ARHGP_HUMAN
ID ARHGP_HUMAN Reviewed; 580 AA.
AC Q86VW2; A6NJH5; A9CQZ6; F8W7Z4; Q8WV84; Q96E63;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Rho guanine nucleotide exchange factor 25;
DE AltName: Full=Guanine nucleotide exchange factor GEFT;
DE AltName: Full=Rac/Cdc42/Rho exchange factor GEFT;
DE AltName: Full=RhoA/Rac/Cdc42 guanine nucleotide exchange factor GEFT;
DE AltName: Full=p63RhoGEF;
GN Name=ARHGEF25; Synonyms=GEFT;
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), FUNCTION, INTERACTION WITH CDC42
RP AND RAC1, TISSUE SPECIFICITY, AND VARIANT TYR-253.
RX PubMed=12547822; DOI=10.1074/jbc.m208896200;
RA Guo X., Stafford L.J., Bryan B., Xia C., Ma W., Wu X., Liu D., Songyang Z.,
RA Liu M.;
RT "A Rac/Cdc42-specific exchange factor, GEFT, induces cell proliferation,
RT transformation, and migration.";
RL J. Biol. Chem. 278:13207-13215(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT ARG-506.
RC TISSUE=Brain;
RA Nagase T., Kikuno R.F., Ohara O.;
RT "Human cDNA derived from mRNA for adult brain.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP TYR-253; ARG-397 AND ARG-506.
RC TISSUE=Brain;
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP LEU-301.
RX PubMed=11861769; DOI=10.1242/jcs.115.3.629;
RA Souchet M., Portales-Casamar E., Mazurais D., Schmidt S., Leger I.,
RA Javre J.L., Robert P., Berrebi-Bertrand I., Bril A., Gout B., Debant A.,
RA Calmels T.P.;
RT "Human p63RhoGEF, a novel RhoA-specific guanine nucleotide exchange factor,
RT is localized in cardiac sarcomere.";
RL J. Cell Sci. 115:629-640(2002).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15069594; DOI=10.1007/s00210-004-0926-5;
RA Lutz S., Freichel-Blomquist A., Rumenapp U., Schmidt M., Jakobs K.H.,
RA Wieland T.;
RT "p63RhoGEF and GEFT are Rho-specific guanine nucleotide exchange factors
RT encoded by the same gene.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 369:540-546(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH GNAQ AND GNA11.
RX PubMed=15632174; DOI=10.1074/jbc.m411322200;
RA Lutz S., Freichel-Blomquist A., Yang Y., Rumenapp U., Jakobs K.H.,
RA Schmidt M., Wieland T.;
RT "The guanine nucleotide exchange factor p63RhoGEF, a specific link between
RT Gq/11-coupled receptor signaling and RhoA.";
RL J. Biol. Chem. 280:11134-11139(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH RHO-FAMILY SMALL GTPASES.
RX PubMed=16314529; DOI=10.1128/mcb.25.24.11089-11101.2005;
RA Bryan B.A., Mitchell D.C., Zhao L., Ma W., Stafford L.J., Teng B.B.,
RA Liu M.;
RT "Modulation of muscle regeneration, myogenesis, and adipogenesis by the Rho
RT family guanine nucleotide exchange factor GEFT.";
RL Mol. Cell. Biol. 25:11089-11101(2005).
RN [10]
RP FUNCTION, INTERACTION WITH GNAQ, DOMAIN, REGION, AND MUTAGENESIS OF
RP PHE-471; LEU-472; LEU-475; PRO-478 AND ILE-479.
RX PubMed=17606614; DOI=10.1074/jbc.m703458200;
RA Rojas R.J., Yohe M.E., Gershburg S., Kawano T., Kozasa T., Sondek J.;
RT "Galphaq directly activates p63RhoGEF and Trio via a conserved extension of
RT the Dbl homology-associated pleckstrin homology domain.";
RL J. Biol. Chem. 282:29201-29210(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 149-502.
RX PubMed=18096806; DOI=10.1126/science.1147554;
RA Lutz S., Shankaranarayanan A., Coco C., Ridilla M., Nance M.R., Vettel C.,
RA Baltus D., Evelyn C.R., Neubig R.R., Wieland T., Tesmer J.J.;
RT "Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the
RT activation of RhoA by GPCRs.";
RL Science 318:1923-1927(2007).
CC -!- FUNCTION: May play a role in actin cytoskeleton reorganization in
CC different tissues since its activation induces formation of actin
CC stress fibers. It works as a guanine nucleotide exchange factor for Rho
CC family of small GTPases. Links specifically G alpha q/11-coupled
CC receptors to RHOA activation. May be an important regulator of
CC processes involved in axon and dendrite formation. In neurons seems to
CC be an exchange factor primarily for RAC1. Involved in skeletal
CC myogenesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:11861769,
CC ECO:0000269|PubMed:12547822, ECO:0000269|PubMed:15069594,
CC ECO:0000269|PubMed:15632174, ECO:0000269|PubMed:16314529,
CC ECO:0000269|PubMed:17606614}.
