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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-dependent Rap1 guanine-nucleotide exchange factor) (cAMP-regulated guanine nucleotide exchange factor II) (cAMP-GEFII)

 RPGF4_MOUSE             Reviewed;        1011 AA.
Q9EQZ6; Q8VIP9; Q9CW52; Q9Z1P0;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 159.
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-dependent Rap1 guanine-nucleotide exchange factor;
AltName: Full=cAMP-regulated guanine nucleotide exchange factor II;
Short=cAMP-GEFII;
Name=Rapgef4; Synonyms=Cgef2, Epac2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
Gaudriault G.E., Takaya K., Vale W.W.;
"A brain cAMP-dependent Rap1 guanine-nucleotide exchange factor.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH RIMS1 AND RIMS2.
PubMed=11056535; DOI=10.1038/35041046;
Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H.,
Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S.;
"cAMP-GEFII is a direct target of cAMP in regulated exocytosis.";
Nat. Cell Biol. 2:805-811(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE PROMOTER
USAGE.
TISSUE=Liver;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-463.
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).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 324-1011 IN COMPLEX WITH CAMP
ANALOG AND RAP1B, SUBUNIT, AND MUTAGENESIS OF LEU-467; TYR-498 AND
TYR-569.
PubMed=18660803; DOI=10.1038/nature07187;
Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O.,
Bos J.L.;
"Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.";
Nature 455:124-127(2008).
-!- 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.
{ECO:0000269|PubMed:11056535}.
-!- SUBUNIT: Interacts with RAP1B, RIMS1 and RIMS2. Probably part of a
complex with RIMS2 and GTP-activated RAB3A.
{ECO:0000269|PubMed:11056535, ECO:0000269|PubMed:18660803}.
-!- INTERACTION:
P01112:HRAS (xeno); NbExp=3; IntAct=EBI-772212, EBI-350145;
P61224:RAP1B (xeno); NbExp=3; IntAct=EBI-15566495, EBI-358143;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9EQZ6-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2;
IsoId=Q9EQZ6-2; Sequence=VSP_007614;
Note=Produced by alternative promoter usage.;
Name=3;
IsoId=Q9EQZ6-3; Sequence=VSP_007615;
Note=Produced by alternative splicing of isoform 1. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in cerebellum, pituitary, adrenal
gland and liver. {ECO:0000269|PubMed:11056535}.
-!- DOMAIN: The N-terminal nucleotide phosphate binding region cAMP 1
has a much lower affinity for cAMP as compared to cAMP 2.
{ECO:0000250}.
-!- DOMAIN: The DEP domain is involved in membrane localization
independent from regulation by cAMP. {ECO:0000250}.
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EMBL; AF115480; AAD09132.1; -; mRNA.
EMBL; AB021132; BAB18976.1; -; mRNA.
EMBL; AB037668; BAB72180.1; -; mRNA.
EMBL; AK004874; BAB23633.1; -; mRNA.
CCDS; CCDS16120.1; -. [Q9EQZ6-3]
CCDS; CCDS57176.1; -. [Q9EQZ6-1]
RefSeq; NP_001191094.1; NM_001204165.1. [Q9EQZ6-1]
RefSeq; NP_001191095.1; NM_001204166.1.
RefSeq; NP_062662.1; NM_019688.2. [Q9EQZ6-3]
UniGene; Mm.196153; -.
PDB; 1O7F; X-ray; 2.50 A; A=1-481.
PDB; 2BYV; X-ray; 2.70 A; E=1-1011.
PDB; 3CF6; X-ray; 2.20 A; E=324-1011.
PDB; 4F7Z; X-ray; 2.60 A; A=1-1011.
PDB; 4MGI; X-ray; 2.80 A; E=324-1011.
PDB; 4MGK; X-ray; 2.70 A; E=324-1011.
PDB; 4MGY; X-ray; 2.60 A; E=324-1011.
PDB; 4MGZ; X-ray; 3.00 A; E=324-1011.
PDB; 4MH0; X-ray; 2.40 A; E=324-1011.
PDBsum; 1O7F; -.
PDBsum; 2BYV; -.
PDBsum; 3CF6; -.
PDBsum; 4F7Z; -.
PDBsum; 4MGI; -.
PDBsum; 4MGK; -.
PDBsum; 4MGY; -.
