RH2B_PLAF7
ID RH2B_PLAF7 Reviewed; 3254 AA.
AC C0H5F4; Q7YWE9; Q9BK45;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Reticulocyte-binding protein homolog 2b {ECO:0000303|PubMed:12228308};
DE Short=PfR2Hb {ECO:0000303|PubMed:11160005};
DE Short=PfRH2b {ECO:0000303|PubMed:12228308};
DE Contains:
DE RecName: Full=Reticulocyte-binding protein homolog 2b 85 kDa form {ECO:0000305};
DE Contains:
DE RecName: Full=Reticulocyte-binding protein homolog 2b 297 kDa form {ECO:0000305};
DE Flags: Precursor;
GN Name=RH2b {ECO:0000303|PubMed:12228308};
GN ORFNames=MAL13P1.176, PF3D7_1335300;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1] {ECO:0000312|EMBL:AAK19245.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11160005; DOI=10.1128/iai.69.2.1084-1092.2001;
RA Triglia T., Thompson J., Caruana S.R., Delorenzi M., Speed T., Cowman A.F.;
RT "Identification of proteins from Plasmodium falciparum that are homologous
RT to reticulocyte binding proteins in Plasmodium vivax.";
RL Infect. Immun. 69:1084-1092(2001).
RN [2] {ECO:0000312|EMBL:AAN39447.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|EMBL:AAN39447.1};
RX PubMed=15964948; DOI=10.4269/ajtmh.2005.72.666;
RA Rayner J.C., Tran T.M., Corredor V., Huber C.S., Barnwell J.W.,
RA Galinski M.R.;
RT "Dramatic difference in diversity between Plasmodium falciparum and
RT Plasmodium vivax reticulocyte binding-like genes.";
RL Am. J. Trop. Med. Hyg. 72:666-674(2005).
RN [3] {ECO:0000312|EMBL:AAG02259.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Matesanz F., Alcina A.;
RT "A novel large antigen from Plasmodium falciparum encoding a reticulocyte
RT binding protein analog.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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 [5] {ECO:0000312|EMBL:CAX64332.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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 [6]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=12228308; DOI=10.1128/iai.70.10.5779-5789.2002;
RA Taylor H.M., Grainger M., Holder A.A.;
RT "Variation in the expression of a Plasmodium falciparum protein family
RT implicated in erythrocyte invasion.";
RL Infect. Immun. 70:5779-5789(2002).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12606570; DOI=10.1093/emboj/cdg096;
RA Duraisingh M.T., Triglia T., Ralph S.A., Rayner J.C., Barnwell J.W.,
RA McFadden G.I., Cowman A.F.;
RT "Phenotypic variation of Plasmodium falciparum merozoite proteins directs
RT receptor targeting for invasion of human erythrocytes.";
RL EMBO J. 22:1047-1057(2003).
RN [8] {ECO:0000305}
RP SYNTHESIS OF 2144-2180, AND POSSIBLE CANDIDATE MALARIA EPITOPE.
RX PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT "Rapid identification of malaria vaccine candidates based on alpha-helical
RT coiled coil protein motif.";
RL PLoS ONE 2:E645-E645(2007).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP BIOTECHNOLOGY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=21698217; DOI=10.1371/journal.ppat.1002075;
RA Triglia T., Chen L., Lopaticki S., Dekiwadia C., Riglar D.T., Hodder A.N.,
RA Ralph S.A., Baum J., Cowman A.F.;
RT "Plasmodium falciparum merozoite invasion is inhibited by antibodies that
RT target the PfRh2a and b binding domains.";
RL PLoS Pathog. 7:e1002075-e1002075(2011).
RN [10]
RP INTERACTION WITH FBPA, AND MOTIF.
RX PubMed=22991428; DOI=10.1128/mbio.00292-12;
RA Pal-Bhowmick I., Andersen J., Srinivasan P., Narum D.L., Bosch J.,
RA Miller L.H.;
RT "Binding of aldolase and glyceraldehyde-3-phosphate dehydrogenase to the
RT cytoplasmic tails of Plasmodium falciparum merozoite duffy binding-like and
RT reticulocyte homology ligands.";
RL MBio 3:0-0(2012).
