RH5_PLAF7
ID RH5_PLAF7 Reviewed; 526 AA.
AC Q8IFM5;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Reticulocyte-binding protein homolog 5 {ECO:0000303|PubMed:18827878};
DE Short=PfRH5 {ECO:0000303|PubMed:18827878};
DE Flags: Precursor;
GN Name=RH5 {ECO:0000305}; Synonyms=PFD1145c {ECO:0000303|PubMed:18827878};
GN ORFNames=PF3D7_0424100 {ECO:0000312|EMBL:CAD49275.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=18827878; DOI=10.1371/journal.pone.0003300;
RA Rodriguez M., Lustigman S., Montero E., Oksov Y., Lobo C.A.;
RT "PfRH5: a novel reticulocyte-binding family homolog of plasmodium
RT falciparum that binds to the erythrocyte, and an investigation of its
RT receptor.";
RL PLoS ONE 3:E3300-E3300(2008).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=19000690; DOI=10.1016/j.ijpara.2008.10.006;
RA Baum J., Chen L., Healer J., Lopaticki S., Boyle M., Triglia T., Ehlgen F.,
RA Ralph S.A., Beeson J.G., Cowman A.F.;
RT "Reticulocyte-binding protein homologue 5 - an essential adhesin involved
RT in invasion of human erythrocytes by Plasmodium falciparum.";
RL Int. J. Parasitol. 39:371-380(2009).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH HUMAN BSG.
RX PubMed=22080952; DOI=10.1038/nature10606;
RA Crosnier C., Bustamante L.Y., Bartholdson S.J., Bei A.K., Theron M.,
RA Uchikawa M., Mboup S., Ndir O., Kwiatkowski D.P., Duraisingh M.T.,
RA Rayner J.C., Wright G.J.;
RT "Basigin is a receptor essential for erythrocyte invasion by Plasmodium
RT falciparum.";
RL Nature 480:534-537(2011).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN COMPLEX WITH RIPR, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=21909261; DOI=10.1371/journal.ppat.1002199;
RA Chen L., Lopaticki S., Riglar D.T., Dekiwadia C., Uboldi A.D., Tham W.H.,
RA O'Neill M.T., Richard D., Baum J., Ralph S.A., Cowman A.F.;
RT "An EGF-like protein forms a complex with PfRh5 and is required for
RT invasion of human erythrocytes by Plasmodium falciparum.";
RL PLoS Pathog. 7:E1002199-E1002199(2011).
RN [7] {ECO:0000305}
RP INTERACTION WITH HUMAN BSG.
RX PubMed=24297912; DOI=10.1073/pnas.1320771110;
RA Wanaguru M., Liu W., Hahn B.H., Rayner J.C., Wright G.J.;
RT "RH5-Basigin interaction plays a major role in the host tropism of
RT Plasmodium falciparum.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20735-20740(2013).
RN [8] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RX PubMed=25583518; DOI=10.1073/pnas.1415466112;
RA Reddy K.S., Amlabu E., Pandey A.K., Mitra P., Chauhan V.S., Gaur D.;
RT "Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr
RT is crucial for Plasmodium falciparum erythrocyte invasion.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1179-1184(2015).
RN [9] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=27374406; DOI=10.1016/j.chom.2016.06.004;
RA Volz J.C., Yap A., Sisquella X., Thompson J.K., Lim N.T., Whitehead L.W.,
RA Chen L., Lampe M., Tham W.H., Wilson D., Nebl T., Marapana D., Triglia T.,
RA Wong W., Rogers K.L., Cowman A.F.;
RT "Essential Role of the PfRh5/PfRipr/CyRPA Complex during Plasmodium
RT falciparum Invasion of Erythrocytes.";
RL Cell Host Microbe 20:60-71(2016).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=28409866; DOI=10.1111/cmi.12747;
RA Aniweh Y., Gao X., Hao P., Meng W., Lai S.K., Gunalan K., Chu T.T.,
RA Sinha A., Lescar J., Chandramohanadas R., Li H.Y., Sze S.K., Preiser P.R.;
RT "P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton
RT of the host RBC.";
RL Cell. Microbiol. 19:0-0(2017).
RN [11] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX, IDENTIFICATION IN
RP COMPLEX WITH P113 AND HUMAN BSG, INTERACTION WITH P113; CYRPA AND HUMAN
RP BSG, BIOTECHNOLOGY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=28186186; DOI=10.1038/ncomms14333;
RA Galaway F., Drought L.G., Fala M., Cross N., Kemp A.C., Rayner J.C.,
RA Wright G.J.;
RT "P113 is a merozoite surface protein that binds the N terminus of
RT Plasmodium falciparum RH5.";
RL Nat. Commun. 8:14333-14333(2017).
