Q9EQZ6 (RPGF4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rap guanine nucleotide exchange factor 4

Alternative name(s):
Exchange factor directly activated by cAMP 2
Exchange protein directly activated by cAMP 2
Short name=EPAC 2
cAMP-dependent Rap1 guanine-nucleotide exchange factor
cAMP-regulated guanine nucleotide exchange factor II
Short name=cAMP-GEFII

Gene names

Name:	Rapgef4
Synonyms:	Cgef2, Epac2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1011 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.2
Subunit structure	Interacts with RAP1B, RIMS1 and RIMS2. Probably part of a complex with RIMS2 and GTP-activated RAB3A. Ref.2 Ref.7
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein By similarity.
Tissue specificity	Expressed in cerebellum, pituitary, adrenal gland and liver. Ref.2
Domain	The N-terminal nucleotide phosphate binding region cAMP 1 has a much lower affinity for cAMP as compared to cAMP 2 By similarity. The DEP domain is involved in membrane localization independent from regulation by cAMP By similarity.
Sequence similarities	Contains 2 cyclic nucleotide-binding domains. Contains 1 DEP domain. Contains 1 N-terminal Ras-GEF domain. Contains 1 Ras-GEF domain.

Ontologies

Keywords
Biological process	Exocytosis
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative promoter usage Alternative splicing
Domain	Repeat
Ligand	Nucleotide-binding cAMP cAMP-binding
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cAMP-mediated signaling Inferred from direct assay Ref.2. Source: MGI calcium ion-dependent exocytosis Inferred from direct assay Ref.2. Source: MGI insulin secretion Inferred from direct assay. Source: MGI regulation of exocytosis Inferred from direct assay. Source: MGI regulation of protein phosphorylation Inferred from electronic annotation. Source: InterPro regulation of small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cAMP-dependent protein kinase complex Inferred from electronic annotation. Source: InterPro cytosol Inferred from direct assay Ref.2. Source: MGI
Molecular function	Ras GTPase binding Inferred from physical interaction Ref.7. Source: UniProtKB Ras guanyl-nucleotide exchange factor activity Inferred from direct assay Ref.7. Source: UniProtKB cAMP binding Inferred from direct assay Ref.7. Source: UniProtKB cAMP-dependent protein kinase regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HRAS	P01112	3	EBI-772212,EBI-350145	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9EQZ6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Produced by alternative promoter usage.

Isoform 2 (identifier: Q9EQZ6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-315: Missing.

Note: Produced by alternative promoter usage.

Isoform 3 (identifier: Q9EQZ6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     180-197: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1011

1011

Rap guanine nucleotide exchange factor 4

PRO_0000068871

Regions

Domain

216 – 291

76

DEP

Domain

496 – 634

139

N-terminal Ras-GEF

Domain

772 – 1009

238

Ras-GEF

Nucleotide binding

43 – 166

124

cAMP 1

Nucleotide binding

356 – 476

121

cAMP 2

Amino acid modifications

Modified residue

681

1

Phosphotyrosine Ref.5

Natural variations

Alternative sequence

1 – 315

315

Missing in isoform 2.

VSP_007614

Alternative sequence

180 – 197

18

Missing in isoform 3.

VSP_007615

Experimental info

Mutagenesis

467

1

L → A: Less than 10% of the wild-type maximal activity. Ref.7

Mutagenesis

498

1

Y → F: 2-fold reduction in maximal activity. Ref.7

Mutagenesis

569

1

Y → A: 2-fold reduction in maximal activity. Ref.7

Mutagenesis

569

1

Y → F: 2-fold reduction in maximal activity. Ref.7

Sequence conflict

313

1

Q → E in BAB23633. Ref.4

Sequence conflict

452

1

D → E in BAB23633. Ref.4

Secondary structure

1

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1011

Helix Strand Turn

Details...

