RH2A_PLAF7
ID RH2A_PLAF7 Reviewed; 3130 AA.
AC Q8IDX6; Q7JU29; Q9BK46;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Reticulocyte-binding protein homolog 2a {ECO:0000303|PubMed:11160005};
DE Short=PfR2Ha {ECO:0000303|PubMed:11160005};
DE Short=PfRH2a {ECO:0000303|PubMed:12228308};
DE Contains:
DE RecName: Full=Reticulocyte-binding protein homolog 2a 85 kDa form {ECO:0000305};
DE Contains:
DE RecName: Full=Reticulocyte-binding protein homolog 2a 285 kDa form {ECO:0000305};
DE Flags: Precursor;
GN Name=RH2a {ECO:0000303|PubMed:12228308}; ORFNames=PF13_0198, PF3D7_1335400;
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:AAK19244.1}
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:AAN39443.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|EMBL:AAN39443.1};
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]
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 [4] {ECO:0000312|EMBL:CAD52492.1}
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 [5]
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 [6]
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 [7] {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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=21628513; DOI=10.1128/iai.00201-11;
RA Gunalan K., Gao X., Liew K.J., Preiser P.R.;
RT "Differences in erythrocyte receptor specificity of different parts of the
RT Plasmodium falciparum reticulocyte binding protein homologue 2a.";
RL Infect. Immun. 79:3421-3430(2011).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP 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).
CC -!- FUNCTION: [Reticulocyte-binding protein homolog 2a]: During the asexual
CC blood stage, binds to a chymotrypsin sensitive, neuraminidase and
CC trypsin resistant receptor on the surface of the host erythrocyte
CC (PubMed:21628513). Despite its binding capacity, appears to be
CC dispensable for merozoite invasion of host erythrocytes
CC (PubMed:12606570, PubMed:21698217). {ECO:0000269|PubMed:12606570,
CC ECO:0000269|PubMed:21628513, ECO:0000269|PubMed:21698217}.
CC -!- FUNCTION: [Reticulocyte-binding protein homolog 2a 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. {ECO:0000269|PubMed:21698217}.
CC -!- SUBUNIT: Forms a heterodimer composed of the 285 kDa and the 85 kDa
CC forms. {ECO:0000269|PubMed:21698217}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21628513,
CC ECO:0000269|PubMed:21698217}; Single-pass type I membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry
CC {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21628513}. Secreted
CC {ECO:0000269|PubMed:21628513}. Cell junction, tight junction
CC {ECO:0000269|PubMed:21628513}. Note=Localizes to the rhoptry neck at
CC the apical end of the merozoite (PubMed:21628513, PubMed:12228308).
CC During merozoite invasion, mainly localizes to the tight junction
CC formed between the parasite and the host erythrocyte membranes and then
CC moves with the tight junction to the posterior end as the parasite
CC enters the erythrocyte (PubMed:21628513). Also, the different processed
CC forms are released from the membrane following proteolytic cleavage
CC (PubMed:21628513). {ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:21628513}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2a 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 285 kDa form. During merozoite invasion,
CC shed from the cell surface. {ECO:0000269|PubMed:21698217}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2a 285 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:21628513,
CC ECO:0000269|PubMed:21698217}.
CC -!- PTM: Proteolytically processed into multiple fragments following
CC schizont rupture (PubMed:21628513, 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 285 kDa and N-terminal 85
CC kDa forms (PubMed:21628513, PubMed:21698217). During merozoite invasion
CC of host erythrocytes, further processing occurs generating a 140 kDa C-
CC terminal form (PubMed:21628513). At the same time, the C-terminal
CC transmembrane region is probably cleaved, probably by a rhomboid
CC protease, to shed all the different processed protein forms from the
CC membrane leaving a transmembrane 7 kDa form on the merozoite surface
CC (PubMed:21628513, PubMed:21698217). {ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:21628513, ECO:0000269|PubMed:21698217}.
CC -!- DISRUPTION PHENOTYPE: Does not affect merozoite invasion of host
CC erythrocytes, either untreated or treated with neuraminidase, trypsin
CC or chymotrypsin. {ECO:0000269|PubMed:12606570}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera. {ECO:0000269|PubMed:17653272}.
CC -!- MISCELLANEOUS: RH2a expression levels greatly vary between isolates;
CC levels are high in isolates 3D7, T996, HB3, D10, 7G8, K1, Pf120 and
CC W2mef, and undetectable in isolates MCAMP, FCB1, T994 and FCR3
CC (PubMed:12228308, PubMed:12606570). A similar variation in expression
CC affects other reticulocyte-binding proteins such as RH2b and RH1
CC (PubMed:12228308, PubMed:12606570). The expression pattern of RH1, RH2a
CC and RH2b allows the strain to use different invasion pathways to enter
CC erythrocytes (Probable). This provides a mechanism of phenotypic
CC variation to evade host immune responses and to adapt to the
CC polymorphic nature of the erythrocyte receptors in human populations
CC (Probable). {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:12606570,
CC ECO:0000305, ECO:0000305|PubMed:12606570}.
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DR EMBL; AF312916; AAK19244.1; -; Genomic_DNA.
DR EMBL; AY138496; AAN39443.1; -; Genomic_DNA.
