ID W5M3K8_LEPOC Unreviewed; 487 AA.
AC W5M3K8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=RalA binding protein 1 {ECO:0000313|Ensembl:ENSLOCP00000002966.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002966.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002966.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AHAT01004193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M3K8; -.
DR STRING; 7918.ENSLOCP00000002966; -.
DR Ensembl; ENSLOCT00000002972.1; ENSLOCP00000002966.1; ENSLOCG00000002522.1.
DR eggNOG; KOG4370; Eukaryota.
DR GeneTree; ENSGT00940000154639; -.
DR HOGENOM; CLU_028068_0_0_1; -.
DR InParanoid; W5M3K8; -.
DR OMA; AMERTMM; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000002522; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR CDD; cd04381; RhoGap_RalBP1; 1.
DR Gene3D; 1.20.58.90; -; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR049041; RalBP1-like_Ral-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12783; RALA BINDING PROTEIN 1 RALBP1; 1.
DR PANTHER; PTHR12783:SF5; RALA-BINDING PROTEIN 1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF20924; RLIP76_Ral-bd; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 110..327
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 56352 MW; C5AB052D412296A5 CRC64;
EGYAAFQEDS SGDEAESPSK MKRSKGIHVF KKPSFSKKKE KDFKVKEKPK EEKHKEDKHK
EEKTKDKKSK DLTAAEVVKQ WKEKKKKKKP VAEPEAVLAE APSARPVFGA PLAEAAERTV
LYDGIQLPAV FRECVDYIES YGMKCEGIYR VSGMKSKVDE LKAAYDREEC PSLEEYDAHT
VASLLKQYLR ELPENLLGRE LNARFEEACG RPAEAEKVQE FQRLLAEMPA CSRLLLSWLV
THMDHVIAKE PDTKMNIQNI SIVLSPTMQI SNRVLYVFFT HVKELFGCVQ LKPVVKPLRW
SNMATMPALP ETQESIKEEI RRQEFLLNCL HRDLQAGIKD LSKEERLWEV QRILTALKRK
LREAKRQECE TKIAQEIASL SKEDVSKEEM TENEEEVINI LLAQENEILT EQEELVSMEQ
LLRRQIATEK EEIERLRAEI AEIQSRQQQH GRSETEEYSS DSESESEDEE ELQIILEDLQ
KQNEELE
//
