ID RPGF4_MOUSE Reviewed; 1011 AA. AC Q9EQZ6; Q8VIP9; Q9CW52; Q9Z1P0; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 190. 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-dependent Rap1 guanine-nucleotide exchange factor; DE AltName: Full=cAMP-regulated guanine nucleotide exchange factor II; DE Short=cAMP-GEFII; GN Name=Rapgef4; Synonyms=Cgef2, Epac2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Brain; RA Gaudriault G.E., Takaya K., Vale W.W.; RT "A brain cAMP-dependent Rap1 guanine-nucleotide exchange factor."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP INTERACTION WITH RIMS1 AND RIMS2. RX PubMed=11056535; DOI=10.1038/35041046; RA Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H., RA Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S.; RT "cAMP-GEFII is a direct target of cAMP in regulated exocytosis."; RL Nat. Cell Biol. 2:805-811(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE PROMOTER USAGE. RC TISSUE=Liver; RX PubMed=11707077; DOI=10.1006/geno.2001.6641; RA Ueno H., Shibasaki T., Iwanaga T., Takahashi K., Yokoyama Y., Liu L.M., RA Yokoi N., Ozaki N., Matsukura S., Yano H., Seino S.; RT "Characterization of the gene EPAC2: structure, chromosomal localization, RT tissue expression, and identification of the liver-specific isoform."; RL Genomics 78:91-98(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-463. RX PubMed=12469113; DOI=10.1038/nsb878; RA Rehmann H., Prakash B., Wolf E., Rueppel A., De Rooij J., Bos J.L., RA Wittinghofer A.; RT "Structure and regulation of the cAMP-binding domains of Epac2."; RL Nat. Struct. Biol. 10:26-32(2003). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 324-1011 IN COMPLEX WITH CAMP RP ANALOG AND RAP1B, SUBUNIT, AND MUTAGENESIS OF LEU-467; TYR-498 AND TYR-569. RX PubMed=18660803; DOI=10.1038/nature07187; RA Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O., Bos J.L.; RT "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B."; RL Nature 455:124-127(2008). 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. {ECO:0000269|PubMed:11056535}. CC -!- SUBUNIT: Interacts with RAP1B, RIMS1 and RIMS2. Probably part of a CC complex with RIMS2 and GTP-activated RAB3A. CC {ECO:0000269|PubMed:11056535, ECO:0000269|PubMed:18660803}. CC -!- INTERACTION: CC Q9EQZ6; P01112: HRAS; Xeno; NbExp=3; IntAct=EBI-772212, EBI-350145; CC Q9EQZ6-3; P61224: RAP1B; Xeno; NbExp=3; IntAct=EBI-15566495, EBI-358143; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9EQZ6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9EQZ6-2; Sequence=VSP_007614; CC Name=3; CC IsoId=Q9EQZ6-3; Sequence=VSP_007615; CC -!- TISSUE SPECIFICITY: Expressed in cerebellum, pituitary, adrenal gland CC and liver. {ECO:0000269|PubMed:11056535}. CC -!- DOMAIN: The N-terminal nucleotide phosphate binding region cAMP 1 has a CC much lower affinity for cAMP as compared to cAMP 2. {ECO:0000250}. CC -!- DOMAIN: The DEP domain is involved in membrane localization independent CC from regulation by cAMP. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF115480; AAD09132.1; -; mRNA. DR EMBL; AB021132; BAB18976.1; -; mRNA. DR EMBL; AB037668; BAB72180.1; -; mRNA. DR EMBL; AK004874; BAB23633.1; -; mRNA. DR CCDS; CCDS16120.1; -. [Q9EQZ6-3] DR CCDS; CCDS57176.1; -. [Q9EQZ6-1] DR RefSeq; NP_001191094.1; NM_001204165.1. [Q9EQZ6-1] DR RefSeq; NP_001191095.1; NM_001204166.1. DR RefSeq; NP_062662.1; NM_019688.2. [Q9EQZ6-3] DR PDB; 1O7F; X-ray; 2.50 A; A=1-481. DR PDB; 2BYV; X-ray; 2.70 A; E=1-1011. DR PDB; 3CF6; X-ray; 2.20 A; E=324-1011. DR PDB; 4F7Z; X-ray; 2.60 A; A=1-1011. DR PDB; 4MGI; X-ray; 2.80 A; E=324-1011. DR PDB; 4MGK; X-ray; 2.70 A; E=324-1011. DR PDB; 4MGY; X-ray; 2.60 A; E=324-1011. DR PDB; 4MGZ; X-ray; 3.00 A; E=324-1011. DR PDB; 4MH0; X-ray; 2.40 A; E=324-1011. DR PDBsum; 1O7F; -. DR PDBsum; 2BYV; -. DR PDBsum; 3CF6; -. DR PDBsum; 4F7Z; -. DR PDBsum; 4MGI; -. DR PDBsum; 4MGK; -. DR PDBsum; 4MGY; -. DR PDBsum; 4MGZ; -. DR PDBsum; 4MH0; -. DR AlphaFoldDB; Q9EQZ6; -. DR SASBDB; Q9EQZ6; -. DR SMR; Q9EQZ6; -. DR BioGRID; 208026; 25. DR CORUM; Q9EQZ6; -. DR DIP; DIP-32333N; -. DR IntAct; Q9EQZ6; 8. DR MINT; Q9EQZ6; -. DR STRING; 10090.ENSMUSP00000088336; -. DR BindingDB; Q9EQZ6; -. DR ChEMBL; CHEMBL3593151; -. DR GlyGen; Q9EQZ6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9EQZ6; -. DR MetOSite; Q9EQZ6; -. DR PhosphoSitePlus; Q9EQZ6; -. DR SwissPalm; Q9EQZ6; -. DR MaxQB; Q9EQZ6; -. DR PaxDb; 10090-ENSMUSP00000099759; -. DR PeptideAtlas; Q9EQZ6; -. DR ProteomicsDB; 299872; -. [Q9EQZ6-1] DR ProteomicsDB; 299873; -. [Q9EQZ6-2] DR ProteomicsDB; 299874; -. [Q9EQZ6-3] DR Antibodypedia; 3825; 198 antibodies from 33 providers. DR DNASU; 56508; -. DR Ensembl; ENSMUST00000090826.12; ENSMUSP00000088336.6; ENSMUSG00000049044.17. [Q9EQZ6-1] DR