ID M3Y6Q0_MUSPF Unreviewed; 1595 AA.
AC M3Y6Q0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Rho guanine nucleotide exchange factor 5 {ECO:0000313|Ensembl:ENSMPUP00000007001.1, ECO:0000313|RefSeq:XP_044919047.1, ECO:0000313|RefSeq:XP_044919048.1};
GN Name=ARHGEF5 {ECO:0000313|Ensembl:ENSMPUP00000007001.1,
GN ECO:0000313|RefSeq:XP_044919047.1, ECO:0000313|RefSeq:XP_044919048.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007001.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007001.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044919047.1, ECO:0000313|RefSeq:XP_044919048.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044919047.1,
RC ECO:0000313|RefSeq:XP_044919048.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AEYP01078306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004772138.1; XM_004772081.2.
DR RefSeq; XP_044919047.1; XM_045063112.1.
DR RefSeq; XP_044919048.1; XM_045063113.1.
DR STRING; 9669.ENSMPUP00000007001; -.
DR Ensembl; ENSMPUT00000007117.1; ENSMPUP00000007001.1; ENSMPUG00000007058.1.
DR KEGG; mpuf:101681990; -.
DR eggNOG; KOG3523; Eukaryota.
DR GeneTree; ENSGT01030000234571; -.
DR HOGENOM; CLU_003633_0_0_1; -.
DR OMA; GQDSQEF; -.
DR OrthoDB; 12272at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0002408; P:myeloid dendritic cell chemotaxis; IEA:Ensembl.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:1904591; P:positive regulation of protein import; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR CDD; cd01221; PH_ephexin; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11940; SH3_ARHGEF5_19; 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR029212; ARHGEF5/35_N.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR047271; Ephexin-like.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR047270; PH_ephexin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12845:SF2; DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR12845; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF15441; ARHGEF5_35; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1172..1356
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1508..1569
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1595 AA; 173028 MW; 79183744AA04FEBB CRC64;
MEAEEPQHGV STPIPALAEL SVTPEALRRS RQTAALGPEA QEGWEPSSAW AEGRGLSETQ
RGASRDVKSC ATKSVTSFPK EAPAGAETTQ EDSVGEMGDT PELQELVPHS PTGGGARTPA
PSQLGACLVQ GEHLDMAPGS GELGGGVEME FRLEPTSSTG ETGHAEEKGA FPDASAQPRF
GPSCEQCPEE THQPGDSVRH GEEPQLTAAR EGPGSGGPEC LLAAEGLGEQ GPADAGFQEE
AAVGEGGRSG EQEQKGEQGD RTKGEQRPKQ QQRQGDPMPA RQGERTGLCG DSEGLHCPEQ
EMKTQGWGDP PQGEEGKREF GGPQESSVDA QNEERQSLVG RSGKGTGRQE GQGLQRKVMF
AQRQEEEPGN WDGDPLRREA GERSTEEGEA RDGPSTQAPV ASEVSSPCDL FLDTCHPKTS
VPGTPREPRA EEPLPVAPAP ARESGQWSSQ PVSLPGSFPA GESPDQEIAL DSQQEGSELG
KGAVFTQGTE LVSAGTSAAP PRTPGSAPCS PADVSPSTAT PSSASPPVAS SRRESSLAAH
SSETSRASVW TNNTSHAEAS GTPPAPLRGF LTTEATVEIS TSSSQANPPS PLGHSTGAFQ
HLRSNSFPGS HRTEPTPDLL GLSLSFSHSE LPQEASKPAI YGSVIPRRDR KSGRDGRIIP
ESPSSLSALG QDSQEFTSDP ERSGSPCSTQ PCGSRHTSAS APESIACGSS PPLVSVDARI
HEPLPPPPPE KRRVHPSMVE RDSHLHAGVP MLKRCGQPLP LAPGSGLHGP PKGPLPPVPD
SLVARQHRPL PSTPDTPHPT QTSPSHRLRY NKPLPPTPDF SQTHHSVPSS SSPRTYRPLP
PVPIVDPPTE PPPLPPKSRG RSRSTQGELM NAGGQGKPRP ICPERTVATP HSVGRTSWPP
AMGRSTDSSA PTSRSKSEGA PGMAFSNVAT LLSPSSPTTP WSLELPGPTS EPGPSEESGA
PGRGSLRRTA PQEGANGLRR LDVGQARQPA KLSHPHLEKA SSWPHRRDPG RPPASSSGQV
VDPGEGSSRH KGWNRQGLRR PSILPEGCSD TRGPAVEKVL GPSDTIVFRE KKPKEVMGGF
SRRRSKLINS SQLLYQEYSD VVLNKEIQSQ QRLDSLGEAT GPASPRQPRR TLVSSESYLQ
RLSMASSGSL WQEIPVVRNS TVLLSMTHED QKLQEAKFEL IVSEASYLRS LHVAVDHFQL
SAPLRATLSN QEYQWLFSRL QDVRDVSTMF LSDLEENFER NIFTFQVCDV VLNHAPGFRR
VYLPYVTNQT YQERTFQGLL TSNSSFREVL EKLESDPVCQ RLSLKSFLIL PFQRITRLKL
LLQNILKRTQ PGSSEEAEAT KAHHALEELI RDCNNNVQRM RRTEELIYLS QKIEFECKIF
PLISQSRWLV KSGELTALEF SLSPGLRRKL NTRPVHLHLF NDCLLLSRPR EGSRFLVFDH
APFSSIRGEK CEMKLHGPHK NLFRLFLLHN AQGTQAEFLF STETQSEKLR WISALAMPRE
ELDLLECYDS PQVQCLRAYK PRENDELALE KADVVMVTQQ SSDGWLEGMR LSDGERGWFP
VQQVEFISNP DVRARNLKEA HRVKTAKLQL VEQRT
//