RN [12] {ECO:0007744|PDB:4WAT}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 126-526, FUNCTION, INTERACTION
RP WITH HUMAN BSG, BIOTECHNOLOGY, GLYCOSYLATION AT ASN-214, AND DISULFIDE
RP BONDS.
RX PubMed=25296023; DOI=10.7554/elife.04187;
RA Chen L., Xu Y., Healer J., Thompson J.K., Smith B.J., Lawrence M.C.,
RA Cowman A.F.;
RT "Crystal structure of PfRh5, an essential P. falciparum ligand for invasion
RT of human erythrocytes.";
RL Elife 3:0-0(2014).
RN [13] {ECO:0007744|PDB:5MI0}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 140-526, INTERACTION WITH HUMAN
RP BSG, DISULFIDE BONDS, AND BIOTECHNOLOGY.
RX PubMed=28096331; DOI=10.1073/pnas.1616903114;
RA Campeotto I., Goldenzweig A., Davey J., Barfod L., Marshall J.M.,
RA Silk S.E., Wright K.E., Draper S.J., Higgins M.K., Fleishman S.J.;
RT "One-step design of a stable variant of the malaria invasion protein RH5
RT for use as a vaccine immunogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:998-1002(2017).
RN [14] {ECO:0007744|PDB:6RCU, ECO:0007744|PDB:6RCV}
RP X-RAY CRYSTALLOGRAPHY (3.58 ANGSTROMS) OF 26-526, FUNCTION, BIOTECHNOLOGY,
RP AND DISULFIDE BONDS.
RX PubMed=31204103; DOI=10.1016/j.cell.2019.05.025;
RA Alanine D.G.W., Quinkert D., Kumarasingha R., Mehmood S., Donnellan F.R.,
RA Minkah N.K., Dadonaite B., Diouf A., Galaway F., Silk S.E., Jamwal A.,
RA Marshall J.M., Miura K., Foquet L., Elias S.C., Labbe G.M., Douglas A.D.,
RA Jin J., Payne R.O., Illingworth J.J., Pattinson D.J., Pulido D.,
RA Williams B.G., de Jongh W.A., Wright G.J., Kappe S.H.I., Robinson C.V.,
RA Long C.A., Crabb B.S., Gilson P.R., Higgins M.K., Draper S.J.;
RT "Human Antibodies that Slow Erythrocyte Invasion Potentiate Malaria-
RT Neutralizing Antibodies.";
RL Cell 178:216-228.E21(2019).
RN [15] {ECO:0007744|PDB:6MPV}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.17 ANGSTROMS) OF 175-504 IN COMPLEX
RP WITH CYRPA AND RIPR, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX,
RP INTERACTION WITH HUMAN BSG, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=30542156; DOI=10.1038/s41586-018-0779-6;
RA Wong W., Huang R., Menant S., Hong C., Sandow J.J., Birkinshaw R.W.,
RA Healer J., Hodder A.N., Kanjee U., Tonkin C.J., Heckmann D., Soroka V.,
RA Sogaard T.M.M., Jorgensen T., Duraisingh M.T., Czabotar P.E.,
RA de Jongh W.A., Tham W.H., Webb A.I., Yu Z., Cowman A.F.;
RT "Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex.";
RL Nature 565:118-121(2019).
CC -!- FUNCTION: Essential for the invasion of host erythrocytes by blood
CC stage merozoites (PubMed:25583518, PubMed:27374406, PubMed:25296023,
CC PubMed:22080952, PubMed:18827878, PubMed:19000690, PubMed:31204103,
CC PubMed:28186186, PubMed:28409866). By binding P113 at the surface of
CC the merozoite and human BSG/basigin on the erythrocyte membrane, leads
CC to the establishment of a tight junction between the merozoite and host
CC erythrocyte membranes (PubMed:25583518, PubMed:27374406,
CC PubMed:25296023, PubMed:22080952, PubMed:28186186). In addition, the
CC interaction with BSG results in BSG dimerization which triggers an
CC increase in intracellular Ca(2+) in the erythrocyte (PubMed:27374406,
CC PubMed:28409866). This essential step leads to a rearrangement of the
CC erythrocyte cytoskeleton required for the merozoite invasion
CC (PubMed:28409866). {ECO:0000269|PubMed:18827878,
CC ECO:0000269|PubMed:19000690, ECO:0000269|PubMed:22080952,
CC ECO:0000269|PubMed:25296023, ECO:0000269|PubMed:25583518,
CC ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:28186186,
CC ECO:0000269|PubMed:28409866, ECO:0000269|PubMed:31204103}.