CC -!- SUBUNIT: Interacts (via the DH domain) with BVES (via the C-terminus
CC cytoplasmic tail) (By similarity). Interacts with activated GNAQ and
CC GNA11. Interacts with RHOA, CDC42 and RAC1. {ECO:0000250,
CC ECO:0000269|PubMed:12547822, ECO:0000269|PubMed:15632174,
CC ECO:0000269|PubMed:16314529, ECO:0000269|PubMed:17606614}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm,
CC myofibril, sarcomere {ECO:0000269|PubMed:11861769}. Note=Highly
CC colocalizes with actin regions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86VW2-1; Sequence=Displayed;
CC Name=2; Synonyms=p63RhoGef;
CC IsoId=Q86VW2-2; Sequence=VSP_031875;
CC Name=3;
CC IsoId=Q86VW2-3; Sequence=VSP_047254;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in
CC excitable tissues, such as brain, heart and muscle. Also detected in
CC kidney and liver. {ECO:0000269|PubMed:11861769,
CC ECO:0000269|PubMed:12547822, ECO:0000269|PubMed:15069594}.
CC -!- DOMAIN: The guanine nucleotide exchange activity is autoinhibited by
CC the PH domain. {ECO:0000269|PubMed:17606614}.
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DR EMBL; AF487514; AAO49463.2; -; mRNA.
DR EMBL; AB370196; BAF94999.1; -; mRNA.
DR EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97037.1; -; Genomic_DNA.
DR EMBL; BC012860; AAH12860.1; -; mRNA.
DR EMBL; BC018536; AAH18536.1; -; mRNA.
DR EMBL; BC047559; AAH47559.1; -; mRNA.
DR CCDS; CCDS44931.1; -. [Q86VW2-3]
DR CCDS; CCDS8947.1; -. [Q86VW2-1]
DR RefSeq; NP_001104740.1; NM_001111270.2. [Q86VW2-3]
DR RefSeq; NP_001334862.1; NM_001347933.1.
DR RefSeq; NP_891992.2; NM_182947.3. [Q86VW2-1]
DR PDB; 2RGN; X-ray; 3.50 A; B/E=149-502.
DR PDBsum; 2RGN; -.
DR AlphaFoldDB; Q86VW2; -.
DR SMR; Q86VW2; -.
DR BioGRID; 125438; 26.
DR CORUM; Q86VW2; -.
DR IntAct; Q86VW2; 7.
DR STRING; 9606.ENSP00000335560; -.
DR iPTMnet; Q86VW2; -.
DR PhosphoSitePlus; Q86VW2; -.
DR SwissPalm; Q86VW2; -.
DR BioMuta; ARHGEF25; -.
DR DMDM; 172046695; -.
DR jPOST; Q86VW2; -.
DR MassIVE; Q86VW2; -.
DR PaxDb; Q86VW2; -.
DR PeptideAtlas; Q86VW2; -.
DR PRIDE; Q86VW2; -.
DR ProteomicsDB; 30042; -.
DR ProteomicsDB; 70082; -. [Q86VW2-1]
DR ProteomicsDB; 70083; -. [Q86VW2-2]
DR Antibodypedia; 34950; 74 antibodies from 18 providers.
DR DNASU; 115557; -.
DR Ensembl; ENST00000286494.9; ENSP00000286494.4; ENSG00000240771.8. [Q86VW2-1]
DR Ensembl; ENST00000333972.11; ENSP00000335560.7; ENSG00000240771.8. [Q86VW2-3]
DR Ensembl; ENST00000616622.1; ENSP00000484303.1; ENSG00000240771.8. [Q86VW2-2]
DR GeneID; 115557; -.
DR KEGG; hsa:115557; -.
DR MANE-Select; ENST00000286494.9; ENSP00000286494.4; NM_182947.4; NP_891992.3.
DR UCSC; uc001spa.5; human. [Q86VW2-1]
DR CTD; 115557; -.
DR DisGeNET; 115557; -.
DR GeneCards; ARHGEF25; -.
DR HGNC; HGNC:30275; ARHGEF25.
DR HPA; ENSG00000240771; Low tissue specificity.
DR MIM; 610215; gene.
DR neXtProt; NX_Q86VW2; -.
DR OpenTargets; ENSG00000240771; -.
DR VEuPathDB; HostDB:ENSG00000240771; -.
DR eggNOG; KOG0689; Eukaryota.
DR GeneTree; ENSGT00940000160422; -.
DR HOGENOM; CLU_001356_6_0_1; -.
DR InParanoid; Q86VW2; -.
DR OMA; HAVEVMC; -.
DR OrthoDB; 301115at2759; -.
