RPGF4_MOUSE
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 03-AUG-2022, entry version 182.
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}.
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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; 24.
DR CORUM; Q9EQZ6; -.
DR DIP; DIP-32333N; -.
DR IntAct; Q9EQZ6; 8.
DR MINT; Q9EQZ6; -.
DR STRING; 10090.ENSMUSP00000099759; -.
DR BindingDB; Q9EQZ6; -.
DR ChEMBL; CHEMBL3593151; -.
DR iPTMnet; Q9EQZ6; -.
DR PhosphoSitePlus; Q9EQZ6; -.
DR MaxQB; Q9EQZ6; -.
DR PaxDb; Q9EQZ6; -.
DR PeptideAtlas; Q9EQZ6; -.
DR PRIDE; Q9EQZ6; -.
DR ProteomicsDB; 299872; -. [Q9EQZ6-1]
DR ProteomicsDB; 299873; -. [Q9EQZ6-2]
DR ProteomicsDB; 299874; -. [Q9EQZ6-3]
DR Antibodypedia; 3825; 178 antibodies from 33 providers.
DR DNASU; 56508; -.
DR Ensembl; ENSMUST00000090826; ENSMUSP00000088336; ENSMUSG00000049044. [Q9EQZ6-1]
DR Ensembl; ENSMUST00000102698; ENSMUSP00000099759; ENSMUSG00000049044. [Q9EQZ6-3]
DR GeneID; 56508; -.
DR KEGG; mmu:56508; -.
DR UCSC; uc008kbn.2; mouse. [Q9EQZ6-1]
DR UCSC; uc008kbo.2; mouse. [Q9EQZ6-3]
DR CTD; 11069; -.
DR MGI; MGI:1917723; Rapgef4.
DR VEuPathDB; HostDB:ENSMUSG00000049044; -.
DR eggNOG; KOG2378; Eukaryota.
DR GeneTree; ENSGT00940000156075; -.
DR InParanoid; Q9EQZ6; -.
DR OMA; HIVFMPT; -.
DR OrthoDB; 143470at2759; -.
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 74 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 205 other tissues.
DR ExpressionAtlas; Q9EQZ6; baseline and differential.
DR Genevisible; Q9EQZ6; MM.
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:0005929; C:cilium; 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; ISO:MGI.
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: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:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
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 GO; GO:0007165; P:signal transduction; ISO:MGI.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
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; PTHR23113; 2.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR SUPFAM; SSF54236; SSF54236; 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.
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
