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Rap guanine nucleotide exchange factor 3 (Exchange factor directly activated by cAMP 1) (Exchange protein directly activated by cAMP 1) (EPAC 1) (Rap1 guanine-nucleotide-exchange factor directly activated by cAMP) (cAMP-regulated guanine nucleotide exchange factor I) (cAMP-GEFI)

 RPGF3_HUMAN             Reviewed;         923 AA.
O95398; A8K2G5; E7EQC8; O95634; Q8WVN0;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 6.
12-SEP-2018, entry version 168.
RecName: Full=Rap guanine nucleotide exchange factor 3;
AltName: Full=Exchange factor directly activated by cAMP 1;
AltName: Full=Exchange protein directly activated by cAMP 1;
Short=EPAC 1;
AltName: Full=Rap1 guanine-nucleotide-exchange factor directly activated by cAMP;
AltName: Full=cAMP-regulated guanine nucleotide exchange factor I;
Short=cAMP-GEFI;
Name=RAPGEF3; Synonyms=CGEF1, EPAC, EPAC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
MUTAGENESIS OF ARG-321, AND VARIANT GLY-193.
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 [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
GLY-193.
TISSUE=Thalamus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-193.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
PRO-16 AND GLY-193.
TISSUE=Kidney;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 43-923 (ISOFORM 1), FUNCTION, AND
VARIANT GLY-193.
TISSUE=Muscle;
PubMed=9853756; DOI=10.1038/24884;
de Rooij J., Zwartkruis F.J.T., Verheijen M.H., Cool R.H.,
Nijman S.M., Wittinghofer A., Bos J.L.;
"Epac is a Rap1 guanine-nucleotide-exchange factor directly activated
by cyclic AMP.";
Nature 396:474-477(1998).
[7]
FUNCTION, DOMAIN DEP, AND SUBCELLULAR LOCATION.
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).
[8]
MUTAGENESIS OF LEU-315 AND PHE-342.
PubMed=12469113; DOI=10.1038/nsb878;
Rehmann H., Prakash B., Wolf E., Rueppel A., De Rooij J., Bos J.L.,
Wittinghofer A.;
"Structure and regulation of the cAMP-binding domains of Epac2.";
Nat. Struct. Biol. 10:26-32(2003).
[9]
FUNCTION.
PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S.,
Linnemann J.R., Spanjaard E., Brouwer P.M., van der Meer A.J.,
Zwartkruis F.J., Rehmann H., de Rooij J., Bos J.L.;
"Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
control.";
Cell. Signal. 23:2056-2064(2011).
[10]
INTERACTION WITH PDE3B, AND MUTAGENESIS OF ASP-412; GLU-415; PHE-417;
ASP-420 AND PHE-421.
PubMed=21393242; DOI=10.1074/jbc.M110.217026;
Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A.,
Zaccolo M., Houslay M.D., Maurice D.H.;
"A phosphodiesterase 3B-based signaling complex integrates exchange
protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals
in human arterial endothelial cells.";
J. Biol. Chem. 286:16285-16296(2011).
-!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A and
RAP2A small GTPases that is activated by binding cAMP. Through
simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled
in a signaling complex in which it activates the PI3K gamma
complex and which is involved in angiogenesis. Plays a role in the
modulation of the cAMP-induced dynamic control of endothelial
barrier function through a pathway that is independent on Rho-
mediated signaling. Required for the actin rearrangement at cell-
cell junctions, such as stress fibers and junctional actin.
{ECO:0000269|PubMed:10777494, ECO:0000269|PubMed:21840392,
ECO:0000269|PubMed:9853756}.
-!- SUBUNIT: Interacts with PDE3B. {ECO:0000269|PubMed:21393242}.
-!- INTERACTION:
Q13370:PDE3B; NbExp=8; IntAct=EBI-6172806, EBI-6172856;
-!- SUBCELLULAR LOCATION: Endomembrane system
{ECO:0000269|PubMed:10777494}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95398-1; Sequence=Displayed;
Name=2;
IsoId=O95398-2; Sequence=VSP_007608, VSP_007609;
Name=3;
IsoId=O95398-3; Sequence=VSP_047007;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in adult
kidney, heart, thyroid and brain, and fetal kidney.
{ECO:0000269|PubMed:9856955}.
-!- DOMAIN: The DEP domain is involved in membrane localization
independent from regulation by cAMP.
{ECO:0000269|PubMed:10777494}.
-!- CAUTION: It is uncertain whether Met-1 or Met-43 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD02890.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD12740.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U78168; AAD12740.1; ALT_INIT; mRNA.
EMBL; U78169; AAD02890.1; ALT_INIT; mRNA.
EMBL; AK290230; BAF82919.1; -; mRNA.
EMBL; AC004241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW57944.1; -; Genomic_DNA.
EMBL; BC017728; AAH17728.2; -; mRNA.
