RPGF4_RAT
ID RPGF4_RAT Reviewed; 436 AA.
AC Q9Z1C7;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Rap guanine nucleotide exchange factor 4;
DE AltName: Full=Exchange factor directly activated by cAMP 2;
DE AltName: Full=Exchange protein directly activated by cAMP 2;
DE Short=EPAC 2;
DE AltName: Full=cAMP-regulated guanine nucleotide exchange factor II;
DE Short=cAMP-GEFII;
DE Flags: Fragment;
GN Name=Rapgef4; Synonyms=Cgef2, Epac2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9856955; DOI=10.1126/science.282.5397.2275;
RA Kawasaki H., Springett G.M., Mochizuki N., Toki S., Nakaya M., Matsuda M.,
RA Housman D.E., Graybiel A.M.;
RT "A family of cAMP-binding proteins that directly activate rap1.";
RL Science 282:2275-2279(1998).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and
CC RAP2A small GTPases that is activated by binding cAMP. Seems not to
CC activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis
CC through interaction with RIMS2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RIMS1 and RIMS2. Probably part of a complex
CC with RIMS2 and GTP-activated RAB3A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
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DR EMBL; U78517; AAD03423.1; -; mRNA.
DR AlphaFoldDB; Q9Z1C7; -.
DR SMR; Q9Z1C7; -.
DR STRING; 10116.ENSRNOP00000010630; -.
DR PhosphoSitePlus; Q9Z1C7; -.
DR PaxDb; Q9Z1C7; -.
DR PRIDE; Q9Z1C7; -.
DR UCSC; RGD:621886; rat.
DR RGD; 621886; Rapgef4.
DR eggNOG; KOG2378; Eukaryota.
DR InParanoid; Q9Z1C7; -.
DR PhylomeDB; Q9Z1C7; -.
DR Reactome; R-RNO-354192; Integrin signaling.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-392517; Rap1 signalling.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0005929; C:cilium; IDA:RGD.
DR GO; GO:0044316; C:cone cell pedicle; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030552; F:cAMP binding; IDA:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0061548; P:ganglion development; IEP:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0046879; P:hormone secretion; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IDA:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:1904457; P:positive regulation of neuronal action potential; IMP:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:1901423; P:response to benzene; IEP:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR CDD; cd00155; RasGEF; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Exocytosis; Guanine-nucleotide releasing factor; Membrane;
KW Reference proteome.
FT CHAIN <1..436
FT /note="Rap guanine nucleotide exchange factor 4"
FT /id="PRO_0000068872"
FT DOMAIN <1..59
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 197..434
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT NON_TER 1
SQ SEQUENCE 436 AA; 50117 MW; 5E73FE45DEB6E3D2 CRC64;
RVIRLVLQWA AMYGDLLQED DVAMAFLEEF YVSVSDDARM MVAFKEQLAE LEKTVKQISE
DAKAPQKKHK VLLQQFNTGD ERAQKRQPIR GSDEVLFKVY CIDHTDTTIR VPVAASVKEV
ISAVADKLGS GEGLIIVKMN SGGEKVVLKP NDVSVFTTLT INGRLFACPR EQFDSLTPLP
EQEGPTTGTV GTFELMSSKD LAYQMTTYDW ELFNCVLELE LIYHTFGRHN FKKTTANLDL
FLRRFNEIQF WVVTEICLCS QLSKRVQLLK KCIKIAAHCK EYKNLNSFFG IVMGLSNVAE
SRLALTWEKL PSKFKKFYAE FESLMDPSRN HKAYRLTAAK LEPPLIPFMP LLIKDMTFTH
EGNKTFIDNL VNFEKMRMIA NTARTVRYYR SQPFNPDAAQ ANKNHQDVRS YVRQLNVIDN
QRTLSQMSHR LEPRRP