RN [11]
RP PHOSPHORYLATION AT SER-3233.
RX PubMed=23544851; DOI=10.1042/bj20121694;
RA Engelberg K., Paul A.S., Prinz B., Kono M., Ching W., Heincke D.,
RA Dobner T., Spielmann T., Duraisingh M.T., Gilberger T.W.;
RT "Specific phosphorylation of the PfRh2b invasion ligand of Plasmodium
RT falciparum.";
RL Biochem. J. 452:457-466(2013).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, BIOTECHNOLOGY, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=27438226; DOI=10.1111/mmi.13468;
RA Aniweh Y., Gao X., Gunalan K., Preiser P.R.;
RT "PfRH2b specific monoclonal antibodies inhibit merozoite invasion.";
RL Mol. Microbiol. 102:386-404(2016).
CC -!- FUNCTION: [Reticulocyte-binding protein homolog 2b]: During the asexual
CC blood stage, binds to a chymotrypsin sensitive, neuraminidase and
CC trypsin resistant receptor on the surface of the host erythrocyte and
CC thus is involved in merozoite invasion (PubMed:27438226,
CC PubMed:12606570). The various processed forms have different binding
CC affinities for the erythrocyte receptor; full length form binds with
CC higher affinity followed by the 250 kDa form and finally the 300 kDa
CC form while the 160 kDa form does not bind erythrocytes
CC (PubMed:27438226). After merozoite attachment and reorientation, RH2b
CC binding to its erythrocyte receptor triggers an increase in
CC intracellular Ca(2+) within the parasite resulting in the release of
CC microneme proteins such as EBA175 which in turn leads to the formation
CC of the tight junction between parasite and host cell (PubMed:27438226).
CC {ECO:0000269|PubMed:12606570, ECO:0000269|PubMed:27438226}.
CC -!- FUNCTION: [Reticulocyte-binding protein homolog 2b 85 kDa form]: During
CC the asexual blood stage, binds to a trypsin-resistant and chymotrypsin
CC and neuraminidase sensitive receptor on the surface of the host
CC erythrocyte and thus is involved in merozoite invasion.
CC {ECO:0000269|PubMed:21698217}.
CC -!- SUBUNIT: Forms a heterodimer composed of the 297 kDa and the 85 kDa
CC forms (PubMed:21698217). Interacts (via YF motif) with aldolase FBPA
CC (PubMed:22991428). {ECO:0000269|PubMed:21698217,
CC ECO:0000269|PubMed:22991428}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27438226};
CC Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle,
CC secretory vesicle, rhoptry {ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:27438226}. Cell junction, tight junction
CC {ECO:0000269|PubMed:27438226}. Secreted {ECO:0000269|PubMed:27438226}.
CC Note=Localizes to the rhoptry neck at the apical end of the merozoite
CC (PubMed:27438226, PubMed:12228308). During merozoite invasion, mainly
CC localizes to the tight junction formed between the parasite and the
CC host erythrocyte membranes and then moves with the tight junction to
CC the posterior end as the parasite enters the erythrocyte
CC (PubMed:27438226). Also, the different processed forms are released
CC from the membrane following proteolytic cleavage (PubMed:27438226). The
CC remaining 7 kDa processed transmembrane fragment is incorporated into
CC the newly formed ring stage (PubMed:21698217).
CC {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21698217,
CC ECO:0000269|PubMed:27438226}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2b 85 kDa
CC form]: Secreted {ECO:0000269|PubMed:21698217}. Cell membrane
CC {ECO:0000269|PubMed:21698217}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21698217}; Extracellular side
CC {ECO:0000269|PubMed:21698217}. Note=In mature schizont, co-localizes to
CC the apical end of the schizont and the merozoite with reticulocyte-
CC binding protein homolog 2b 297 kDa form. During merozoite invasion,
CC shed from the cell surface. {ECO:0000269|PubMed:21698217}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2b 297 kDa
CC form]: Secreted {ECO:0000269|PubMed:21698217}. Cell membrane
CC {ECO:0000269|PubMed:21698217}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=In mature schizont, co-localizes to the apical end
CC of the schizont and the merozoite with reticulocyte-binding protein
CC homolog 2b 85 kDa form. During merozoite invasion, shed from the cell
CC surface. {ECO:0000269|PubMed:21698217}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages,
CC specifically at the late schizont stage prior to merozoite release and
CC in free merozoites (at protein level). {ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:12606570, ECO:0000269|PubMed:21698217,
CC ECO:0000269|PubMed:27438226}.