CC -!- SUBUNIT: Forms a complex composed of RH5, P113 and human BSG/basigin;
CC the complex bridges the merozoite and host erythrocyte membranes
CC (PubMed:28186186). Within the complex, interacts (via C-terminus) with
CC human BSG/basigin isoform 2 (via the extracellular domain); the
CC interaction is independent of BSG glycosylation status
CC (PubMed:22080952, PubMed:25296023, PubMed:28186186, PubMed:24297912,
CC PubMed:30542156, PubMed:28096331). Weakly interacts with P.troglodytes
CC BSG but not with G.gorilla BSG (PubMed:24297912). Also, interacts (via
CC N-terminus) with P113; the interaction tethers RH5 to the merozoite
CC membrane (PubMed:28186186). Component of the PfRH5 adhesion complex
CC composed of 1 copy of CyRPA, RH5 and RIPR; the complex is formed during
CC merozoite invasion of host erythrocytes specifically at the interface
CC between the parasite and host membranes (PubMed:25583518,
CC PubMed:27374406, PubMed:28186186, PubMed:21909261, PubMed:30542156).
CC Within the complex, interacts with CyRPA (PubMed:28186186,
CC PubMed:30542156). CyRPA recruits RIPR to the RH5-P113-BSG complex; the
CC formation of the PfRH5 adhesion complex increases the affinity of RH5
CC for BSG and probably leads to the release of RH5 from P113 while
CC maintaining the interaction of the PfRH5 adhesion complex with BSG
CC (PubMed:28186186, PubMed:30542156). {ECO:0000269|PubMed:21909261,
CC ECO:0000269|PubMed:22080952, ECO:0000269|PubMed:24297912,
CC ECO:0000269|PubMed:25296023, ECO:0000269|PubMed:25583518,
CC ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:28096331,
CC ECO:0000269|PubMed:28186186, ECO:0000269|PubMed:30542156}.
CC -!- INTERACTION:
CC Q8IFM5; A0A0M5L610: BSG; Xeno; NbExp=3; IntAct=EBI-22304327, EBI-25648504;
CC Q8IFM5; P35613-2: BSG; Xeno; NbExp=3; IntAct=EBI-22304327, EBI-11037868;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19000690,
CC ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:25583518,
CC ECO:0000269|PubMed:28409866}. Cytoplasmic vesicle, secretory vesicle,
CC rhoptry lumen {ECO:0000269|PubMed:19000690,
CC ECO:0000269|PubMed:21909261, ECO:0000269|PubMed:28409866}. Host cell
CC membrane {ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406,
CC ECO:0000269|PubMed:30542156}. Note=In late schizonts, localizes in the
CC rhoptry lumen (PubMed:19000690, PubMed:21909261, PubMed:28409866).
CC During merozoite invasion of host erythrocytes, secreted at the
CC merozoite apical surface where it colocalizes with CyPRA and RIPR at
CC the interface between the merozoite and the erythrocyte
CC (PubMed:19000690, PubMed:21909261, PubMed:25583518, PubMed:27374406).
CC {ECO:0000269|PubMed:19000690, ECO:0000269|PubMed:21909261,
CC ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406,
CC ECO:0000269|PubMed:28409866}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages,
CC specifically at the schizont stage and in free merozoites (at protein
CC level). {ECO:0000269|PubMed:19000690, ECO:0000269|PubMed:21909261,
CC ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406,
CC ECO:0000269|PubMed:28409866}.
CC -!- PTM: Cleaved into a 45kDa form during merozoite invasion of host
CC erythrocyte. {ECO:0000269|PubMed:19000690, ECO:0000269|PubMed:21909261,
CC ECO:0000269|PubMed:28186186, ECO:0000269|PubMed:28409866}.
CC -!- BIOTECHNOLOGY: Potential candidate for the development of parasite
CC blood stage vaccines. In vitro and in vivo, induces neutralizing
CC antibodies capable of inhibiting merozoite invasion of host
CC erythrocytes. {ECO:0000269|PubMed:25296023,
CC ECO:0000269|PubMed:28096331, ECO:0000269|PubMed:28186186,
CC ECO:0000269|PubMed:31204103}.
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DR EMBL; AL844503; CAD49275.1; -; Genomic_DNA.
DR RefSeq; XP_001351544.1; XM_001351508.1.
DR PDB; 4WAT; X-ray; 2.18 A; A=126-526.
DR PDB; 5MI0; X-ray; 2.35 A; A=140-526.
DR PDB; 6MPV; EM; 7.17 A; B=175-504.
DR PDB; 6RCU; X-ray; 4.00 A; A=26-526.
