RH1_PLAF7
ID RH1_PLAF7 Reviewed; 2971 AA.
AC P86148; B9ZSJ4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 23-FEB-2022, entry version 42.
DE RecName: Full=Reticulocyte-binding protein homolog 1 {ECO:0000303|PubMed:12228308};
DE Short=PfRH1 {ECO:0000303|PubMed:12228308};
DE AltName: Full=Normocyte-binding protein 1 {ECO:0000303|PubMed:11733572};
DE Short=PfNBP1 {ECO:0000303|PubMed:11733572};
DE Contains:
DE RecName: Full=Reticulocyte-binding protein homolog 1 240 kDa form {ECO:0000305};
DE Contains:
DE RecName: Full=Reticulocyte-binding protein homolog 1 120 kDa form {ECO:0000305};
DE Flags: Precursor;
GN Name=RH1 {ECO:0000303|PubMed:12228308};
GN Synonyms=NBP1 {ECO:0000303|PubMed:11733572};
GN ORFNames=PF3D7_0402300, PFD0110w;
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]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11733572; DOI=10.1084/jem.194.11.1571;
RA Rayner J.C., Vargas-Serrato E., Huber C.S., Galinski M.R., Barnwell J.W.;
RT "A Plasmodium falciparum homologue of Plasmodium vivax reticulocyte binding
RT protein (PvRBP1) defines a trypsin-resistant erythrocyte invasion
RT pathway.";
RL J. Exp. Med. 194:1571-1581(2001).
RN [4]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=3D7 {ECO:0000269|PubMed:12228308},
RC FCB1 {ECO:0000269|PubMed:12228308}, and T996 {ECO:0000269|PubMed:12228308};
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 [5]
RP DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15612925; DOI=10.1111/j.1365-2958.2004.04388.x;
RA Triglia T., Duraisingh M.T., Good R.T., Cowman A.F.;
RT "Reticulocyte-binding protein homologue 1 is required for sialic acid-
RT dependent invasion into human erythrocytes by Plasmodium falciparum.";
RL Mol. Microbiol. 55:162-174(2005).
RN [6]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=17040128; DOI=10.1371/journal.ppat.0020113;
RA Baker R.P., Wijetilaka R., Urban S.;
RT "Two Plasmodium rhomboid proteases preferentially cleave different adhesins
RT implicated in all invasive stages of malaria.";
RL PLoS Pathog. 2:e113-e113(2006).
RN [7] {ECO:0000305}
RP SYNTHESIS OF 758-782; 813-839; 1396-1420; 1814-1840; 1904-1957; 2070-2096;
RP 2208-2232 AND 2359-2383, 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, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=18617995; DOI=10.1371/journal.ppat.1000104;
RA Gao X., Yeo K.P., Aw S.S., Kuss C., Iyer J.K., Genesan S.,
RA Rajamanonmani R., Lescar J., Bozdech Z., Preiser P.R.;
RT "Antibodies targeting the PfRH1 binding domain inhibit invasion of
RT Plasmodium falciparum merozoites.";
RL PLoS Pathog. 4:e1000104-e1000104(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=FCR3 {ECO:0000269|PubMed:19614665}, and
RC W2mef {ECO:0000269|PubMed:19614665};
RX PubMed=19614665; DOI=10.1111/j.1462-5822.2009.01358.x;
RA Triglia T., Tham W.H., Hodder A., Cowman A.F.;
RT "Reticulocyte binding protein homologues are key adhesins during
RT erythrocyte invasion by Plasmodium falciparum.";
RL Cell. Microbiol. 11:1671-1687(2009).
RN [10]
RP FUNCTION, AND BIOTECHNOLOGY.
RC STRAIN=T994 {ECO:0000269|PubMed:24280897};
RX PubMed=24280897; DOI=10.1038/ncomms3862;
RA Gao X., Gunalan K., Yap S.S., Preiser P.R.;
RT "Triggers of key calcium signals during erythrocyte invasion by Plasmodium
RT falciparum.";
RL Nat. Commun. 4:2862-2862(2013).