CC -!- PTM: Proteolytically processed into multiple fragments following
CC schizont rupture (PubMed:27438226, PubMed:12228308, PubMed:21698217).
CC In the mature schizont stage prior to merozoite release, full length
CC RH2b is processed post-Golgi into C-terminal 297 kDa and N-terminal 85
CC kDa forms (PubMed:21698217, PubMed:27438226). Alternatively, full
CC length RH2b can also be processed into C-terminal 250 kDa and N-
CC terminal 130 kDa forms (PubMed:27438226). During merozoite invasion of
CC host erythrocytes, further processing occurs generating a 160 kDa form
CC (PubMed:27438226). At the same time, the C-terminal transmembrane
CC region is cleaved, probably by a rhomboid protease, to shed all the
CC different processed protein forms from the membrane leaving a
CC transmembrane 7 kDa form on the merozoite surface (PubMed:27438226,
CC PubMed:21698217). {ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:21698217, ECO:0000269|PubMed:27438226}.
CC -!- PTM: Phosphorylated at Ser-3233 by CK2alpha in schizonts.
CC {ECO:0000269|PubMed:23544851}.
CC -!- DISRUPTION PHENOTYPE: Does not affect merozoite invasion of host
CC erythrocytes (PubMed:12606570). However, merozoites invade either
CC neuraminidase- or trypsin-treated erythrocytes at a significantly lower
CC efficiency than the wild-type (PubMed:12606570). Invasion of
CC erythrocytes treated with both neuraminidase and trypsin is further
CC impaired (PubMed:12606570). {ECO:0000269|PubMed:12606570}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera (PubMed:17653272). Antibodies
CC against the erythrocyte binding domain (EBD) prevent merozoite invasion
CC of host erythrocytes (PubMed:21698217, PubMed:27438226). However,
CC inhibition efficiency varies across isolates due to the variation in
CC RH2b expression levels and can also be affected by the expression
CC levels of RH1, another erythrocyte binding receptor (PubMed:21698217).
CC {ECO:0000269|PubMed:17653272, ECO:0000269|PubMed:21698217,
CC ECO:0000269|PubMed:27438226}.
CC -!- MISCELLANEOUS: RH2b expression levels greatly vary between isolates;
CC levels are high in isolates 3D7, K1, 7G8, Pf120 and W2mef, low in
CC isolates HB3 and T996, and undetectable in isolates MCAMP, FCB1, T994
CC and FCR3 (PubMed:12606570, PubMed:12228308). RH2b gene is missing in
CC isolate D10 (PubMed:11160005). A similar variation in expression
CC affects other reticulocyte-binding proteins such as RH2a and RH1
CC (PubMed:12228308). The expression pattern of RH1, RH2a and RH2b allows
CC the strain to use different invasion pathways to enter erythrocytes
CC (Probable). This provides a mechanism of phenotypic variation to evade
CC host immune responses and to adapt to the polymorphic nature of the
CC erythrocyte receptors in human populations (Probable).
CC {ECO:0000269|PubMed:11160005, ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:12606570, ECO:0000305, ECO:0000305|PubMed:12606570}.
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DR EMBL; AF312917; AAK19245.1; -; Genomic_DNA.
DR EMBL; AY138500; AAN39447.1; -; Genomic_DNA.
DR EMBL; AY005149; AAG02259.1; -; Genomic_DNA.
DR EMBL; AL844509; CAX64332.2; -; Genomic_DNA.
DR RefSeq; XP_002809051.1; XM_002809005.1.