Helix

14 – 19

6

Helix

28 – 38

11

Turn

42 – 46

5

Helix

49 – 58

10

Beta strand

60 – 64

5

Beta strand

69 – 71

3

Beta strand

79 – 86

8

Beta strand

88 – 92

5

Beta strand

94 – 96

3

Helix

98 – 100

3

Beta strand

102 – 107

6

Helix

115 – 119

5

Beta strand

124 – 139

16

Helix

140 – 150

11

Helix

151 – 153

3

Turn

154 – 157

4

Turn

160 – 162

3

Helix

202 – 217

16

Helix

219 – 221

3

Beta strand

222 – 226

5

Beta strand

231 – 237

7

Helix

238 – 247

10

Beta strand

248 – 250

3

Helix

255 – 267

13

Beta strand

270 – 275

6

Beta strand

282 – 284

3

Beta strand

286 – 289

4

Helix

290 – 292

3

Beta strand

293 – 296

4

Helix

303 – 310

8

Helix

313 – 331

19

Helix

341 – 351

11

Helix

355 – 357

3

Helix

362 – 371

10

Beta strand

373 – 377

5

Beta strand

383 – 385

3

Beta strand

393 – 406

14

Turn

407 – 409

3

Beta strand

410 – 416

7

Helix

423 – 426

4

Beta strand

433 – 449

17

Helix

450 – 459

10

Beta strand

464 – 479

16

Beta strand

498 – 503

6

Helix

505 – 515

11

Helix

520 – 522

3

Helix

523 – 540

18

Helix

543 – 554

12

Helix

563 – 588

26

Turn

590 – 592

3

Helix

596 – 611

16

Turn

612 – 614

3

Turn

618 – 622

5

Helix

625 – 628

4

Beta strand

666 – 673

8

Turn

677 – 679

3

Beta strand

683 – 687

5

Helix

692 – 699

8

Helix

700 – 702

3

Beta strand

712 – 714

3

Beta strand

720 – 722

3

Beta strand

739 – 741

3

Helix

755 – 758

4

Helix

767 – 770

4

Helix

773 – 788

16

Helix

793 – 801

9

Helix

803 – 805

3

Helix

811 – 833

23

Helix

837 – 856

20

Helix

860 – 871

12

Helix

873 – 876

4

Helix

879 – 884

6

Helix

887 – 899

13

Helix

903 – 914

12

Helix

924 – 936

13

Beta strand

940 – 947

8

Helix

948 – 964

17

Beta strand

965 – 967

3

Beta strand

973 – 975

3

Helix

981 – 988

8

Helix

996 – 1006

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 449BC537475B03AA	FASTA	1,011	115,491
	10 20 30 40 50 60 MVAAHAAHSQ SSAEWIACLD KRPLERSSED VDIIFTRLKG VKAFEKFHPN LLRQICLCGY 70 80 90 100 110 120 YENLEKGITL FRQGDIGTNW YAVLAGSLDV KVSETSSHQD AVTICTLGIG TAFGESILDN 130 140 150 160 170 180 TPRHATIVTR ESSELLRIEQ EDFKALWEKY RQYMAGLLAP PYGVMETGSN NDRIPDKENT 190 200 210 220 230 240 PLIEPHVPLR PAHTITKVPS EKILRAGKIL RIAILSRAPH MIRDRKYHLK TYRQCCVGTE 250 260 270 280 290 300 LVDWMIQQTS CVHSRTQAVG MWQVLLEDGV LNHVDQERHF QDKYLFYRFL DDEREDAPLP 310 320 330 340 350 360 TEEEKKECDE ELQDTMLLLS QMGPDAHMRM ILRKPPGQRT VDDLEIIYDE LLHIKALSHL 370 380 390 400 410 420 STTVKRELAG VLIFESHAKG GTVLFNQGEE GTSWYIILKG SVNVVIYGKG VVCTLHEGDD 430 440 450 460 470 480 FGKLALVNDA PRAASIVLRE DNCHFLRVDK EDFNRILRDV EANTVRLKEH DQDVLVLEKV 490 500 510 520 530 540 PAGNRAANQG NSQPQQKYTV MSGTPEKILE HFLETIRLEP SLNEATDSVL NDFVMMHCVF 550 560 570 580 590 600 MPNTQLCPAL VAHYHAQPSQ GTEQERMDYA LNNKRRVIRL VLQWAAMYGD LLQEDDVAMA 610 620 630 640 650 660 FLEEFYVSVS DDARMMAAFK EQLPELEKIV KQISEDAKAP QKKHKVLLQQ FNTGDERAQK 670 680 690 700 710 720 RQPIRGSDEV LFKVYCIDHT YTTIRVPVAA SVKEVISAVA DKLGSGEGLI IVKMNSGGEK 730 740 750 760 770 780 VVLKSNDVSV FTTLTINGRL FACPREQFDS LTPLPEQEGP TTGTVGTFEL MSSKDLAYQM 790 800 810 820 830 840 TTYDWELFNC VHELELIYHT FGRHNFKKTT ANLDLFLRRF NEIQFWVVTE VCLCSQLSKR 850 860 870 880 890 900 VQLLKKFIKI AAHCKEYKNL NSFFAIVMGL SNVAVSRLAL TWEKLPSKFK KFYAEFESLM 910 920 930 940 950 960 DPSRNHRAYR LTAAKLEPPL IPFMPLLIKD MTFTHEGNKT FIDNLVNFEK MRMIANTART 970 980 990 1000 1010 VRYYRSQPFN PDAAQANKNH QDVRSYVRQL NVIDNQRTLS QMSHRLEPRR P
	Isoform 2 [UniParc]. Checksum: 4006240D4B85A747	FASTA	696	79,440