PDBsum; 4MGZ; -.
PDBsum; 4MH0; -.
ProteinModelPortal; Q9EQZ6; -.
SMR; Q9EQZ6; -.
BioGrid; 208026; 8.
CORUM; Q9EQZ6; -.
DIP; DIP-32333N; -.
IntAct; Q9EQZ6; 8.
STRING; 10090.ENSMUSP00000088336; -.
BindingDB; Q9EQZ6; -.
ChEMBL; CHEMBL3593151; -.
iPTMnet; Q9EQZ6; -.
PhosphoSitePlus; Q9EQZ6; -.
PaxDb; Q9EQZ6; -.
PeptideAtlas; Q9EQZ6; -.
PRIDE; Q9EQZ6; -.
Ensembl; ENSMUST00000090826; ENSMUSP00000088336; ENSMUSG00000049044. [Q9EQZ6-1]
Ensembl; ENSMUST00000102698; ENSMUSP00000099759; ENSMUSG00000049044. [Q9EQZ6-3]
GeneID; 56508; -.
KEGG; mmu:56508; -.
UCSC; uc008kbn.2; mouse. [Q9EQZ6-1]
UCSC; uc008kbo.2; mouse. [Q9EQZ6-3]
CTD; 11069; -.
MGI; MGI:1917723; Rapgef4.
eggNOG; KOG2378; Eukaryota.
eggNOG; ENOG410XPX9; LUCA.
GeneTree; ENSGT00880000137870; -.
HOGENOM; HOG000230545; -.
HOVERGEN; HBG056985; -.
InParanoid; Q9EQZ6; -.
KO; K04351; -.
OMA; CKEYKNL; -.
OrthoDB; EOG091G0HKG; -.
TreeFam; TF313184; -.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-MMU-392517; Rap1 signalling.
Reactome; R-MMU-422356; Regulation of insulin secretion.
EvolutionaryTrace; Q9EQZ6; -.
PRO; PR:Q9EQZ6; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000049044; -.
CleanEx; MM_RAPGEF4; -.
ExpressionAtlas; Q9EQZ6; baseline and differential.
Genevisible; Q9EQZ6; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005903; C:brush border; ISO:MGI.
GO; GO:0005929; C:cilium; ISO:MGI.
GO; GO:0044316; C:cone cell pedicle; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0060076; C:excitatory synapse; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0017016; F:Ras GTPase binding; IPI:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0017156; P:calcium ion regulated exocytosis; IDA:MGI.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI.
GO; GO:0030073; P:insulin secretion; IDA:MGI.
GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI.
GO; GO:1904457; P:positive regulation of neuronal action potential; ISO:MGI.
GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0050773; P:regulation of dendrite development; ISO:MGI.
GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
GO; GO:0007165; P:signal transduction; ISO:MGI.
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;
3D-structure; 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_0000068871.
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,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_007614.
VAR_SEQ 180 197 Missing (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_007615.
MUTAGEN 467 467 L->A: Less than 10% of the wild-type
maximal activity.
{ECO:0000269|PubMed:18660803}.
MUTAGEN 498 498 Y->F: 2-fold reduction in maximal
activity. {ECO:0000269|PubMed:18660803}.
MUTAGEN 569 569 Y->A: 2-fold reduction in maximal
activity. {ECO:0000269|PubMed:18660803}.
MUTAGEN 569 569 Y->F: 2-fold reduction in maximal
activity. {ECO:0000269|PubMed:18660803}.
CONFLICT 313 313 Q -> E (in Ref. 4; BAB23633).
{ECO:0000305}.
CONFLICT 452 452 D -> E (in Ref. 4; BAB23633).
{ECO:0000305}.
HELIX 14 19 {ECO:0000244|PDB:1O7F}.
STRAND 23 25 {ECO:0000244|PDB:4F7Z}.
HELIX 28 38 {ECO:0000244|PDB:1O7F}.
TURN 42 46 {ECO:0000244|PDB:1O7F}.
HELIX 49 58 {ECO:0000244|PDB:1O7F}.
STRAND 60 64 {ECO:0000244|PDB:1O7F}.
STRAND 69 71 {ECO:0000244|PDB:1O7F}.
STRAND 79 86 {ECO:0000244|PDB:1O7F}.