DR PDB; 6RCV; X-ray; 3.58 A; A/F=26-526.
DR PDB; 7PHU; X-ray; 2.53 A; A=26-526.
DR PDBsum; 4WAT; -.
DR PDBsum; 5MI0; -.
DR PDBsum; 6MPV; -.
DR PDBsum; 6RCU; -.
DR PDBsum; 6RCV; -.
DR PDBsum; 7PHU; -.
DR AlphaFoldDB; Q8IFM5; -.
DR SMR; Q8IFM5; -.
DR IntAct; Q8IFM5; 3.
DR STRING; 5833.PFD1145c; -.
DR PRIDE; Q8IFM5; -.
DR ABCD; Q8IFM5; 4 sequenced antibodies.
DR EnsemblProtists; CAD49275; CAD49275; PF3D7_0424100.
DR GeneID; 812437; -.
DR KEGG; pfa:PF3D7_0424100; -.
DR VEuPathDB; PlasmoDB:PF3D7_0424100; -.
DR HOGENOM; CLU_518280_0_0_1; -.
DR InParanoid; Q8IFM5; -.
DR OMA; NHENDFN; -.
DR PhylomeDB; Q8IFM5; -.
DR Proteomes; UP000001450; Chromosome 4.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:GeneDB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0020008; C:rhoptry; IDA:UniProtKB.
DR GO; GO:0034591; C:rhoptry lumen; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:GeneDB.
DR GO; GO:0046789; F:host cell surface receptor binding; IPI:UniProtKB.
DR GO; GO:0044409; P:entry into host; IDA:UniProtKB.
DR InterPro; IPR041668; Rh5_CC.
DR Pfam; PF18515; Rh5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..526
FT /note="Reticulocyte-binding protein homolog 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448483"
FT REGION 33..51
FT /note="Mediates interaction with human BSG"
FT /evidence="ECO:0000269|PubMed:28186186"
FT REGION 259..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 140..141
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:28186186"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25296023,
FT ECO:0007744|PDB:4WAT"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 224..317
FT /evidence="ECO:0000269|PubMed:25296023,
FT ECO:0000269|PubMed:28096331, ECO:0000269|PubMed:30542156,
FT ECO:0000269|PubMed:31204103, ECO:0007744|PDB:4WAT,
FT ECO:0007744|PDB:5MI0, ECO:0007744|PDB:6MPV,
FT ECO:0007744|PDB:6RCU, ECO:0007744|PDB:6RCV"
FT DISULFID 345..351
FT /evidence="ECO:0000269|PubMed:25296023,
FT ECO:0000269|PubMed:28096331, ECO:0000269|PubMed:30542156,
FT ECO:0000269|PubMed:31204103, ECO:0007744|PDB:4WAT,
FT ECO:0007744|PDB:5MI0, ECO:0007744|PDB:6MPV,
FT ECO:0007744|PDB:6RCU, ECO:0007744|PDB:6RCV"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4WAT"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4WAT"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 176..194
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 203..221
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 298..320
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 322..341
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 376..400
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 405..443
FT /evidence="ECO:0007829|PDB:4WAT"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 452..496
FT /evidence="ECO:0007829|PDB:4WAT"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:4WAT"
SQ SEQUENCE 526 AA; 62996 MW; DAC99A6181B78AEB CRC64;
MIRIKKKLIL TIIYIHLFIL NRLSFENAIK KTKNQENNLT LLPIKSTEEE KDDIKNGKDI
KKEIDNDKEN IKTNNAKDHS TYIKSYLNTN VNDGLKYLFI PSHNSFIKKY SVFNQINDGM
LLNEKNDVKN NEDYKNVDYK NVNFLQYHFK ELSNYNIANS IDILQEKEGH LDFVIIPHYT
FLDYYKHLSY NSIYHKSSTY GKCIAVDAFI KKINETYDKV KSKCNDIKND LIATIKKLEH
PYDINNKNDD SYRYDISEEI DDKSEETDDE TEEVEDSIQD TDSNHTPSNK KKNDLMNRTF
KKMMDEYNTK KKKLIKCIKN HENDFNKICM DMKNYGTNLF EQLSCYNNNF CNTNGIRYHY
DEYIHKLILS VKSKNLNKDL SDMTNILQQS ELLLTNLNKK MGSYIYIDTI KFIHKEMKHI
FNRIEYHTKI INDKTKIIQD KIKLNIWRTF QKDELLKRIL DMSNEYSLFI TSDHLRQMLY
NTFYSKEKHL NNIFHHLIYV LQMKFNDVPI KMEYFQTYKK NKPLTQ