	10 20 30 40 50 60 MLLLSQMGPD AHMRMILRKP PGQRTVDDLE IIYDELLHIK ALSHLSTTVK RELAGVLIFE 70 80 90 100 110 120 SHAKGGTVLF NQGEEGTSWY IILKGSVNVV IYGKGVVCTL HEGDDFGKLA LVNDAPRAAS 130 140 150 160 170 180 IVLREDNCHF LRVDKEDFNR ILRDVEANTV RLKEHDQDVL VLEKVPAGNR AANQGNSQPQ 190 200 210 220 230 240 QKYTVMSGTP EKILEHFLET IRLEPSLNEA TDSVLNDFVM MHCVFMPNTQ LCPALVAHYH 250 260 270 280 290 300 AQPSQGTEQE RMDYALNNKR RVIRLVLQWA AMYGDLLQED DVAMAFLEEF YVSVSDDARM 310 320 330 340 350 360 MAAFKEQLPE LEKIVKQISE DAKAPQKKHK VLLQQFNTGD ERAQKRQPIR GSDEVLFKVY 370 380 390 400 410 420 CIDHTYTTIR VPVAASVKEV ISAVADKLGS GEGLIIVKMN SGGEKVVLKS NDVSVFTTLT 430 440 450 460 470 480 INGRLFACPR EQFDSLTPLP EQEGPTTGTV GTFELMSSKD LAYQMTTYDW ELFNCVHELE 490 500 510 520 530 540 LIYHTFGRHN FKKTTANLDL FLRRFNEIQF WVVTEVCLCS QLSKRVQLLK KFIKIAAHCK 550 560 570 580 590 600 EYKNLNSFFA IVMGLSNVAV SRLALTWEKL PSKFKKFYAE FESLMDPSRN HRAYRLTAAK 610 620 630 640 650 660 LEPPLIPFMP LLIKDMTFTH EGNKTFIDNL VNFEKMRMIA NTARTVRYYR SQPFNPDAAQ 670 680 690 ANKNHQDVRS YVRQLNVIDN QRTLSQMSHR LEPRRP
	Isoform 3 [UniParc]. Checksum: F503405FD9A9C12F	FASTA	993	113,489
	10 20 30 40 50 60 MVAAHAAHSQ SSAEWIACLD KRPLERSSED VDIIFTRLKG VKAFEKFHPN LLRQICLCGY 70 80 90 100 110 120 YENLEKGITL FRQGDIGTNW YAVLAGSLDV KVSETSSHQD AVTICTLGIG TAFGESILDN 130 140 150 160 170 180 TPRHATIVTR ESSELLRIEQ EDFKALWEKY RQYMAGLLAP PYGVMETGSN NDRIPDKENV 190 200 210 220 230 240 PSEKILRAGK ILRIAILSRA PHMIRDRKYH LKTYRQCCVG TELVDWMIQQ TSCVHSRTQA 250 260 270 280 290 300 VGMWQVLLED GVLNHVDQER HFQDKYLFYR FLDDEREDAP LPTEEEKKEC DEELQDTMLL 310 320 330 340 350 360 LSQMGPDAHM RMILRKPPGQ RTVDDLEIIY DELLHIKALS HLSTTVKREL AGVLIFESHA 370 380 390 400 410 420 KGGTVLFNQG EEGTSWYIIL KGSVNVVIYG KGVVCTLHEG DDFGKLALVN DAPRAASIVL 430 440 450 460 470 480 REDNCHFLRV DKEDFNRILR DVEANTVRLK EHDQDVLVLE KVPAGNRAAN QGNSQPQQKY 490 500 510 520 530 540 TVMSGTPEKI LEHFLETIRL EPSLNEATDS VLNDFVMMHC VFMPNTQLCP ALVAHYHAQP 550 560 570 580 590 600 SQGTEQERMD YALNNKRRVI RLVLQWAAMY GDLLQEDDVA MAFLEEFYVS VSDDARMMAA 610 620 630 640 650 660 FKEQLPELEK IVKQISEDAK APQKKHKVLL QQFNTGDERA QKRQPIRGSD EVLFKVYCID 670 680 690 700 710 720 HTYTTIRVPV AASVKEVISA VADKLGSGEG LIIVKMNSGG EKVVLKSNDV SVFTTLTING 730 740 750 760 770 780 RLFACPREQF DSLTPLPEQE GPTTGTVGTF ELMSSKDLAY QMTTYDWELF NCVHELELIY 790 800 810 820 830 840 HTFGRHNFKK TTANLDLFLR RFNEIQFWVV TEVCLCSQLS KRVQLLKKFI KIAAHCKEYK 850 860 870 880 890 900 NLNSFFAIVM GLSNVAVSRL ALTWEKLPSK FKKFYAEFES LMDPSRNHRA YRLTAAKLEP 910 920 930 940 950 960 PLIPFMPLLI KDMTFTHEGN KTFIDNLVNF EKMRMIANTA RTVRYYRSQP FNPDAAQANK 970 980 990 NHQDVRSYVR QLNVIDNQRT LSQMSHRLEP RRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A brain cAMP-dependent Rap1 guanine-nucleotide exchange factor." Gaudriault G.E., Takaya K., Vale W.W. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain.
[2]	"cAMP-GEFII is a direct target of cAMP in regulated exocytosis." Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H., Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S. Nat. Cell Biol. 2:805-811(2000) [PubMed: 11056535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RIMS1 AND RIMS2.
[3]	"Characterization of the gene EPAC2: structure, chromosomal localization, tissue expression, and identification of the liver-specific isoform." Ueno H., Shibasaki T., Iwanaga T., Takahashi K., Yokoyama Y., Liu L.M., Yokoi N., Ozaki N., Matsukura S., Yano H., Seino S. Genomics 78:91-98(2001) [PubMed: 11707077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE. Tissue: Liver.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Liver.
[5]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-681, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Structure and regulation of the cAMP-binding domains of Epac2." Rehmann H., Prakash B., Wolf E., Rueppel A., De Rooij J., Bos J.L., Wittinghofer A. Nat. Struct. Biol. 10:26-32(2003) [PubMed: 12469113] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-463.
[7]	"Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B." Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O., Bos J.L. Nature 455:124-127(2008) [PubMed: 18660803] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 324-1011 IN COMPLEX WITH CAMP ANALOG AND RAP1B, SUBUNIT, MUTAGENESIS OF LEU-467; TYR-498 AND TYR-569.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF115480 mRNA. Translation: AAD09132.1.
AB021132 mRNA. Translation: BAB18976.1.
AB037668 mRNA. Translation: BAB72180.1.
AK004874 mRNA. Translation: BAB23633.1.