RN [11]
RP INTERACTION WITH AMA1, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=T994 {ECO:0000269|PubMed:32452132};
RX PubMed=32452132; DOI=10.1111/cmi.13232;
RA Gunalan K., Gao X., Yap S.S.L., Lai S.K., Ravasio A., Ganesan S., Li H.Y.,
RA Preiser P.R.;
RT "A processing product of the Plasmodium falciparum reticulocyte binding
RT protein RH1 shows a close association with AMA1 during junction
RT formation.";
RL Cell. Microbiol. 22:e13232-e13232(2020).
CC -!- FUNCTION: [Reticulocyte-binding protein homolog 1 240 kDa form]: During
CC the asexual blood stage, binds to a sialic acid containing receptor on
CC the surface of the host erythrocyte and thus is involved in merozoite
CC invasion (PubMed:18617995). Binds erythrocytes via a neuraminidase
CC sensitive and trypsin-, chymotrypsin-resistant receptor
CC (PubMed:11733572, PubMed:18617995). After merozoite attachment and
CC reorientation, RH1 binding to its erythrocyte receptor triggers an
CC increase in intracellular Ca(2+) within the parasite resulting in the
CC release of microneme proteins such as EBA175 which in turn leads to the
CC formation of the tight junction between parasite and host cell
CC (PubMed:24280897). {ECO:0000269|PubMed:11733572,
CC ECO:0000269|PubMed:18617995, ECO:0000269|PubMed:24280897}.
CC -!- SUBUNIT: [Reticulocyte-binding protein homolog 1 240 kDa form]: May in
CC part interact with AMA1 in the moving tight junction between the
CC parasite and the erythrocyte membranes; the interaction may facilitate
CC junction formation and active invasion. {ECO:0000269|PubMed:32452132}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 1]: Cell
CC membrane {ECO:0000305|PubMed:12228308}; Single-pass type I membrane
CC protein {ECO:0000305}. Note=Localizes to apical organelles in the
CC maturing schizont and then translocates to the apical surface of the
CC merozoite. {ECO:0000269|PubMed:12228308}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 1 240 kDa
CC form]: Secreted {ECO:0000269|PubMed:19614665}. Cell junction, tight
CC junction {ECO:0000269|PubMed:19614665}. Cytoplasmic vesicle, secretory
CC vesicle, rhoptry {ECO:0000269|PubMed:19614665,
CC ECO:0000269|PubMed:32452132}. Note=Localized to the rhoptry neck at the
CC apical end of the merozoite (PubMed:19614665, PubMed:32452132). During
CC merozoite invasion, mainly localizes to the tight junction formed
CC between the parasite and the host erythrocytes membranes and then moves
CC with the tight junction to the posterior end as the parasite enters the
CC erythrocyte (PubMed:19614665). The remaining protein that does not
CC participate in the tight junction, remains at the apical end of the
CC merozoite and is incorporated into the newly formed ring stage
CC (PubMed:19614665). {ECO:0000269|PubMed:19614665,
CC ECO:0000269|PubMed:32452132}.
CC -!- SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 1 120 kDa
CC form]: Cell membrane {ECO:0000269|PubMed:19614665}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, tight junction
CC {ECO:0000269|PubMed:19614665, ECO:0000269|PubMed:32452132}. Cytoplasmic
CC vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:19614665,
CC ECO:0000269|PubMed:32452132}. Note=Localized to the rhoptry neck at the
CC apical end of the merozoite (PubMed:19614665, PubMed:32452132). During
CC merozoite invasion, mainly localizes to the tight junction formed
CC between the parasite and the host erythrocytes membranes and then moves
CC with the tight junction to the posterior end as the parasite enters the
CC erythrocyte (PubMed:19614665). The remaining protein that does not
CC participate in the tight junction, remains at the apical end of the
CC merozoite and is incorporated into the newly formed ring stage
CC (PubMed:19614665). {ECO:0000269|PubMed:19614665,
CC ECO:0000269|PubMed:32452132}.
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) (PubMed:11733572,
CC PubMed:12228308, PubMed:15612925). Expression levels are low in isolate
CC 3D7 when compared to other isolates (at protein level)
CC (PubMed:12228308, PubMed:15612925, PubMed:18617995).