DR EMBL; AL844509; CAD52492.1; -; Genomic_DNA.
DR RefSeq; XP_001350083.1; XM_001350047.1.
DR SMR; Q8IDX6; -.
DR BioGRID; 1209422; 13.
DR IntAct; Q8IDX6; 14.
DR STRING; 5833.PF13_0198; -.
DR PRIDE; Q8IDX6; -.
DR EnsemblProtists; CAD52492; CAD52492; PF3D7_1335400.
DR GeneID; 814167; -.
DR KEGG; pfa:PF3D7_1335400; -.
DR VEuPathDB; PlasmoDB:PF3D7_1335400; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000438000; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130039700; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130039800; -.
DR VEuPathDB; PlasmoDB:PfCD01_130041000; -.
DR VEuPathDB; PlasmoDB:PfDd2_130041200; -.
DR VEuPathDB; PlasmoDB:PfGA01_130041500; -.
DR VEuPathDB; PlasmoDB:PfGB4_130041200; -.
DR VEuPathDB; PlasmoDB:PfGB4_130041300; -.
DR VEuPathDB; PlasmoDB:PfGN01_130042100; -.
DR VEuPathDB; PlasmoDB:PfHB3_130041600; -.
DR VEuPathDB; PlasmoDB:PfHB3_130041700; -.
DR VEuPathDB; PlasmoDB:PfIT_130040700; -.
DR VEuPathDB; PlasmoDB:PfKE01_130040900; -.
DR VEuPathDB; PlasmoDB:PfKH01_130039400; -.
DR VEuPathDB; PlasmoDB:PfKH02_130038200; -.
DR VEuPathDB; PlasmoDB:PfKH02_130038300; -.
DR VEuPathDB; PlasmoDB:PfNF135_130039900; -.
DR VEuPathDB; PlasmoDB:PfNF166_130040500; -.
DR VEuPathDB; PlasmoDB:PfNF54_130040300; -.
DR VEuPathDB; PlasmoDB:PfSD01_130042000; -.
DR VEuPathDB; PlasmoDB:PfSN01_130038400; -.
DR VEuPathDB; PlasmoDB:PfTG01_130041000; -.
DR VEuPathDB; PlasmoDB:PfTG01_130041100; -.
DR HOGENOM; CLU_225324_0_0_1; -.
DR InParanoid; Q8IDX6; -.
DR OMA; LMCENAN; -.
DR PhylomeDB; Q8IDX6; -.
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; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:1990225; C:rhoptry neck; 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:0098609; P:cell-cell adhesion; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Glycoprotein; Leucine-rich repeat; Membrane; Merozoite; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Tight junction;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..3130
FT /note="Reticulocyte-binding protein homolog 2a"
FT /evidence="ECO:0000255"
FT /id="PRO_0000371501"
FT CHAIN 25..?
FT /note="Reticulocyte-binding protein homolog 2a 85 kDa form"
FT /evidence="ECO:0000269|PubMed:21698217"
FT /id="PRO_0000453540"
FT CHAIN ?..3130
FT /note="Reticulocyte-binding protein homolog 2a 285 kDa
FT form"
FT /evidence="ECO:0000269|PubMed:21698217"
FT /id="PRO_0000453541"
FT TOPO_DOM 25..3066
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 3067..3087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3088..3130
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..2545
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 2915..2936
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 2937..2959
FT /note="LRR 24"
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..2753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3021..3056
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..2874
FT /evidence="ECO:0000255"
FT COMPBIAS 3021..3038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3039..3056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 2940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3056
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3062
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 1766
FT /note="I -> L (in Ref. 1; AAK19244)"
FT /evidence="ECO:0000305"
FT CONFLICT 3029
FT /note="E -> D (in Ref. 1; AAK19244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3130 AA; 370436 MW; 87323A119F5DE8E6 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 RISNTAAYTN ITLQDIENNK NKENNNMNIE TIDKLIDHIK
IHNEKIQAEI LIIDDAKRKV KEITDNINKA FNEITENYNN ENNGVIKSAK NIVDEATYLN
NELDKFLLKL NELLSHNNND IKDLGDEKLI LKEEEERKER ERLEKAKQEE ERKERERIEK
EKQEKERLER EKQEQLKKEE ELRKKEQERQ EQQQKEEALK RQEQERLQKE EELKRQEQER
LEREKQEQLQ KEEELKRQEQ ERLQKEEALK RQEQERLQKE EELKRQEQER LEREKQEQLQ
KEEELKRQEQ ERLQKEEALK RQEQERLQKE EELKRQEQER LERKKIELAE REQHIKSKLE
SDMVKIIKDE LTKEKDEIIK NKDIKLRHSL EQKWLKHLQN ILSLKIDSLL NKNDEVIKDN
ETQLKTNILN SLKNQLYLNL KRELNEIIKE YEENQKKILH SNQLVNDSLE QKTNRLVDIK
PTKHGDIYTN KLSDNETEML ITSKEKKDET ESTKRSGTDH TNSSESTTDD NTNDRNFSRS
KNLSVAIYTA GSVALCVLIF SSIGLLLIKT NSGDNNSNEI NEAFEPNDDV LFKEKDEIIE
ITFNDNDSTI