Ensembl; ENSMUST00000102698.10; ENSMUSP00000099759.4; ENSMUSG00000049044.17. [Q9EQZ6-3] DR GeneID; 56508; -. DR KEGG; mmu:56508; -. DR UCSC; uc008kbn.2; mouse. [Q9EQZ6-1] DR UCSC; uc008kbo.2; mouse. [Q9EQZ6-3] DR AGR; MGI:1917723; -. DR CTD; 11069; -. DR MGI; MGI:1917723; Rapgef4. DR VEuPathDB; HostDB:ENSMUSG00000049044; -. DR eggNOG; KOG2378; Eukaryota. DR GeneTree; ENSGT00940000156075; -. DR InParanoid; Q9EQZ6; -. DR OMA; LYCYVLE; -. DR OrthoDB; 5473909at2759; -. DR PhylomeDB; Q9EQZ6; -. DR TreeFam; TF313184; -. DR Reactome; R-MMU-354192; Integrin signaling. DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-MMU-392517; Rap1 signalling. DR Reactome; R-MMU-422356; Regulation of insulin secretion. DR BioGRID-ORCS; 56508; 3 hits in 79 CRISPR screens. DR ChiTaRS; Rapgef4; mouse. DR EvolutionaryTrace; Q9EQZ6; -. DR PRO; PR:Q9EQZ6; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q9EQZ6; Protein. DR Bgee; ENSMUSG00000049044; Expressed in globus pallidus and 207 other cell types or tissues. DR ExpressionAtlas; Q9EQZ6; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0005903; C:brush border; ISO:MGI. DR GO; GO:0044316; C:cone cell pedicle; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0060076; C:excitatory synapse; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0030426; C:growth cone; ISO:MGI. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0014069; C:postsynaptic density; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0030552; F:cAMP binding; IDA:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:MGI. DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:MGI. DR GO; GO:0046879; P:hormone secretion; IMP:MGI. DR GO; GO:0030073; P:insulin secretion; IDA:MGI. DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI. DR GO; GO:1904457; P:positive regulation of neuronal action potential; ISO:MGI. DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI. DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central. DR GO; GO:0050773; P:regulation of dendrite development; ISO:MGI. DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI. DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI. DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI. DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO. DR CDD; cd00038; CAP_ED; 2. DR CDD; cd04437; DEP_Epac; 1. DR CDD; cd00155; RasGEF; 1. DR CDD; cd06224; REM; 1. DR Gene3D; 1.10.8.1240; -; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1. DR Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR000591; DEP_dom. 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; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1. DR PANTHER; PTHR23113:SF175; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 4; 1. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00610; DEP; 1. DR Pfam; PF00617; RasGEF; 1. DR Pfam; PF00618; RasGEF_N; 1. DR PRINTS; PR00103; CAMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00049; DEP; 1. DR SMART; SM00147; RasGEF; 1. DR SMART; SM00229; RasGEFN; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 2. DR SUPFAM; SSF48366; Ras GEF; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 2. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS00720; RASGEF; 1. DR PROSITE; PS50009; RASGEF_CAT; 1. DR PROSITE; PS50212; RASGEF_NTER; 1. DR Genevisible; Q9EQZ6; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative promoter usage; Alternative splicing; cAMP; KW cAMP-binding; Cytoplasm; Exocytosis; Guanine-nucleotide releasing factor; KW Membrane; Nucleotide-binding; Reference proteome; Repeat. FT CHAIN 1..1011 FT /note="Rap guanine nucleotide exchange factor 4" FT /id="PRO_0000068871" FT DOMAIN 216..291 FT /note="DEP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066" FT DOMAIN 496..634 FT /note="N-terminal Ras-GEF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135" FT DOMAIN 772..1009 FT /note="Ras-GEF" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168" FT BINDING 422..425 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /evidence="ECO:0000250|UniProtKB:O95398" FT BINDING 432..433 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /evidence="ECO:0000250|UniProtKB:O95398" FT VAR_SEQ 1..315 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11707077, FT ECO:0000303|PubMed:16141072" FT /id="VSP_007614" FT VAR_SEQ 180..197 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_007615" FT MUTAGEN 467 FT /note="L->A: Less than 10% of the wild-type maximal FT activity." FT /evidence="ECO:0000269|PubMed:18660803" FT MUTAGEN 498 FT /note="Y->F: 2-fold reduction in maximal activity." FT /evidence="ECO:0000269|PubMed:18660803" FT MUTAGEN 569 FT /note="Y->A: 2-fold reduction in maximal activity." FT /evidence="ECO:0000269|PubMed:18660803" FT MUTAGEN 569 FT /note="Y->F: 2-fold reduction in