CC {ECO:0000269|PubMed:11733572, ECO:0000269|PubMed:12228308,
CC ECO:0000269|PubMed:15612925, ECO:0000269|PubMed:18617995}.
CC -!- PTM: Proteolytically processed into multiple fragments following
CC schizont rupture (PubMed:19614665, PubMed:32452132). In the mature
CC schizont stage prior to merozoite release, full length RH1 is processed
CC post-Golgi into a 240 kDa N-terminal form and a 120 kDa C-terminal form
CC containing the transmembrane region (PubMed:12228308, PubMed:15612925,
CC PubMed:19614665, PubMed:32452132). Both forms appear not to form a
CC complex (PubMed:19614665). However, they appear to remain in close
CC proximity in late schizonts (PubMed:32452132). Following merozoite
CC invasion of host erythrocytes, the 240 kDa form is further processed
CC into a 140 kDa form which may be involved in the disengagement of the
CC ligand-receptor complex required during the invasion process
CC (PubMed:19614665, PubMed:32452132). Also, the 120 kDa is further
CC cleaved into a 110 kDa form and a transmembrane 9 kDa form probably by
CC ROM4 (PubMed:17040128, PubMed:19614665, PubMed:32452132).
CC {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:15612925,
CC ECO:0000269|PubMed:17040128, ECO:0000269|PubMed:19614665,
CC ECO:0000269|PubMed:32452132}.
CC -!- DISRUPTION PHENOTYPE: No difference in the ability to invade
CC neuraminidase-, trypsin or chymotrypsin-treated host erythrocytes
CC compared with wild-type. {ECO:0000269|PubMed:15612925}.
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:18617995, PubMed:24280897). However,
CC inhibition efficiency varies across isolates due to the variation in
CC RH1 expression levels and can also be affected by the expression levels
CC of RH2a and/or RH2b, two other erythrocyte binding receptors
CC (PubMed:18617995). Isolates 3D7 or HB3 are insensitive to antibodies
CC against EBD while isolates W2mef, T994, FCR3 and Dd2 are sensitive
CC (PubMed:18617995, PubMed:24280897). {ECO:0000269|PubMed:17653272,
CC ECO:0000269|PubMed:18617995, ECO:0000269|PubMed:24280897}.
CC -!- MISCELLANEOUS: RH1 expression levels greatly vary between isolates in
CC part due to multiple RH1 gene copies; levels are high in isolates
CC W2mef, FCR3, FCB1 and T994, and low in isolates 3D7, HB3, K1, 7G8, T996
CC and Dd2 (PubMed:12228308, PubMed:15612925, PubMed:18617995). A similar
CC variation in expression affects other reticulocyte-binding proteins
CC such as RH2a and RH2b (PubMed:12228308). The expression pattern of RH1
CC and RH2 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:15612925,
CC ECO:0000269|PubMed:18617995, ECO:0000305, ECO:0000305|PubMed:12228308,
CC ECO:0000305|PubMed:15612925}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL844503; CAX51862.2; -; Genomic_DNA.
DR RefSeq; XP_002808637.1; XM_002808591.1.
DR SMR; P86148; -.
DR STRING; 5833.PFD0110w; -.
DR PRIDE; P86148; -.
DR EnsemblProtists; CAX51862; CAX51862; PF3D7_0402300.
DR GeneID; 9221810; -.
DR KEGG; pfa:PF3D7_0402300; -.
DR VEuPathDB; PlasmoDB:PF3D7_0402300; -.
DR HOGENOM; CLU_226794_0_0_1; -.
DR PhylomeDB; P86148; -.
DR Proteomes; UP000001450; Chromosome 4.
DR GO; GO:0020007; C:apical complex; IDA:GeneDB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020008; C:rhoptry; IDA:GeneDB.
DR GO; GO:0008201; F:heparin binding; IDA:GeneDB.
DR GO; GO:0046789; F:host cell surface receptor binding; IDA:GeneDB.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:GeneDB.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cytoplasmic vesicle; Glycoprotein;
KW Leucine-rich repeat; Membrane; Merozoite; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..2971
FT /note="Reticulocyte-binding protein homolog 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000361077"
FT CHAIN 21..?