DR PhylomeDB; Q86VW2; -.
DR TreeFam; TF318080; -.
DR PathwayCommons; Q86VW2; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q86VW2; -.
DR SIGNOR; Q86VW2; -.
DR BioGRID-ORCS; 115557; 18 hits in 1079 CRISPR screens.
DR EvolutionaryTrace; Q86VW2; -.
DR GeneWiki; GEFT; -.
DR GenomeRNAi; 115557; -.
DR Pharos; Q86VW2; Tbio.
DR PRO; PR:Q86VW2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86VW2; protein.
DR Bgee; ENSG00000240771; Expressed in right hemisphere of cerebellum and 97 other tissues.
DR ExpressionAtlas; Q86VW2; baseline and differential.
DR Genevisible; Q86VW2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030738; ARHGEF25.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR22826:SF117; PTHR22826:SF117; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN 1..580
FT /note="Rho guanine nucleotide exchange factor 25"
FT /id="PRO_0000322132"
FT DOMAIN 160..336
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 348..466
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 48..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..299
FT /note="Important for binding to Rho GTPases"
FT REGION 467..493
FT /note="Sufficient to bind activated GNAQ"
FT REGION 482..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031875"
FT VAR_SEQ 1..32
FT /note="MRGGHKGGRCACPRVIRKVLAKCGCCFARGGR -> MKPPDRPAPGRTDRIL
FT GVMGGMLRACALPGQEGPPRRSPLGLVGTEPESERTEGDHRRDREHEVLAGALQP (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047254"
FT VARIANT 253
FT /note="C -> Y (in dbSNP:rs17857333)"
FT /evidence="ECO:0000269|PubMed:12547822,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_039402"
FT VARIANT 397
FT /note="G -> R (in dbSNP:rs17854492)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039403"
FT VARIANT 506
FT /note="Q -> R (in dbSNP:rs1564374)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_039404"
FT MUTAGEN 301
FT /note="L->E: Abolishes its exchange activity on RHOA."
FT /evidence="ECO:0000269|PubMed:11861769"
FT MUTAGEN 471
FT /note="F->A: Reduces exchange activity mediated by GNAQ
FT activation; in truncated construct."
FT /evidence="ECO:0000269|PubMed:17606614"
FT MUTAGEN 472
FT /note="L->A: Reduces exchange activity mediated by GNAQ
FT activation; in truncated construct."
FT /evidence="ECO:0000269|PubMed:17606614"
FT MUTAGEN 475
FT /note="L->A: Reduces exchange activity mediated by GNAQ
FT activation; in truncated construct."
FT /evidence="ECO:0000269|PubMed:17606614"
FT MUTAGEN 478
FT /note="P->A: Reduces exchange activity mediated by GNAQ
FT activation; in truncated construct."
FT /evidence="ECO:0000269|PubMed:17606614"
FT MUTAGEN 479
FT /note="I->A: Reduces exchange activity mediated by GNAQ
FT activation; in truncated construct."
FT /evidence="ECO:0000269|PubMed:17606614"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 156..183
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2RGN"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:2RGN"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 316..338
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 355..364
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 378..393
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:2RGN"
FT STRAND 441..450
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 451..475
FT /evidence="ECO:0007829|PDB:2RGN"
FT HELIX 478..489
FT /evidence="ECO:0007829|PDB:2RGN"
SQ SEQUENCE 580 AA; 63843 MW; F3EC80445D965BFB CRC64;
MRGGHKGGRC ACPRVIRKVL AKCGCCFARG GRESYSIAGS EGSISASAAS GLAAPSGPSS
GLSSGPCSPG PPGPVSGLRR WLDHSKHCLS VETEADSGQA GPYENWMLEP ALATGEELPE
LTLLTTLLEG PGDKTQPPEE ETLSQAPESE EEQKKKALER SMYVLSELVE TEKMYVDDLG
QIVEGYMATM AAQGVPESLR GRDRIVFGNI QQIYEWHRDY FLQELQRCLK DPDWLAQLFI
KHERRLHMYV VYCQNKPKSE HVVSEFGDSY FEELRQQLGH RLQLNDLLIK PVQRIMKYQL
LLKDFLKYYN RAGMDTADLE QAVEVMCFVP KRCNDMMTLG RLRGFEGKLT AQGKLLGQDT
FWVTEPEAGG LLSSRGRERR VFLFEQIIIF SEALGGGVRG GTQPGYVYKN SIKVSCLGLE
GNLQGDPCRF ALTSRGPEGG IQRYVLQAAD PAISQAWIKH VAQILESQRD FLNALQSPIE
YQRRESQTNS LGRPRGPGVG SPGRIQLGDQ AQGSTHTPIN GSLPSLLLSP KGEVARALLP
LDKQALGDIP QAPHDSPPVS PTPKTPPCQA RLAKLDEDEL
