ID L5MH05_MYODS Unreviewed; 526 AA.
AC L5MH05;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Rho guanine nucleotide exchange factor 3 {ECO:0000256|ARBA:ARBA00023847};
GN ORFNames=MDA_GLEAN10016632 {ECO:0000313|EMBL:ELK37018.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK37018.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for RhoA
CC and RhoB GTPases. {ECO:0000256|ARBA:ARBA00043905}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KB100898; ELK37018.1; -; Genomic_DNA.
DR RefSeq; XP_006754749.1; XM_006754686.2.
DR AlphaFoldDB; L5MH05; -.
DR GeneID; 102766685; -.
DR CTD; 50650; -.
DR eggNOG; KOG4305; Eukaryota.
DR OrthoDB; 24012at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd10572; PH_RhoGEF3_XPLN; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR044129; PH_RhoGEF3_XPLN.
DR PANTHER; PTHR46006:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 3; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 122..304
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 334..449
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 59720 MW; 2BE7EC2851A4565C CRC64;
MVAKDYPFYL SVKRANCSLE VPPASSPAKD AEEPSNKRVK PLSRVTSLAN LIPPVKATPL
KRFSQTLQRS ISFRSESRPD ILTPRPWSRN AAPSSTKRRD SKLWSETFDV CVNQMLTSKE
IKRQEAIFEL SQGEEDLIED LKLAKKAYHD PMLKLSIMTE QELNQIFGTL DSLIPLHEEL
LSQLRDVRKP DGSTEHVGAI LVGWLPCLSS YDSYCSNQVA AKALLDHKKQ DHRVQDFLQR
CLESPFSRKL DLWNFLDIPR SRLVKYPLLL REILRHTPND NPDQQHLEEA INIIQGIVAE
INIKTGESEC HYYKERLLYL EEGQKDSLID SSRVLCCHGE LKNNRGMKLH VFLFQEVLVI
TRAITHNEQL CYQLYRQPIP VKDLLLEDLQ DGEVRLGGSL RGAFSNNERI KNFFRVSFKN
GSQSQTHSLQ ANDTFNKQQW LNCIRQAKET VLCAAGQAGV LDSEGPFLNP AAGSNEPQGE
TKLEQMDQSD SDSDCSMDTS EVSLDCERME QTDSSCGNSK HVESNV
//