RPGF4_HUMAN
ID RPGF4_HUMAN Reviewed; 1011 AA.
AC Q8WZA2; B2R7R3; B7Z283; B7Z3T6; B7Z912; O95636; Q8IXK6; Q8TAA4;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 173.
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-regulated guanine nucleotide exchange factor II;
DE Short=cAMP-GEFII;
GN Name=RAPGEF4; Synonyms=CGEF2, EPAC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=9856955; DOI=10.1126/science.282.5397.2275;
RA Kawasaki H., Springett G.M., Mochizuki N., Toki S., Nakaya M., Matsuda M.,
RA Housman D.E., Graybiel A.M.;
RT "A family of cAMP-binding proteins that directly activate rap1.";
RL Science 282:2275-2279(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE PROMOTER
RP USAGE.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Amygdala, Hippocampus, Thalamus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Hypothalamus, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=10777494; DOI=10.1074/jbc.m001113200;
RA de Rooij J., Rehmann H., van Triest M., Cool R.H., Wittinghofer A.,
RA Bos J.L.;
RT "Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs.";
RL J. Biol. Chem. 275:20829-20836(2000).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10777494, ECO:0000269|PubMed:9856955}.
CC -!- SUBUNIT: Interacts with RIMS1 and RIMS2. Probably part of a complex
CC with RIMS2 and GTP-activated RAB3A (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8WZA2; Q96MC5: BMERB1; NbExp=4; IntAct=EBI-948476, EBI-718468;
CC Q8WZA2; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-948476, EBI-745369;
CC Q8WZA2; P42858: HTT; NbExp=3; IntAct=EBI-948476, EBI-466029;
CC Q8WZA2; P05455: SSB; NbExp=3; IntAct=EBI-948476, EBI-358037;
CC Q8WZA2; Q9UH65: SWAP70; NbExp=4; IntAct=EBI-948476, EBI-310749;
CC Q8WZA2; P49459: UBE2A; NbExp=3; IntAct=EBI-948476, EBI-2339348;
CC Q8WZA2-3; P54253: ATXN1; NbExp=3; IntAct=EBI-25977442, EBI-930964;
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=5;
CC Name=1;
CC IsoId=Q8WZA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WZA2-2; Sequence=VSP_007611;
CC Name=3;
CC IsoId=Q8WZA2-3; Sequence=VSP_007612, VSP_007613;
CC Name=4;
CC IsoId=Q8WZA2-4; Sequence=VSP_054423;
CC Name=5;
CC IsoId=Q8WZA2-5; Sequence=VSP_054423, VSP_054424;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and adrenal gland.
CC Isoform 2 is expressed in liver. Isoform 1 is expressed in liver at
CC very low levels.
CC -!- DOMAIN: The N-terminal nucleotide phosphate binding region cAMP 1 has a
CC much lower affinity for cAMP as compared to cAMP 2.
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 Promoter analysis was carried out in mouse.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC Promoter analysis was carried out in mouse. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
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DR EMBL; U78516; AAD03422.1; -; mRNA.
DR EMBL; AB027471; BAB72179.1; -; mRNA.
DR EMBL; AK294445; BAH11769.1; -; mRNA.
DR EMBL; AK296340; BAH12322.1; -; mRNA.
DR EMBL; AK304278; BAH14148.1; -; mRNA.
DR EMBL; AK313084; BAG35910.1; -; mRNA.
DR EMBL; AK316072; BAH14443.1; -; mRNA.
DR EMBL; AC009484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024004; AAH24004.1; -; mRNA.
DR EMBL; BC040183; AAH40183.1; -; mRNA.
DR CCDS; CCDS42775.1; -. [Q8WZA2-1]
DR CCDS; CCDS42776.1; -. [Q8WZA2-3]
DR CCDS; CCDS63060.1; -. [Q8WZA2-4]
DR CCDS; CCDS63061.1; -. [Q8WZA2-5]
DR RefSeq; NP_001093867.1; NM_001100397.1. [Q8WZA2-3]
DR RefSeq; NP_001269828.1; NM_001282899.1. [Q8WZA2-4]
DR RefSeq; NP_001269829.1; NM_001282900.1. [Q8WZA2-5]
DR RefSeq; NP_001269830.1; NM_001282901.1.
DR RefSeq; NP_008954.2; NM_007023.3. [Q8WZA2-1]
DR RefSeq; XP_006712268.1; XM_006712205.3. [Q8WZA2-5]
DR AlphaFoldDB; Q8WZA2; -.
DR SMR; Q8WZA2; -.
DR BioGRID; 116253; 18.
DR IntAct; Q8WZA2; 14.
DR STRING; 9606.ENSP00000380271; -.
DR BindingDB; Q8WZA2; -.
DR ChEMBL; CHEMBL2029198; -.
DR GuidetoPHARMACOLOGY; 1293; -.
DR iPTMnet; Q8WZA2; -.
DR PhosphoSitePlus; Q8WZA2; -.
DR BioMuta; RAPGEF4; -.
DR DMDM; 32171491; -.
DR jPOST; Q8WZA2; -.
DR MassIVE; Q8WZA2; -.
DR PaxDb; Q8WZA2; -.
DR PeptideAtlas; Q8WZA2; -.
DR PRIDE; Q8WZA2; -.
DR ProteomicsDB; 6419; -.
DR ProteomicsDB; 6544; -.
DR ProteomicsDB; 75243; -. [Q8WZA2-1]
DR ProteomicsDB; 75244; -. [Q8WZA2-2]
DR ProteomicsDB; 75245; -. [Q8WZA2-3]
DR Antibodypedia; 3825; 178 antibodies from 33 providers.
DR DNASU; 11069; -.