DR SMR; C0H5F4; -.
DR BioGRID; 1209000; 1.
DR STRING; 5833.MAL13P1.176; -.
DR PRIDE; C0H5F4; -.
DR EnsemblProtists; CAX64332; CAX64332; PF3D7_1335300.
DR VEuPathDB; PlasmoDB:PF3D7_1335300; -.
DR VEuPathDB; PlasmoDB:PF3D7_1335400; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000438000; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130039700; -.
DR VEuPathDB; PlasmoDB:PfCD01_130040900; -.
DR VEuPathDB; PlasmoDB:PfCD01_130041000; -.
DR VEuPathDB; PlasmoDB:PfDd2_130041200; -.
DR VEuPathDB; PlasmoDB:PfGA01_130041400; -.
DR VEuPathDB; PlasmoDB:PfGA01_130041500; -.
DR VEuPathDB; PlasmoDB:PfGB4_130041200; -.
DR VEuPathDB; PlasmoDB:PfGN01_130042100; -.
DR VEuPathDB; PlasmoDB:PfHB3_130041600; -.
DR VEuPathDB; PlasmoDB:PfIT_130040700; -.
DR VEuPathDB; PlasmoDB:PfKE01_130040900; -.
DR VEuPathDB; PlasmoDB:PfKH01_130039400; -.
DR VEuPathDB; PlasmoDB:PfKH02_130038200; -.
DR VEuPathDB; PlasmoDB:PfNF135_130039900; -.
DR VEuPathDB; PlasmoDB:PfNF166_130040500; -.
DR VEuPathDB; PlasmoDB:PfNF54_130040300; -.
DR VEuPathDB; PlasmoDB:PfSD01_130042000; -.
DR VEuPathDB; PlasmoDB:PfSN01_130038300; -.
DR VEuPathDB; PlasmoDB:PfSN01_130038400; -.
DR VEuPathDB; PlasmoDB:PfTG01_130041000; -.
DR HOGENOM; CLU_225324_0_0_1; -.
DR InParanoid; C0H5F4; -.
DR PhylomeDB; C0H5F4; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0044647; C:host-symbiont bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0020008; C:rhoptry; IDA:GeneDB.
DR GO; GO:1990225; C:rhoptry neck; IDA:UniProtKB.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:GeneDB.
DR GO; GO:0046789; F:host cell surface receptor binding; IMP:UniProtKB.
DR GO; GO:0044650; P:adhesion of symbiont to host cell; IDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0044409; P:entry into host; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Glycoprotein; Leucine-rich repeat; Membrane; Merozoite; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..3254
FT /note="Reticulocyte-binding protein homolog 2b"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399036"
FT CHAIN 25..?
FT /note="Reticulocyte-binding protein homolog 2b 85 kDa form"
FT /evidence="ECO:0000269|PubMed:21698217"
FT /id="PRO_0000453542"
FT CHAIN ?..3254
FT /note="Reticulocyte-binding protein homolog 2b 297 kDa
FT form"
FT /evidence="ECO:0000269|PubMed:21698217"
FT /id="PRO_0000453543"
FT TOPO_DOM 25..3187
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3188..3208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3209..3254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 182..206
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 300..323
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 419..443
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 659..683
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 757..778
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 801..824
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 1116..1139
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 1305..1328