FT /note="Reticulocyte-binding protein homolog 1 240 kDa form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453520"
FT CHAIN ?..2971
FT /note="Reticulocyte-binding protein homolog 1 120 kDa form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453521"
FT TOPO_DOM 21..2897
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2898..2918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2919..2971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 528..553
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 607..633
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 736..758
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 785..808
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 993..1018
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 1356..1381
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 1466..1489
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 1512..1537
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 1586..1609
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 1611..1636
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 1700..1723
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 1809..1834
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 1880..1903
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 1944..1967
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 2523..2548
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 2731..2754
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..833
FT /note="Erythrocyte binding domain (EBD)"
FT /evidence="ECO:0000269|PubMed:18617995"
FT REGION 2773..2825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2840..2862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2773..2803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2848..2862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2054
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 2971 AA; 357669 MW; CCCC10CDE22F7898 CRC64;
MQRWIFCNIV LHILIYLAEF SHEQESYSSN EKIRKDYSDD NNYEPTPSYE KRKKEYGKDE
SYIKNYRGNN FSYDLSKNSS IFLHMGNGSN SKTLKRCNKK KNIKTNFLRP IEEEKTVLNN
YVYKGVNFLD TIKRNDSSYK FDVYKDTSFL KNREYKELIT MQYDYAYLEA TKEVLYLIPK
DKDYHKFYKN ELEKILFNLK DSLKLLREGY IQSKLEMIRI HSDIDILNEF HQGNIINDNY
FNNEIKKKKE DMEKYIREYN LYIYKYENQL KIKIQKLTNE VSINLNKSTC EKNCYNYILK
LEKYKNIIKD KINKWKDLPE IYIDDKSFSY TFLKDVINNK IDIYKTISSF ISTQKQLYYF
EYIYIMNKNT LNLLSYNIQK TDINSSSKYT YTKSHFLKDN HILLSKYYTA KFIDILNKTY
YYNLYKNKIL LFNKYIIKLR NDLKEYAFKS IQFIQDKIKK HKDELSIENI LQEVNNIYIK
YDTSINEISK YNNLIINTDL QIVQQKLLEI KQKKNDITHK VQLINHIYKN IHDEILNKKN
NEITKIIINN IKDHKKDLQD LLLFIQQIKQ YNILTDHKIT QCNNYYKEII KMKEDINHIH
