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Rap guanine nucleotide exchange factor 4 (Exchange factor directly activated by cAMP 2) (Exchange protein directly activated by cAMP 2) (EPAC 2) (cAMP-regulated guanine nucleotide exchange factor II) (cAMP-GEFII)

 RPGF4_HUMAN             Reviewed;        1011 AA.
Q8WZA2; B2R7R3; B7Z283; B7Z3T6; B7Z912; O95636; Q8IXK6; Q8TAA4;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
12-SEP-2018, entry version 149.
RecName: Full=Rap guanine nucleotide exchange factor 4;
AltName: Full=Exchange factor directly activated by cAMP 2;
AltName: Full=Exchange protein directly activated by cAMP 2;
Short=EPAC 2;
AltName: Full=cAMP-regulated guanine nucleotide exchange factor II;
Short=cAMP-GEFII;
Name=RAPGEF4; Synonyms=CGEF2, EPAC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=9856955; DOI=10.1126/science.282.5397.2275;
Kawasaki H., Springett G.M., Mochizuki N., Toki S., Nakaya M.,
Matsuda M., Housman D.E., Graybiel A.M.;
"A family of cAMP-binding proteins that directly activate rap1.";
Science 282:2275-2279(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE
PROMOTER USAGE.
PubMed=11707077; DOI=10.1006/geno.2001.6641;
Ueno H., Shibasaki T., Iwanaga T., Takahashi K., Yokoyama Y.,
Liu L.M., Yokoi N., Ozaki N., Matsukura S., Yano H., Seino S.;
"Characterization of the gene EPAC2: structure, chromosomal
localization, tissue expression, and identification of the liver-
specific isoform.";
Genomics 78:91-98(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
TISSUE=Amygdala, Hippocampus, Thalamus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Hypothalamus, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
PubMed=10777494; DOI=10.1074/jbc.M001113200;
de Rooij J., Rehmann H., van Triest M., Cool R.H., Wittinghofer A.,
Bos J.L.;
"Mechanism of regulation of the Epac family of cAMP-dependent
RapGEFs.";
J. Biol. Chem. 275:20829-20836(2000).
-!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A,
RAP1B and RAP2A small GTPases that is activated by binding cAMP.
Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-
independent exocytosis through interaction with RIMS2 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10777494,
ECO:0000269|PubMed:9856955}.
-!- SUBUNIT: Interacts with RIMS1 and RIMS2. Probably part of a
complex with RIMS2 and GTP-activated RAB3A (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q96MC5:C16orf45; NbExp=3; IntAct=EBI-948476, EBI-718468;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8WZA2-1; Sequence=Displayed;
Note=Produced by alternative promoter usage. Promoter analysis
was carried out in mouse.;
Name=2;
IsoId=Q8WZA2-2; Sequence=VSP_007611;
Note=Produced by alternative promoter usage. Promoter analysis
was carried out in mouse.;
Name=3;
IsoId=Q8WZA2-3; Sequence=VSP_007612, VSP_007613;
Note=Produced by alternative splicing of isoform 1. No
experimental confirmation available.;
Name=4;
IsoId=Q8WZA2-4; Sequence=VSP_054423;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8WZA2-5; Sequence=VSP_054423, VSP_054424;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in brain and adrenal
gland. Isoform 2 is expressed in liver. Isoform 1 is expressed in
liver at very low levels.
-!- DOMAIN: The N-terminal nucleotide phosphate binding region cAMP 1
has a much lower affinity for cAMP as compared to cAMP 2.
-!- DOMAIN: The DEP domain is involved in membrane localization
independent from regulation by cAMP. {ECO:0000250}.
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EMBL; U78516; AAD03422.1; -; mRNA.
EMBL; AB027471; BAB72179.1; -; mRNA.
EMBL; AK294445; BAH11769.1; -; mRNA.
EMBL; AK296340; BAH12322.1; -; mRNA.
EMBL; AK304278; BAH14148.1; -; mRNA.
EMBL; AK313084; BAG35910.1; -; mRNA.
EMBL; AK316072; BAH14443.1; -; mRNA.
EMBL; AC009484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC018712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC019046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC024004; AAH24004.1; -; mRNA.
EMBL; BC040183; AAH40183.1; -; mRNA.