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 1336..1362
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 1438..1461
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 1536..1561
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 1628..1652
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 1795..1818
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 1890..1913
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 2014..2041
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 2052..2076
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 2126..2152
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 2345..2368
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 2409..2434
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 2522..2550
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 2572..2599
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 2650..2671
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 3105..3128
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REGION 446..557
FT /note="Erythrocyte binding domain (EBD)"
FT /evidence="ECO:0000269|PubMed:21698217"
FT REGION 1173..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2680..2874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2909..2969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2991..3018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3035..3097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..517
FT /evidence="ECO:0000255"
FT COILED 1805..1842
FT /evidence="ECO:0000255"
FT COILED 2661..2794
FT /evidence="ECO:0000255"
FT MOTIF 3253..3254
FT /note="Mediates the interaction with FBPA"
FT /evidence="ECO:0000269|PubMed:22991428"
FT COMPBIAS 2680..2815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2817..2842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2855..2874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2909..2957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3046..3067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3068..3091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3233
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:23544851"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1971
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 3254 AA; 382883 MW; 6F9CAFA5AA6167BA CRC64;
MKTTLFCSIS FCNIIFFFLE LSHEHFVGQS SNTHGASSVT DFNFSEEKNL KSFEGKNNNN
DNYASINRLY RKKPYMKRSL INLENDLFRL EPISYIQRYY KKNINRSDIF HNKKERGSKV
YSNVSSFHSF IQEGKEEVEV FSIWGSNSVL DHIDVLRDNG TVVFSVQPYY LDIYTCKEAI
LFTTSFYKDL DKSSITKINE DIEKFNEEII KNEEQCLVGG KTDFDNLLIV LENAEKANVR
KTLFDNTFND YKNKKSSFYN CLKNKKNDYD KKIKNIKNEI TKLLKNIEST GNMCKTESYV
MNNNLYLLRV NEVKSTPIDL YLNRAKELLE SSSKLVNPIK MKLGDNKNMY SIGYIHDEIK
DIIKRYNFHL KHIEKGKEYI KRITQANNIA DKMKKDELIK KIFESSKHFA SFKYSNEMIS
KLDSLFIKNE EILNNLFNNI FNIFKKKYET YVDMKTIESK YTTVMTLSEH LLEYAMDVLK
ANPQKPIDPK ANLDSEVVKL QIKINEKSNE LDNAISQVKT LIIIMKSFYD IIISEKASMD
