;
DE Flags: Precursor;
GN Name=rsef-1 {ECO:0000312|WormBase:CBG14124a};
GN Synonyms=tag-312 {ECO:0000312|WormBase:CBG14124a};
GN ORFNames=CBG14124 {ECO:0000312|WormBase:CBG14124a};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Binds GTP and GDP. Plays a role in uterine seam cell
CC development. {ECO:0000250|UniProtKB:Q22908,
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; HE600983; CAP32754.3; -; Genomic_DNA.
DR RefSeq; XP_002644316.1; XM_002644270.1.
DR AlphaFoldDB; Q619T5; -.
DR SMR; Q619T5; -.
DR STRING; 6238.CBG14124; -.
DR PRIDE; Q619T5; -.
DR EnsemblMetazoa; CBG14124a.1; CBG14124a.1; WBGene00034723.
DR GeneID; 8586311; -.
DR KEGG; cbr:CBG_14124; -.
DR CTD; 8586311; -.
DR WormBase; CBG14124a; CBP22969; WBGene00034723; Cbr-rsef-1.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_023178_1_0_1; -.
DR InParanoid; Q619T5; -.
DR OMA; EHYHSES; -.
DR OrthoDB; 1184845at2759; -.
DR Proteomes; UP000008549; Chromosome X.
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; PF13833; EF-hand_8; 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; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW Calcium; Coiled coil; Cytoplasm; GTP-binding; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..631
FT /note="Ras and EF-hand domain-containing protein homolog"
FT /id="PRO_0000299581"
FT PROPEP 632..634
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370841"
FT DOMAIN 5..33
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 33..68
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..310
FT /evidence="ECO:0000255"
FT COMPBIAS 308..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT BINDING 585..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ41"
SQ SEQUENCE 634 AA; 72268 MW; 5B905A5A027069DD CRC64;
MANPDVENLF SLCDSESKGF LTMEDLKKVC PQLDDNDLRF IFNELDRDGS GKIEKMEFLQ
GFQETVQHGE SRGLNGMQRR ASVAFDDGGP VFRRDELVFE SESDSSSRPA IRVYDEEHYH
SESDTNINID FSVPCQEEVL VLYEQLQSSG VPALLRKFER VVGSFHKELS EKKHENERLQ
RIYASEREMY NRRMEEMESE VDQQLELIEM KARQEERERL TKEKEEMRER MSEEMSEMRT
NIERLQRMEK VLERENERLN HQKDLSDKLK VVNEENNDLR QNLAENHLEL AMIKSELAQV
RADFDQKQDE LSARRDQASH ATEESESVRK QLQLLFDANR KLHETNESLR DALDSRASVL
RQFNLRTPSP GLINSNRNSV ENFQTSTNMF KSVPLHAISD EEPDPETSLI LDDAHSLQGM
DIAEGLVGLN DANGPAERTF RIVMCGDAAV GKSSFVMRVI RRQFTNQLPS TLGVDFHVKT
VNVDGRNVAL QLWDTAGQER FRSLCKSYFR RADGAILVYD VCAEHSFLRV RDWIETIKES
TERSIPIILV GNKVDMRLQT PGAVAKTDGA SMAAAMGVLF METSALDGSN IDNAMLALTR
ELMAVEDVEI RSTGVVLNPA ATKKGGCFSK CRGS