EMBL; AF103905; AAC83381.1; -; mRNA.
CCDS; CCDS31784.1; -. [O95398-3]
CCDS; CCDS41775.1; -. [O95398-1]
RefSeq; NP_001092002.1; NM_001098532.2.
RefSeq; NP_006096.2; NM_006105.5.
UniGene; Hs.8578; -.
ProteinModelPortal; O95398; -.
SMR; O95398; -.
BioGrid; 115682; 9.
IntAct; O95398; 4.
MINT; O95398; -.
STRING; 9606.ENSP00000373864; -.
BindingDB; O95398; -.
ChEMBL; CHEMBL2029197; -.
GuidetoPHARMACOLOGY; 1292; -.
iPTMnet; O95398; -.
PhosphoSitePlus; O95398; -.
BioMuta; RAPGEF3; -.
MaxQB; O95398; -.
PaxDb; O95398; -.
PeptideAtlas; O95398; -.
PRIDE; O95398; -.
ProteomicsDB; 50849; -.
ProteomicsDB; 50850; -. [O95398-2]
Ensembl; ENST00000389212; ENSP00000373864; ENSG00000079337. [O95398-1]
Ensembl; ENST00000395358; ENSP00000378764; ENSG00000079337. [O95398-2]
Ensembl; ENST00000405493; ENSP00000384521; ENSG00000079337. [O95398-3]
Ensembl; ENST00000449771; ENSP00000395708; ENSG00000079337. [O95398-1]
Ensembl; ENST00000549151; ENSP00000448619; ENSG00000079337. [O95398-3]
GeneID; 10411; -.
KEGG; hsa:10411; -.
UCSC; uc001rpz.5; human. [O95398-1]
CTD; 10411; -.
DisGeNET; 10411; -.
EuPathDB; HostDB:ENSG00000079337.15; -.
GeneCards; RAPGEF3; -.
HGNC; HGNC:16629; RAPGEF3.
HPA; CAB004386; -.
HPA; HPA040365; -.
HPA; HPA043518; -.
MIM; 606057; gene.
neXtProt; NX_O95398; -.
OpenTargets; ENSG00000079337; -.
PharmGKB; PA134910959; -.
eggNOG; KOG2378; Eukaryota.
eggNOG; ENOG410XPX9; LUCA.
GeneTree; ENSGT00880000137870; -.
HOGENOM; HOG000230545; -.
InParanoid; O95398; -.
KO; K08014; -.
OMA; WVATELC; -.
OrthoDB; EOG091G0HKG; -.
PhylomeDB; O95398; -.
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; RAPGEF3; human.
GeneWiki; RAPGEF3; -.
GenomeRNAi; 10411; -.
PRO; PR:O95398; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000079337; Expressed in 214 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_RAPGEF3; -.
ExpressionAtlas; O95398; baseline and differential.
Genevisible; O95398; HS.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0017034; F:Rap guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0019933; P:cAMP-mediated signaling; NAS:BHF-UCL.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0034242; P:negative regulation of syncytium formation by plasma membrane fusion; IMP:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:1901985; P:positive regulation of protein acetylation; IMP:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:0060143; P:positive regulation of syncytium formation by plasma membrane fusion; IMP:UniProtKB.
GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00038; CAP_ED; 1.
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; -; 1.
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; 1.
Pfam; PF00610; DEP; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
SMART; SM00100; cNMP; 1.
SMART; SM00049; DEP; 1.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF48366; SSF48366; 3.
SUPFAM; SSF51206; SSF51206; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS50186; DEP; 1.
PROSITE; PS00720; RASGEF; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; cAMP; cAMP-binding;
Complete proteome; Guanine-nucleotide releasing factor; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 923 Rap guanine nucleotide exchange factor 3.
/FTId=PRO_0000068867.
DOMAIN 110 186 DEP. {ECO:0000255|PROSITE-
ProRule:PRU00066}.
DOMAIN 384 518 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 662 889 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
NP_BIND 245 363 cAMP.
REGION 218 242 Interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
REGION 398 422 Interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VCC8}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VCC8}.
MOD_RES 864 864 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VCC8}.
VAR_SEQ 1 42 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047007.
VAR_SEQ 533 598 ARNLPVWLPNQDEPLPGSSCAIQVGDKVPYDICRPDHSVLT
LQLPVTASVREVMAALAQEDGWTKG -> VSAWPQFLSSAP
PGLQAPPSPPDPEGLCGRGKLSSHRHTLGSLIGVHGALAAC
GALGQAVPGGAEA (in isoform 2).
{ECO:0000303|PubMed:9856955}.
/FTId=VSP_007608.
VAR_SEQ 599 923 Missing (in isoform 2).
{ECO:0000303|PubMed:9856955}.
/FTId=VSP_007609.
VARIANT 16 16 A -> P (in dbSNP:rs11168230).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_047924.