DR Ensembl; ENST00000397081.8; ENSP00000380271.3; ENSG00000091428.18. [Q8WZA2-1]
DR Ensembl; ENST00000397087.7; ENSP00000380276.3; ENSG00000091428.18. [Q8WZA2-3]
DR Ensembl; ENST00000538974.5; ENSP00000440135.1; ENSG00000091428.18. [Q8WZA2-5]
DR Ensembl; ENST00000540783.5; ENSP00000440250.1; ENSG00000091428.18. [Q8WZA2-4]
DR GeneID; 11069; -.
DR KEGG; hsa:11069; -.
DR MANE-Select; ENST00000397081.8; ENSP00000380271.3; NM_007023.4; NP_008954.2.
DR UCSC; uc002uhv.5; human. [Q8WZA2-1]
DR CTD; 11069; -.
DR DisGeNET; 11069; -.
DR GeneCards; RAPGEF4; -.
DR HGNC; HGNC:16626; RAPGEF4.
DR HPA; ENSG00000091428; Tissue enhanced (brain, choroid plexus).
DR MIM; 606058; gene.
DR neXtProt; NX_Q8WZA2; -.
DR OpenTargets; ENSG00000091428; -.
DR PharmGKB; PA134861108; -.
DR VEuPathDB; HostDB:ENSG00000091428; -.
DR eggNOG; KOG2378; Eukaryota.
DR GeneTree; ENSGT00940000156075; -.
DR InParanoid; Q8WZA2; -.
DR OMA; HIVFMPT; -.
DR OrthoDB; 143470at2759; -.
DR PhylomeDB; Q8WZA2; -.
DR TreeFam; TF313184; -.
DR PathwayCommons; Q8WZA2; -.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-392517; Rap1 signalling.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR SignaLink; Q8WZA2; -.
DR SIGNOR; Q8WZA2; -.
DR BioGRID-ORCS; 11069; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; RAPGEF4; human.
DR GeneWiki; RAPGEF4; -.
DR GenomeRNAi; 11069; -.
DR Pharos; Q8WZA2; Tchem.
DR PRO; PR:Q8WZA2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WZA2; protein.
DR Bgee; ENSG00000091428; Expressed in right frontal lobe and 168 other tissues.
DR ExpressionAtlas; Q8WZA2; baseline and differential.
DR Genevisible; Q8WZA2; HS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; TAS:Reactome.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IEA:Ensembl.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl.
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 Alternative promoter usage; Alternative splicing; cAMP; cAMP-binding;
KW Cytoplasm; Exocytosis; Guanine-nucleotide releasing factor; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1011
FT /note="Rap guanine nucleotide exchange factor 4"
FT /id="PRO_0000068870"
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 /id="VSP_007611"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054423"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007612"
FT VAR_SEQ 145..148
FT /note="ALWE -> MLYK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007613"
FT VAR_SEQ 180..197
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054424"
FT CONFLICT 324
FT /note="P -> R (in Ref. 5; AAH40183)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="H -> R (in Ref. 5; AAH40183)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="L -> I (in Ref. 5; AAH40183)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="H -> P (in Ref. 5; AAH24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="T -> M (in Ref. 5; AAH24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="V -> I (in Ref. 1; AAD03422)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="P -> T (in Ref. 5; AAH40183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1011 AA; 115522 MW; 9427C5F92F2FFAD1 CRC64;
MVAAHAAHSS SSAEWIACLD KRPLERSSED VDIIFTRLKE VKAFEKFHPN LLHQICLCGY
YENLEKGITL FRQGDIGTNW YAVLAGSLDV KVSETSSHQD AVTICTLGIG TAFGESILDN
TPRHATIVTR ESSELLRIEQ KDFKALWEKY RQYMAGLLAP PYGVMETGSN NDRIPDKENT
PLIEPHVPLR PANTITKVPS EKILRAGKIL RNAILSRAPH MIRDRKYHLK TYRQCCVGTE
LVDWMMQQTP CVHSRTQAVG MWQVLLEDGV LNHVDQEHHF QDKYLFYRFL DDEHEDAPLP
TEEEKKECDE ELQDTMLLLS QMGPDAHMRM ILRKPPGQRT VDDLEIIYEE LLHIKALSHL
STTVKRELAG VLIFESHAKG GTVLFNQGEE GTSWYIILKG SVNVVIYGKG VVCTLHEGDD
FGKLALVNDA PRAASIVLRE DNCHFLRVDK EDFNRILRDV EANTVRLKEH DQDVLVLEKV
PAGNRASNQG NSQPQQKYTV MSGTPEKILE HFLETIRLEA TLNEATDSVL NDFIMMHCVF
MPNTQLCPAL VAHYHAQPSQ GTEQEKMDYA LNNKRRVIRL VLQWAAMYGD LLQEDDVSMA
FLEEFYVSVS DDARMIAALK EQLPELEKIV KQISEDAKAP QKKHKVLLQQ FNTGDERAQK
RQPIRGSDEV LFKVYCMDHT YTTIRVPVAT SVKEVISAVA DKLGSGEGLI IVKMSSGGEK
VVLKPNDVSV FTTLTINGRL FACPREQFDS LTPLPEQEGP TVGTVGTFEL MSSKDLAYQM
TIYDWELFNC VHELELIYHT FGRHNFKKTT ANLDLFLRRF NEIQFWVVTE ICLCSQLSKR
VQLLKKFIKI AAHCKEYKNL NSFFAIVMGL SNVAVSRLAL TWEKLPSKFK KFYAEFESLM
DPSRNHRAYR LTVAKLEPPL IPFMPLLIKD MTFTHEGNKT FIDNLVNFEK MRMIANTART
VRYYRSQPFN PDAAQANKNH QDVRSYVRQL NVIDNQRTLS QMSHRLEPRR P