CCDS; CCDS42775.1; -. [Q8WZA2-1]
CCDS; CCDS42776.1; -. [Q8WZA2-3]
CCDS; CCDS63060.1; -. [Q8WZA2-4]
CCDS; CCDS63061.1; -. [Q8WZA2-5]
RefSeq; NP_001093867.1; NM_001100397.1. [Q8WZA2-3]
RefSeq; NP_001269828.1; NM_001282899.1. [Q8WZA2-4]
RefSeq; NP_001269829.1; NM_001282900.1. [Q8WZA2-5]
RefSeq; NP_001269830.1; NM_001282901.1.
RefSeq; NP_008954.2; NM_007023.3. [Q8WZA2-1]
RefSeq; XP_006712268.1; XM_006712205.3. [Q8WZA2-5]
UniGene; Hs.470646; -.
ProteinModelPortal; Q8WZA2; -.
SMR; Q8WZA2; -.
BioGrid; 116253; 11.
IntAct; Q8WZA2; 4.
STRING; 9606.ENSP00000380271; -.
BindingDB; Q8WZA2; -.
ChEMBL; CHEMBL2029198; -.
GuidetoPHARMACOLOGY; 1293; -.
iPTMnet; Q8WZA2; -.
PhosphoSitePlus; Q8WZA2; -.
BioMuta; RAPGEF4; -.
DMDM; 32171491; -.
PaxDb; Q8WZA2; -.
PeptideAtlas; Q8WZA2; -.
PRIDE; Q8WZA2; -.
ProteomicsDB; 75243; -.
ProteomicsDB; 75244; -. [Q8WZA2-2]
ProteomicsDB; 75245; -. [Q8WZA2-3]
DNASU; 11069; -.
Ensembl; ENST00000397081; ENSP00000380271; ENSG00000091428. [Q8WZA2-1]
Ensembl; ENST00000397087; ENSP00000380276; ENSG00000091428. [Q8WZA2-3]
Ensembl; ENST00000538974; ENSP00000440135; ENSG00000091428. [Q8WZA2-5]
Ensembl; ENST00000540783; ENSP00000440250; ENSG00000091428. [Q8WZA2-4]
GeneID; 11069; -.
KEGG; hsa:11069; -.
UCSC; uc002uhv.5; human. [Q8WZA2-1]
CTD; 11069; -.
DisGeNET; 11069; -.
EuPathDB; HostDB:ENSG00000091428.17; -.
GeneCards; RAPGEF4; -.
HGNC; HGNC:16626; RAPGEF4.
HPA; CAB004388; -.
HPA; HPA028968; -.
MIM; 606058; gene.
neXtProt; NX_Q8WZA2; -.
OpenTargets; ENSG00000091428; -.
PharmGKB; PA134861108; -.
eggNOG; KOG2378; Eukaryota.
eggNOG; ENOG410XPX9; LUCA.
GeneTree; ENSGT00880000137870; -.
HOGENOM; HOG000230545; -.
HOVERGEN; HBG056985; -.
InParanoid; Q8WZA2; -.
KO; K04351; -.
OMA; CKEYKNL; -.
OrthoDB; EOG091G0HKG; -.
PhylomeDB; Q8WZA2; -.
TreeFam; TF313184; -.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-392517; Rap1 signalling.
Reactome; R-HSA-422356; Regulation of insulin secretion.
ChiTaRS; RAPGEF4; human.
GeneWiki; RAPGEF4; -.
GenomeRNAi; 11069; -.
PRO; PR:Q8WZA2; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000091428; Expressed in 199 organ(s), highest expression level in right frontal lobe.
CleanEx; HS_RAPGEF4; -.
ExpressionAtlas; Q8WZA2; baseline and differential.
Genevisible; Q8WZA2; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
GO; GO:0017016; F:Ras GTPase binding; ISS:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0017156; P:calcium ion regulated exocytosis; IEA:Ensembl.
GO; GO:0019933; P:cAMP-mediated signaling; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0017157; P:regulation of exocytosis; IEA:Ensembl.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
CDD; cd00038; CAP_ED; 2.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 1.10.840.10; -; 1.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR000591; DEP_dom.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF00610; DEP; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
SMART; SM00100; cNMP; 2.
SMART; SM00049; DEP; 1.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF48366; SSF48366; 2.
SUPFAM; SSF51206; SSF51206; 2.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50042; CNMP_BINDING_3; 2.
PROSITE; PS50186; DEP; 1.
PROSITE; PS00720; RASGEF; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
Alternative promoter usage; Alternative splicing; cAMP; cAMP-binding;
Complete proteome; Cytoplasm; Exocytosis;
Guanine-nucleotide releasing factor; Membrane; Nucleotide-binding;
Reference proteome; Repeat.
