ID M3Y0X6_MUSPF Unreviewed; 909 AA.
AC M3Y0X6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000256|ARBA:ARBA00017262};
DE AltName: Full=Guanine nucleotide exchange factor H1 {ECO:0000256|ARBA:ARBA00031760};
GN Name=ARHGEF2 {ECO:0000313|Ensembl:ENSMPUP00000004977.1};
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:ENSMPUP00000004977.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000004977.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
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DR EMBL; AEYP01094725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01094726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000004977; -.
DR Ensembl; ENSMPUT00000005062.1; ENSMPUP00000004977.1; ENSMPUG00000005016.1.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000158341; -.
DR HOGENOM; CLU_002466_1_1_1; -.
DR InParanoid; M3Y0X6; -.
DR OMA; RVFQQGM; -.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0055059; P:asymmetric neuroblast division; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR CDD; cd20877; C1_ARHGEF2; 1.
DR CDD; cd13393; PH_ARHGEF2; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR037806; ARHGEF2_PH.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF20; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell junction {ECO:0000256|ARBA:ARBA00022427};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 36..83
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 233..430
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 470..569
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 681..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 102067 MW; D507D16DE487DCE2 CRC64;
SGRLVPSASL PVSLPLAQAR EKEKMKEAKD ARYTNGHLFT TISVSGMTMC YACNKSITAK
EALICPTCNV TIHNRCKDTL ANCTKVKQKQ QKAALLKNNT ALQSVSLRSK TTPRERPSSA
IYPSDSFRQS LLGSRRGRSS LSLAKSVSTT NIAGHFNEES PLGLRRILSQ STDSLNMRNR
TLSVESLIDE GAEVIYSELM SDFETDERDF AADSWSLAVD SGFLQQQKKE VMKQQDVIYE
LIQTELHHVR TLKIMTRLFR AGMLEELQLE PGVVQGLFPC VDELSDIHTR FLSQLLERRR
QSLCPGSTRN FVIHRLGDLL INQFSGPSAE QMRKTYSEFC SRHTKALKLY KELCARDKRF
QQFIRKVTRS AVLKRHGVQE CILLVTQRVT KYPVLISRIL QHSHGPEEER QDLTTALGLV
KELLSNVDQD VHELEKGARL QEIYHRMDPR AQAPVPGKGP FGREELLRRR LIHDGCLLWK
TATGRFKDVL MLLMTDVLLF LQEKDQKYIF PALDKPSVVS LQNLIVRDIA NQEKGMFLIS
AAPPEMYEVH TASRDDRSTW IRVIQQSVRV CPSREDFPLI ETEHEAYLRR IKMELQQKDQ
ALVELLQEKV GLFAEMTHFQ VDEDGGGLTL PTLPRGLFRS ESLECPRGER LLQDAIREVE
GLKDLLVGPG VELLLTAREP ALPGDLDSGG STSPGVTANG EAGTFNGSTE LCGTDSDSSR
KDRNGNQLRA PQEEALQRLV NLYGLLHGLQ AAVAQQDTLM EARFPEGPER REKLARANSR
XRPRGRETVA GQLGRRPRRR RGMGAAGPAE LTSRPAAFPA GPSQPSRGHE RLDLSVTIRS
VHRPFEDRER QDLGSPEERL QDSSDPDTGS EEEGGCRLSP PHSPRDFTRM QDIPEEIESR
DGEPVASES
//