VARIANT 193 193 R -> G (in dbSNP:rs2016123).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9853756,
ECO:0000269|PubMed:9856955,
ECO:0000269|Ref.4}.
/FTId=VAR_047925.
VARIANT 374 374 G -> S (in dbSNP:rs12422983).
/FTId=VAR_047926.
VARIANT 517 517 C -> Y (in dbSNP:rs61709815).
/FTId=VAR_061784.
MUTAGEN 315 315 L->W: Abolishes activation of RAP1A.
{ECO:0000269|PubMed:12469113}.
MUTAGEN 321 321 R->K: Reduces activation of RAP1A.
{ECO:0000269|PubMed:9856955}.
MUTAGEN 342 342 F->A,T: Diminishes GEF activity
dependence on cAMP concentration.
{ECO:0000269|PubMed:12469113}.
MUTAGEN 412 412 D->A: Abolishes interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 415 415 E->A: Abolishes interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 417 417 F->A: Abolishes interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 420 420 D->A: Abolishes interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
MUTAGEN 421 421 F->A: Abolishes interaction with PDE3B.
{ECO:0000269|PubMed:21393242}.
CONFLICT 64 64 R -> H (in Ref. 1; AAD12740/AAD02890).
{ECO:0000305}.
CONFLICT 106 106 R -> Q (in Ref. 1; AAD12740/AAD02890).
{ECO:0000305}.
CONFLICT 116 116 I -> T (in Ref. 6; AAC83381).
{ECO:0000305}.
CONFLICT 330 330 D -> Y (in Ref. 1; AAD12740/AAD02890).
{ECO:0000305}.
CONFLICT 394 394 E -> D (in Ref. 1; AAD12740/AAD02890).
{ECO:0000305}.
CONFLICT 406 406 P -> L (in Ref. 1; AAD12740/AAD02890).
{ECO:0000305}.
CONFLICT 414 414 T -> K (in Ref. 1; AAD12740/AAD02890).
{ECO:0000305}.
CONFLICT 491 491 Q -> H (in Ref. 1; AAD12740).
{ECO:0000305}.
CONFLICT 638 638 V -> A (in Ref. 6; AAC83381).
{ECO:0000305}.
CONFLICT 736 736 R -> K (in Ref. 1; AAD12740).
{ECO:0000305}.
CONFLICT 751 751 L -> V (in Ref. 1; AAD12740).
{ECO:0000305}.
CONFLICT 765 765 A -> P (in Ref. 1; AAD12740).
{ECO:0000305}.
SEQUENCE 923 AA; 103751 MW; 8B3A24341F20515F CRC64;
MKVGWPGESC WQVGLAVEDS PALGAPRVGA LPDVVPEGTL LNMVLRRMHR PRSCSYQLLL
EHQRPSCIQG LRWTPLTNSE ESLDFSESLE QASTERVLRA GRQLHRHLLA TCPNLIRDRK
YHLRLYRQCC SGRELVDGIL ALGLGVHSRS QVVGICQVLL DEGALCHVKH DWAFQDRDAQ
FYRFPGPEPE PVRTHEMEEE LAEAVALLSQ RGPDALLTVA LRKPPGQRTD EELDLIFEEL
LHIKAVAHLS NSVKRELAAV LLFEPHSKAG TVLFSQGDKG TSWYIIWKGS VNVVTHGKGL
VTTLHEGDDF GQLALVNDAP RAATIILRED NCHFLRVDKQ DFNRIIKDVE AKTMRLEEHG
KVVLVLERAS QGAGPSRPPT PGRNRYTVMS GTPEKILELL LEAMGPDSSA HDPTETFLSD
FLLTHRVFMP SAQLCAALLH HFHVEPAGGS EQERSTYVCN KRQQILRLVS QWVALYGSML
HTDPVATSFL QKLSDLVGRD TRLSNLLREQ WPERRRCHRL ENGCGNASPQ MKARNLPVWL
PNQDEPLPGS SCAIQVGDKV PYDICRPDHS VLTLQLPVTA SVREVMAALA QEDGWTKGQV
LVKVNSAGDA IGLQPDARGV ATSLGLNERL FVVNPQEVHE LIPHPDQLGP TVGSAEGLDL
VSAKDLAGQL TDHDWSLFNS IHQVELIHYV LGPQHLRDVT TANLERFMRR FNELQYWVAT
ELCLCPVPGP RAQLLRKFIK LAAHLKEQKN LNSFFAVMFG LSNSAISRLA HTWERLPHKV
RKLYSALERL LDPSWNHRVY RLALAKLSPP VIPFMPLLLK DMTFIHEGNH TLVENLINFE
KMRMMARAAR MLHHCRSHNP VPLSPLRSRV SHLHEDSQVA RISTCSEQSL STRSPASTWA
YVQQLKVIDN QRELSRLSRE LEP


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