IPI

IPI00270362.
IPI00323505.
IPI00623205.

RefSeq

NP_001191094.1. NM_001204165.1.
NP_001191095.1. NM_001204166.1.
NP_062662.1. NM_019688.2.

UniGene

Mm.196153.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O7F	X-ray	2.50	A	1-481	[»]
2BYV	X-ray	2.70	E	1-993	[»]
3CF6	X-ray	2.20	E	324-1011	[»]

ProteinModelPortal

Q9EQZ6.

SMR

Q9EQZ6. Positions 13-1009.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9EQZ6. 2 interactions.

STRING

Q9EQZ6.

PTM databases

PhosphoSite

Q9EQZ6.

Proteomic databases

PRIDE

Q9EQZ6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000090826; ENSMUSP00000088336; ENSMUSG00000049044.
ENSMUST00000102698; ENSMUSP00000099759; ENSMUSG00000049044.

GeneID

56508.

KEGG

mmu:56508.

Organism-specific databases

CTD

11069.

MGI

MGI:1917723. Rapgef4.

Phylogenomic databases

GeneTree

ENSGT00560000077091.

HOVERGEN

HBG056985.

InParanoid

Q9EQZ6.

OMA

TIYDWEL.

OrthoDB

EOG4W0XC9.

Gene expression databases

ArrayExpress

Q9EQZ6.

Bgee

Q9EQZ6.

CleanEx

MM_RAPGEF4.

Genevestigator

Q9EQZ6.

GermOnline

ENSMUSG00000049044. Mus musculus.

Family and domain databases

InterPro

IPR002373. cAMP/cGMP_kin.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR000591. DEP_dom.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR019804. Ras_G-nucl-exch_fac_CS.
IPR008937. Ras_GEF.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
IPR014710. RmlC-like_jellyroll.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.840.10. RasGRF_CDC25. 1 hit.
G3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K04351.

PANTHER

PTHR23113. Ras_GEF. 1 hit.

Pfam

PF00027. cNMP_binding. 2 hits.
PF00610. DEP. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]

PRINTS

PR00103. CAMPKINASE.

SMART

SM00100. cNMP. 2 hits.
SM00049. DEP. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]

SUPFAM

SSF51206. cNMP_binding. 2 hits.
SSF48366. Ras_GEF. 1 hit.

PROSITE

PS00888. CNMP_BINDING_1. False negative.
PS00889. CNMP_BINDING_2. False negative.
PS50042. CNMP_BINDING_3. 2 hits.
PS50186. DEP. 1 hit.
PS00720. RASGEF. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

312814.

SOURCE

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Entry information

Entry name

RPGF4_MOUSE

Accession

Primary (citable) accession number: Q9EQZ6
Secondary accession number(s): Q8VIP9, Q9CW52, Q9Z1P0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	March 1, 2001
Last modified:	November 16, 2011
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program