IYIQPILNNL HTLKQVQNNK IKYEEHIKQI LQKIYDKKES LKKIILLKDE AQLDITLLDD
LIQKQTKKQT QTQTQTQKQT LIQNNETIQL ISGQEDKHES NPFNHIQTYI QQKDTQNKNI
QNLLKSLYNG NINTFIDTIS KYILKQKDIE LTQHVYTDEK INDYLEEIKN EQNKIDKTID
DIKIQETLKQ ITHIVNNIKT IKKDLLKEFI QHLIKYMNER YQNMQQGYNN LTNYINQYEE
ENNNMKQYIT TIRNIQKIYY DNIYAKEKEI RSGQYYKDFI TSRKNIYNIR ENISKNVDMI
KNEEKKKIQN CVDKYNSIKQ YVKMLKNGDT QDENNNNNND IYDKLIVPLD SIKQNIDKYN
TEHNFITFTN KINTHNKKNQ EMMEEFIYAY KRLKILKILN ISLKACEKNN KSINTLNDKT
QELKKIVTHE IDLLQKDILT SQISNKNVLL LNDLLKEIEQ YIIDVHKLKK KSNDLFTYYE
QSKNYFYFKN KKDNFDIQKT INKMNEWLAI KNYINEINKN YQTLYEKKIN VLLHNSKSYV
QYFYDHIINL ILQKKNYLEN TLKTKIQDNE HSLYALQQNE EYQKVKNEKD QNEIKKIKQL
IEKNKNDILT YENNIEQIEQ KNIELKTNAQ NKDDQIVNTL NEVKKKIIYT YEKVDNQISN
VLKNYEEGKV EYDKNVVQNV NDADDTNDID EINDIDEIND IDEINDIDEI NDIDEIKDID
HIKHFDDTKH FDDIYHADDT RDEYHIALSN YIKTELRNIN LQEIKNNIIK IFKEFKSAHK
EIKKESEQIN KEFTKMDVVI NQLRDIDRQM LDLYKELDEK YSEFNKTKIE EINNIRENIN
NVEIWYEKNI IEYFLRHMND QKDKAAKYME NIDTYKNNIE IISKQINPEN YVETLNKSNM
YSYVEKANDL FYKQINNIII NSNQLKNEAF TIDELQNIQK NRKNLLTKKQ QIIQYTNEIE
NIFNEIKNIN NILVLTNYKS ILQDISQNIN HVSIYTEQLH NLYIKLEEEK EQMKTLYHKS
NVLHNQINFN EDAFINNLLI NIEKIKNDIT HIKEKTNIYM IDVNKSKNNA QLYFHNTLRG
NEKIEYLKNL KNSTNQQITL QELKQVQENV EKVKDIYNQT IKYEEEIKKN YHIITDYENK
INDILHNSFI KQINMESSNN KKQTKQIIDI INDKTFEEHI KTSKTKINML KEQSQMKHID
KTLLNEQALK LFVDINSTNN NLDNMLSEIN SIQNNIHTYI QEANKSFDKF KIICDQNVND
LLNKLSLGDL NYMNHLKNLQ NEIRNMNLEK NFMLDKSKKI DEEEKKLDIL KVNISNINNS
LDKLKKYYEE ALFQKVKEKA EIQKENIEKI KQEINTLSDV FKKPFFFIQL NTDSSQHEKD
INNNVETYKN NIDEIYNVFI QSYNLIQKYS SEIFSSTLNY IQTKEIKEKS IKEQNQLNQN
EKEASVLLKN IKINETIKLF KQIKNERQND VHNIKEDYNL LQQYLNYMKN EMEQLKKYKN
DVHMDKNYVE NNNGEKEKLL KETISSYYDK INNINNKLYI YKNKEDTYFN NMIKVSEILN
IIIKKKQQNE QRIVINAEYD SSLINKDEEI KKEINNQIIE LNKHNENISN IFKDIQNIKK
QSQDIITNMN DMYKSTILLV DIIQKKEEAL NKQKNILRNI DNILNKKENI IDKVIKCNCD
DYKDILIQNE TEYQKLQNIN HTYEEKKKSI DILKIKNIKQ KNIQEYKNKL EQMNTIINQS
IEQHVFINAD ILQNEKIKLE EIIKNLDILD EQIMTYHNSI DELYKLGIQC DNHLITTISV
VVNKNTTKIM IHIKKQKEDI QKINNYIQTN YNIINEEALQ FHRLYGHNLI SEDDKNNLVH
IIKEQKNIYT QKEIDISKII KHVKKGLYSL NEHDMNHDTH MNIINEHINN NILQPYTQLI
NMIKDIDNVF IKIQNNKFEQ IQKYIEIIKS LEQLNKNINT DNLNKLKDTQ NKLINIETEM
KHKQKQLINK MNDIEKDNIT DQYMHDVQQN IFEPITLKMN EYNTLLNDNH NNNINNEHQF
NHLNSLHTKI FSHNYNKEQQ QEYITNIMQR IDVFINDLDT YQYEYYFYEW NQEYKQIDKN
KINQHINNIK NNLIHVKKQF EHTLENIKNN ENIFDNIQLK KKDIDDIIIN INNTKETYLK
ELNKKKMLQN KKKVDEKSEI NNHHTLQHDN QNVEQKNKIK DHNLITKPNN NSSEESHQNE
QMKEQNKNIL EKQTRNIKPH HVHNHNHNHN QNQKDSTKLQ EQDISTHKLH NTIHEQQSKD
NHQGNREKKQ KNGNHERMYF ASGIVVSILF LSSLGFVINS KNNKQEYDKE QEKQQQNDFV
CDNNKMDDKS TQKYGRNQEE VMEISFDNDY I