CHAIN 1 1011 Rap guanine nucleotide exchange factor 4.
/FTId=PRO_0000068870.
DOMAIN 216 291 DEP. {ECO:0000255|PROSITE-
ProRule:PRU00066}.
DOMAIN 496 634 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 772 1009 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
NP_BIND 43 166 cAMP 1.
NP_BIND 356 476 cAMP 2.
VAR_SEQ 1 315 Missing (in isoform 2).
{ECO:0000303|PubMed:11707077}.
/FTId=VSP_007611.
VAR_SEQ 1 153 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054423.
VAR_SEQ 1 144 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007612.
VAR_SEQ 145 148 ALWE -> MLYK (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007613.
VAR_SEQ 180 197 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054424.
CONFLICT 324 324 P -> R (in Ref. 5; AAH40183).
{ECO:0000305}.
CONFLICT 511 511 H -> R (in Ref. 5; AAH40183).
{ECO:0000305}.
CONFLICT 647 647 L -> I (in Ref. 5; AAH40183).
{ECO:0000305}.
CONFLICT 679 679 H -> P (in Ref. 5; AAH24004).
{ECO:0000305}.
CONFLICT 732 732 T -> M (in Ref. 5; AAH24004).
{ECO:0000305}.
CONFLICT 873 873 V -> I (in Ref. 1; AAD03422).
{ECO:0000305}.
CONFLICT 902 902 P -> T (in Ref. 5; AAH40183).
{ECO:0000305}.
SEQUENCE 1011 AA; 115522 MW; 9427C5F92F2FFAD1 CRC64;
MVAAHAAHSS SSAEWIACLD KRPLERSSED VDIIFTRLKE VKAFEKFHPN LLHQICLCGY
YENLEKGITL FRQGDIGTNW YAVLAGSLDV KVSETSSHQD AVTICTLGIG TAFGESILDN
TPRHATIVTR ESSELLRIEQ KDFKALWEKY RQYMAGLLAP PYGVMETGSN NDRIPDKENT
PLIEPHVPLR PANTITKVPS EKILRAGKIL RNAILSRAPH MIRDRKYHLK TYRQCCVGTE
LVDWMMQQTP CVHSRTQAVG MWQVLLEDGV LNHVDQEHHF QDKYLFYRFL DDEHEDAPLP
TEEEKKECDE ELQDTMLLLS QMGPDAHMRM ILRKPPGQRT VDDLEIIYEE LLHIKALSHL
STTVKRELAG VLIFESHAKG GTVLFNQGEE GTSWYIILKG SVNVVIYGKG VVCTLHEGDD
FGKLALVNDA PRAASIVLRE DNCHFLRVDK EDFNRILRDV EANTVRLKEH DQDVLVLEKV
PAGNRASNQG NSQPQQKYTV MSGTPEKILE HFLETIRLEA TLNEATDSVL NDFIMMHCVF
MPNTQLCPAL VAHYHAQPSQ GTEQEKMDYA LNNKRRVIRL VLQWAAMYGD LLQEDDVSMA
FLEEFYVSVS DDARMIAALK EQLPELEKIV KQISEDAKAP QKKHKVLLQQ FNTGDERAQK
RQPIRGSDEV LFKVYCMDHT YTTIRVPVAT SVKEVISAVA DKLGSGEGLI IVKMSSGGEK
VVLKPNDVSV FTTLTINGRL FACPREQFDS LTPLPEQEGP TVGTVGTFEL MSSKDLAYQM
TIYDWELFNC VHELELIYHT FGRHNFKKTT ANLDLFLRRF NEIQFWVVTE ICLCSQLSKR
VQLLKKFIKI AAHCKEYKNL NSFFAIVMGL SNVAVSRLAL TWEKLPSKFK KFYAEFESLM
DPSRNHRAYR LTVAKLEPPL IPFMPLLIKD MTFTHEGNKT FIDNLVNFEK MRMIANTART
VRYYRSQPFN PDAAQANKNH QDVRSYVRQL NVIDNQRTLS QMSHRLEPRR P


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Epac-112AP Polyclonal Antibody Exchange protein 1 directly activated by cAMP (C-epitope) Immunogen: peptide Host: Rabbit 200ul
Epac-101AP Polyclonal Antibody Exchange protein 1 directly activated by cAMP (N-epitope) Immunogen: peptide Host: Rabbit 200ul
Epac-101AP Exchange protein 1 directly activated by cAMP (N-epitope) Antigenic peptide: P-Epac100 Host: Rabbit Affinity purifed 100ul


 

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