maximal activity." FT /evidence="ECO:0000269|PubMed:18660803" FT CONFLICT 313 FT /note="Q -> E (in Ref. 4; BAB23633)" FT /evidence="ECO:0000305" FT CONFLICT 452 FT /note="D -> E (in Ref. 4; BAB23633)" FT /evidence="ECO:0000305" FT HELIX 14..19 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:4F7Z" FT HELIX 28..38 FT /evidence="ECO:0007829|PDB:1O7F" FT TURN 42..46 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 49..58 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 79..86 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 115..119 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 124..139 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 140..150 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:1O7F" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:1O7F" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 202..217 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 231..237 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 238..247 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 255..267 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 270..275 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 286..289 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:1O7F" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 303..310 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 329..333 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 341..351 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:1O7F" FT HELIX 362..368 FT /evidence="ECO:0007829|PDB:4MH0" FT TURN 369..371 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 373..377 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 393..400 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 402..406 FT /evidence="ECO:0007829|PDB:4MH0" FT TURN 407..409 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 410..415 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 423..428 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 433..438 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 440..449 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 450..456 FT /evidence="ECO:0007829|PDB:4MH0" FT TURN 457..460 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 465..469 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 472..479 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 498..503 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 505..514 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 520..522 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 523..540 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 543..554 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 563..588 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 589..594 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 596..616 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 617..620 FT /evidence="ECO:0007829|PDB:4F7Z" FT HELIX 622..629 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 668..675 FT /evidence="ECO:0007829|PDB:4MH0" FT TURN 677..679 FT /evidence="ECO:0007829|PDB:2BYV" FT STRAND 681..687 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 692..703 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 710..714 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 720..722 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 731..733 FT /evidence="ECO:0007829|PDB:4MGY" FT STRAND 739..743 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 745..750 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 755..757 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 765..768 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 773..789 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 793..801 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 803..805 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 811..832 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 837..856 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 860..871 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 873..876 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 879..884 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 887..898 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 903..915 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 924..937 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 940..942 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 945..947 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 948..964 FT /evidence="ECO:0007829|PDB:4MH0" FT STRAND 965..967 FT /evidence="ECO:0007829|PDB:2BYV" FT STRAND 973..975 FT /evidence="ECO:0007829|PDB:2BYV" FT HELIX 981..987 FT /evidence="ECO:0007829|PDB:4MH0" FT HELIX 996..1006 FT /evidence="ECO:0007829|PDB:4MH0" SQ 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 //