STRAND 88 92 {ECO:0000244|PDB:1O7F}.
STRAND 94 96 {ECO:0000244|PDB:1O7F}.
HELIX 98 100 {ECO:0000244|PDB:1O7F}.
STRAND 102 107 {ECO:0000244|PDB:1O7F}.
HELIX 115 119 {ECO:0000244|PDB:1O7F}.
STRAND 124 139 {ECO:0000244|PDB:1O7F}.
HELIX 140 150 {ECO:0000244|PDB:1O7F}.
HELIX 151 153 {ECO:0000244|PDB:1O7F}.
TURN 154 157 {ECO:0000244|PDB:1O7F}.
TURN 160 162 {ECO:0000244|PDB:1O7F}.
HELIX 202 217 {ECO:0000244|PDB:1O7F}.
HELIX 219 221 {ECO:0000244|PDB:1O7F}.
STRAND 222 226 {ECO:0000244|PDB:1O7F}.
STRAND 231 237 {ECO:0000244|PDB:1O7F}.
HELIX 238 247 {ECO:0000244|PDB:1O7F}.
STRAND 248 250 {ECO:0000244|PDB:1O7F}.
HELIX 255 267 {ECO:0000244|PDB:1O7F}.
STRAND 270 275 {ECO:0000244|PDB:1O7F}.
STRAND 282 284 {ECO:0000244|PDB:1O7F}.
STRAND 286 289 {ECO:0000244|PDB:1O7F}.
HELIX 290 292 {ECO:0000244|PDB:1O7F}.
STRAND 293 296 {ECO:0000244|PDB:1O7F}.
HELIX 303 310 {ECO:0000244|PDB:1O7F}.
HELIX 329 333 {ECO:0000244|PDB:4MH0}.
HELIX 336 338 {ECO:0000244|PDB:4MH0}.
HELIX 341 351 {ECO:0000244|PDB:4MH0}.
HELIX 355 357 {ECO:0000244|PDB:1O7F}.
HELIX 362 368 {ECO:0000244|PDB:4MH0}.
TURN 369 371 {ECO:0000244|PDB:4MH0}.
STRAND 373 377 {ECO:0000244|PDB:4MH0}.
STRAND 383 385 {ECO:0000244|PDB:4MH0}.
STRAND 393 400 {ECO:0000244|PDB:4MH0}.
STRAND 402 406 {ECO:0000244|PDB:4MH0}.
TURN 407 409 {ECO:0000244|PDB:4MH0}.
STRAND 410 415 {ECO:0000244|PDB:4MH0}.
HELIX 423 428 {ECO:0000244|PDB:4MH0}.
STRAND 433 438 {ECO:0000244|PDB:4MH0}.
STRAND 440 449 {ECO:0000244|PDB:4MH0}.
HELIX 450 456 {ECO:0000244|PDB:4MH0}.
TURN 457 460 {ECO:0000244|PDB:4MH0}.
STRAND 465 469 {ECO:0000244|PDB:4MH0}.
STRAND 472 479 {ECO:0000244|PDB:4MH0}.
STRAND 498 503 {ECO:0000244|PDB:4MH0}.
HELIX 505 514 {ECO:0000244|PDB:4MH0}.
HELIX 520 522 {ECO:0000244|PDB:4MH0}.
HELIX 523 540 {ECO:0000244|PDB:4MH0}.
HELIX 543 554 {ECO:0000244|PDB:4MH0}.
STRAND 559 561 {ECO:0000244|PDB:4MH0}.
HELIX 563 588 {ECO:0000244|PDB:4MH0}.
HELIX 589 594 {ECO:0000244|PDB:4MH0}.
HELIX 596 616 {ECO:0000244|PDB:4MH0}.
HELIX 617 620 {ECO:0000244|PDB:4F7Z}.
HELIX 622 629 {ECO:0000244|PDB:4MH0}.
STRAND 668 675 {ECO:0000244|PDB:4MH0}.
TURN 677 679 {ECO:0000244|PDB:2BYV}.
STRAND 681 687 {ECO:0000244|PDB:4MH0}.
HELIX 692 703 {ECO:0000244|PDB:4MH0}.
STRAND 710 714 {ECO:0000244|PDB:4MH0}.
STRAND 720 722 {ECO:0000244|PDB:4MH0}.