EMEKKELSLN NYIEKTDYIL QTYNIFKSKS NIINNNSKNI SSKYITIEGL KNDIDELNSL
ISYFKDSQET LIKDDELKKN MKTDYLNNVK YIEENVTHIN EIILLKDSIT QRIADIDELN
SLNLININDF INEKNISQEK VSYNLNKLYK GSFEELESEL SHFLDTKYLF HEKKSVNELQ
TILNTSNNEC AKLNFMKSDN NNNNNNSNII NLLKTELSHL LSLKENIIKK LLNHIEQNIQ
NSSNKYTITY TDINNRMEDY KEEIESLEVY KHTIGNIQKE YILHLYENDK NALAVHNTSM
QILQYKDAIQ NIKNKISDDI KILKKYKEMN QDLLNYYEIL DKKLKDNTYI KEMHTASLVQ
ITQYIPYEDK TISELEQEFN NNNQKLDNIL QDINAMNLNI NILQTLNIGI NACNTNNKNV
EHLLNKKIEL KNILNDQMKI IKNDDIIQDN EKENFSNVLK KEEEKLEKEL DDIKFNNLKM
DIHKLLNSYD HTKQNIESNL KINLDSFEKE KDSWVHFKST IDSLYVEYNI CNQKTHNTIK
QQKNDIIELI YKRIKDINQE IIEKVDNYYS LSDKALTKLK SIHFNIDKEK YKNPKSQENI
KLLEDRVMIL EKKIKEDKDA LIQIKNLSHD HFVNADNEKK KQKEKEEDDE QTHYSKKRKV
MGDIYKDIKK NLDELNNKNL IDITLNEANK IESEYEKILI DDICEQITNE AKKSDTIKEK
IESYKKDIDY VDVDVSKTRN DHHLNGDKIH DSFFYEDTLN YKAYFDKLKD LYENINKLTN
ESNGLKSDAH NNNTQVDKLK EINLQVFSNL GNIIKYVEKL ENTLHELKDM YEFLETIDIN
KILKSIHNSM KKSEEYSNET KKIFEQSVNI TNQFIEDVEI LKTSINPNYE SLNDDQIDDN
IKSLVLKKEE ISEKRKQVNK YITDIESNKE QSDLHLRYAS RSIYVIDLFI KHEIINPSDG
KNFDIIKVKE MINKTKQVSN EAMEYANKMD EKNKDIIKIE NELYNLINNN IRSLKGVKYE
KVRKQARNAI DDINNIHSNI KTILTKSKER LDEIKKQPNI KREGDVLNND KTKIAYITIQ
INNGRIESNL LNILNMKHNI DTILNKAMDY MNDVSKSDQI VINIDSLNMN DIYNKDKDLL
INILKEKQNM EAEYKKMNEM YNYVNETEKE IIKHKKNYEI RIMEHIKKET NEKKKKFMES
NNKSLTTLMD SFRSMFYNEY INDYNINENF EKHQNILNEI YNGFNESYNI INTKMTEIIN
DNLDYNEIKE IKEVAQTEYD KLNKKVDELK NYLNNIKEQE GHRLIDYIKE KIFNLYIKCS
EQQNIIDDSY NYITVKKQYI KTIEDVKFLL DSLNTIEEKN KSVANLEICT NKEDIKNLLK
HVIKLANFSG IIVMSDTNTE ITPENPLEDN DLLNLQLYFE RKHEITSTLE NDSDLELDHL
GSNSDESIDN LKVYNDIIEL HTYSTQILKY LDNIQKLKGD CNDLVKDCKE LRELSTALYD
LKIQITSVIN RENDISNNID IVSNKLNEID AIQYNFEKYK EIFDNVEEYK TLDDTKNAYI
VKKAEILKNV DINKTKEDLD IYFNDLDELE KSLTLSSNEM EIKTIVQNSY NSFSDINKNI
NDIDKEMKTL IPMLDELLNE GHNIDISLYN FIIRNIQIKI GNDIKNIREQ ENDTNICFEY
IQNNYNFIKS DISIFNKYDD HIKVDNYISN NIDVVNKHNS LLSEHVINAT NIIENIMTSI
VEINEDTEMN SLEETQDKLL ELYENFKKEK NIINNNYKIV HFNKLKEIEN SLETYNSIST
NFNKINETQN IDILKNEFNN IKTKINDKVK ELVHVDSTLT LESIQTFNNL YGDLMSNIQD
VYKYEDINNV ELKKVKLYIE NITNLLGRIN TFIKELDKYQ DENNGIDKYI EINKENNSYI
IKLKEKANNL KENFSKLLQN IKRNETELYN INNIKDDIMN TGKSVNNIKQ KFSSNLPLKE
KLFQMEEMLL NINNIMNETK RISNTDAYTN ITLQDIENNK NKENNNMNIE TIDKLIDHIK
IHNEKIQAEI LIIDDAKRKV KEITDNINKA FNEITENYNN ENNGVIKSAK NIVDKATYLN
NELDKFLLKL NELLSHNNND IKDLGDEKLI LKEEEERKER ERLEKAKQEE ERKERERIEK
EKQEKERLER EKQEQLKKEA LKKQEQERQE QQQKEEALKR QEQERLQKEE ELKRQEQERL
EREKQEQLQK EEELRKKEQE KQQQRNIQEL EEQKKPEIIN EALVKGDKIL EGSDQRNMEL
SKPNVSMDNT NNSPISNSEI TESDDIDNSE NIHTSHMSDI ESTQTSHRSN THGQQISDIV
EDQITHPSNI GGEKITHNDE ISITGERNNI SDVNDYSESS NIFENGDSTI NTSTRNTSST
HDESHISPIS NAYDHVVSDN KKSMDENIKD KLKIDESITT DEQIRLDDNS NIVRIDSTDQ
RDASSHGSSN RDDDEISHVG SDIHMDSVDI HDSIDTDENA DHRHNVNSVD SLSSSDYTDT
QKDFSSIIKD GGNKEGHAEN ESKEYESQTE QTHEEGIMNP NKYSISEVDG IKLNEEAKHK
ITEKLVDIYP STYRTLDEPM ETHGPNEKFH MFGSPYVTEE DYTEKHDYDK HEDFNNERYS
NHNKMDDFVY NAGGVVCCVL FFASITFFSM DRSNKDECDF DMCEEVNNND HLSNYADKEE
IIEIVFDENE EKYF