HELIX 731 733 {ECO:0000244|PDB:4MGY}.
STRAND 739 743 {ECO:0000244|PDB:4MH0}.
HELIX 745 750 {ECO:0000244|PDB:4MH0}.
HELIX 755 757 {ECO:0000244|PDB:4MH0}.
HELIX 765 768 {ECO:0000244|PDB:4MH0}.
HELIX 773 789 {ECO:0000244|PDB:4MH0}.
HELIX 793 801 {ECO:0000244|PDB:4MH0}.
HELIX 803 805 {ECO:0000244|PDB:4MH0}.
HELIX 811 832 {ECO:0000244|PDB:4MH0}.
HELIX 837 856 {ECO:0000244|PDB:4MH0}.
HELIX 860 871 {ECO:0000244|PDB:4MH0}.
HELIX 873 876 {ECO:0000244|PDB:4MH0}.
HELIX 879 884 {ECO:0000244|PDB:4MH0}.
HELIX 887 898 {ECO:0000244|PDB:4MH0}.
HELIX 903 915 {ECO:0000244|PDB:4MH0}.
HELIX 924 937 {ECO:0000244|PDB:4MH0}.
STRAND 940 942 {ECO:0000244|PDB:4MH0}.
STRAND 945 947 {ECO:0000244|PDB:4MH0}.
HELIX 948 964 {ECO:0000244|PDB:4MH0}.
STRAND 965 967 {ECO:0000244|PDB:2BYV}.
STRAND 973 975 {ECO:0000244|PDB:2BYV}.
HELIX 981 987 {ECO:0000244|PDB:4MH0}.
HELIX 996 1006 {ECO:0000244|PDB:4MH0}.
SEQUENCE 1011 AA; 115491 MW; 449BC537475B03AA CRC64;
MVAAHAAHSQ SSAEWIACLD KRPLERSSED VDIIFTRLKG VKAFEKFHPN LLRQICLCGY
YENLEKGITL FRQGDIGTNW YAVLAGSLDV KVSETSSHQD AVTICTLGIG TAFGESILDN
TPRHATIVTR ESSELLRIEQ EDFKALWEKY RQYMAGLLAP PYGVMETGSN NDRIPDKENT
PLIEPHVPLR PAHTITKVPS EKILRAGKIL RIAILSRAPH MIRDRKYHLK TYRQCCVGTE
LVDWMIQQTS CVHSRTQAVG MWQVLLEDGV LNHVDQERHF QDKYLFYRFL DDEREDAPLP
TEEEKKECDE ELQDTMLLLS QMGPDAHMRM ILRKPPGQRT VDDLEIIYDE LLHIKALSHL
STTVKRELAG VLIFESHAKG GTVLFNQGEE GTSWYIILKG SVNVVIYGKG VVCTLHEGDD
FGKLALVNDA PRAASIVLRE DNCHFLRVDK EDFNRILRDV EANTVRLKEH DQDVLVLEKV
PAGNRAANQG NSQPQQKYTV MSGTPEKILE HFLETIRLEP SLNEATDSVL NDFVMMHCVF
MPNTQLCPAL VAHYHAQPSQ GTEQERMDYA LNNKRRVIRL VLQWAAMYGD LLQEDDVAMA
FLEEFYVSVS DDARMMAAFK EQLPELEKIV KQISEDAKAP QKKHKVLLQQ FNTGDERAQK
RQPIRGSDEV LFKVYCIDHT YTTIRVPVAA SVKEVISAVA DKLGSGEGLI IVKMNSGGEK
VVLKSNDVSV FTTLTINGRL FACPREQFDS LTPLPEQEGP TTGTVGTFEL MSSKDLAYQM
TTYDWELFNC VHELELIYHT FGRHNFKKTT ANLDLFLRRF NEIQFWVVTE VCLCSQLSKR
VQLLKKFIKI AAHCKEYKNL NSFFAIVMGL SNVAVSRLAL TWEKLPSKFK KFYAEFESLM
DPSRNHRAYR LTAAKLEPPL IPFMPLLIKD MTFTHEGNKT FIDNLVNFEK MRMIANTART
VRYYRSQPFN PDAAQANKNH QDVRSYVRQL NVIDNQRTLS QMSHRLEPRR P


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