| IED ID | IndEnz0002008715 |
| Enzyme Type ID | protease008715 |
| Protein Name |
Reticulocyte-binding protein homolog 2a PfR2Ha PfRH2a Cleaved into: Reticulocyte-binding protein homolog 2a 85 kDa form; Reticulocyte-binding protein homolog 2a 285 kDa form |
| Gene Name | RH2a PF13_0198 PF3D7_1335400 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MKTTLFCSISFCNIIFFFLELSHEHFVGQSSNTHGASSVTDFNFSEEKNLKSFEGKNNNNDNYASINRLYRKKPYMKRSLINLENDLFRLEPISYIQRYYKKNINRSDIFHNKKERGSKVYSNVSSFHSFIQEGKEEVEVFSIWGSNSVLDHIDVLRDNGTVVFSVQPYYLDIYTCKEAILFTTSFYKDLDKSSITKINEDIEKFNEEIIKNEEQCLVGGKTDFDNLLIVLENAEKANVRKTLFDNTFNDYKNKKSSFYNCLKNKKNDYDKKIKNIKNEITKLLKNIESTGNMCKTESYVMNNNLYLLRVNEVKSTPIDLYLNRAKELLESSSKLVNPIKMKLGDNKNMYSIGYIHDEIKDIIKRYNFHLKHIEKGKEYIKRITQANNIADKMKKDELIKKIFESSKHFASFKYSNEMISKLDSLFIKNEEILNNLFNNIFNIFKKKYETYVDMKTIESKYTTVMTLSEHLLEYAMDVLKANPQKPIDPKANLDSEVVKLQIKINEKSNELDNAISQVKTLIIIMKSFYDIIISEKASMDEMEKKELSLNNYIEKTDYILQTYNIFKSKSNIINNNSKNISSKYITIEGLKNDIDELNSLISYFKDSQETLIKDDELKKNMKTDYLNNVKYIEENVTHINEIILLKDSITQRIADIDELNSLNLININDFINEKNISQEKVSYNLNKLYKGSFEELESELSHFLDTKYLFHEKKSVNELQTILNTSNNECAKLNFMKSDNNNNNNNSNIINLLKTELSHLLSLKENIIKKLLNHIEQNIQNSSNKYTITYTDINNRMEDYKEEIESLEVYKHTIGNIQKEYILHLYENDKNALAVHNTSMQILQYKDAIQNIKNKISDDIKILKKYKEMNQDLLNYYEILDKKLKDNTYIKEMHTASLVQITQYIPYEDKTISELEQEFNNNNQKLDNILQDINAMNLNINILQTLNIGINACNTNNKNVEHLLNKKIELKNILNDQMKIIKNDDIIQDNEKENFSNVLKKEEEKLEKELDDIKFNNLKMDIHKLLNSYDHTKQNIESNLKINLDSFEKEKDSWVHFKSTIDSLYVEYNICNQKTHNTIKQQKNDIIELIYKRIKDINQEIIEKVDNYYSLSDKALTKLKSIHFNIDKEKYKNPKSQENIKLLEDRVMILEKKIKEDKDALIQIKNLSHDHFVNADNEKKKQKEKEEDDEQTHYSKKRKVMGDIYKDIKKNLDELNNKNLIDITLNEANKIESEYEKILIDDICEQITNEAKKSDTIKEKIESYKKDIDYVDVDVSKTRNDHHLNGDKIHDSFFYEDTLNYKAYFDKLKDLYENINKLTNESNGLKSDAHNNNTQVDKLKEINLQVFSNLGNIIKYVEKLENTLHELKDMYEFLETIDINKILKSIHNSMKKSEEYSNETKKIFEQSVNITNQFIEDVEILKTSINPNYESLNDDQIDDNIKSLVLKKEEISEKRKQVNKYITDIESNKEQSDLHLRYASRSIYVIDLFIKHEIINPSDGKNFDIIKVKEMINKTKQVSNEAMEYANKMDEKNKDIIKIENELYNLINNNIRSLKGVKYEKVRKQARNAIDDINNIHSNIKTILTKSKERLDEIKKQPNIKREGDVLNNDKTKIAYITIQINNGRIESNLLNILNMKHNIDTILNKAMDYMNDVSKSDQIVINIDSLNMNDIYNKDKDLLINILKEKQNMEAEYKKMNEMYNYVNETEKEIIKHKKNYEIRIMEHIKKETNEKKKKFMESNNKSLTTLMDSFRSMFYNEYINDYNINENFEKHQNILNEIYNGFNESYNIINTKMTEIINDNLDYNEIKEIKEVAQTEYDKLNKKVDELKNYLNNIKEQEGHRLIDYIKEKIFNLYIKCSEQQNIIDDSYNYITVKKQYIKTIEDVKFLLDSLNTIEEKNKSVANLEICTNKEDIKNLLKHVIKLANFSGIIVMSDTNTEITPENPLEDNDLLNLQLYFERKHEITSTLENDSDLELDHLGSNSDESIDNLKVYNDIIELHTYSTQILKYLDNIQKLKGDCNDLVKDCKELRELSTALYDLKIQITSVINRENDISNNIDIVSNKLNEIDAIQYNFEKYKEIFDNVEEYKTLDDTKNAYIVKKAEILKNVDINKTKEDLDIYFNDLDELEKSLTLSSNEMEIKTIVQNSYNSFSDINKNINDIDKEMKTLIPMLDELLNEGHNIDISLYNFIIRNIQIKIGNDIKNIREQENDTNICFEYIQNNYNFIKSDISIFNKYDDHIKVDNYISNNIDVVNKHNSLLSEHVINATNIIENIMTSIVEINEDTEMNSLEETQDKLLELYENFKKEKNIINNNYKIVHFNKLKEIENSLETYNSISTNFNKINETQNIDILKNEFNNIKTKINDKVKELVHVDSTLTLESIQTFNNLYGDLMSNIQDVYKYEDINNVELKKVKLYIENITNLLGRINTFIKELDKYQDENNGIDKYIEINKENNSYIIKLKEKANNLKENFSKLLQNIKRNETELYNINNIKDDIMNTGKSVNNIKQKFSSNLPLKEKLFQMEEMLLNINNIMNETKRISNTAAYTNITLQDIENNKNKENNNMNIETIDKLIDHIKIHNEKIQAEILIIDDAKRKVKEITDNINKAFNEITENYNNENNGVIKSAKNIVDEATYLNNELDKFLLKLNELLSHNNNDIKDLGDEKLILKEEEERKERERLEKAKQEEERKERERIEKEKQEKERLEREKQEQLKKEEELRKKEQERQEQQQKEEALKRQEQERLQKEEELKRQEQERLEREKQEQLQKEEELKRQEQERLQKEEALKRQEQERLQKEEELKRQEQERLEREKQEQLQKEEELKRQEQERLQKEEALKRQEQERLQKEEELKRQEQERLERKKIELAEREQHIKSKLESDMVKIIKDELTKEKDEIIKNKDIKLRHSLEQKWLKHLQNILSLKIDSLLNKNDEVIKDNETQLKTNILNSLKNQLYLNLKRELNEIIKEYEENQKKILHSNQLVNDSLEQKTNRLVDIKPTKHGDIYTNKLSDNETEMLITSKEKKDETESTKRSGTDHTNSSESTTDDNTNDRNFSRSKNLSVAIYTAGSVALCVLIFSSIGLLLIKTNSGDNNSNEINEAFEPNDDVLFKEKDEIIEITFNDNDSTI |
| Enzyme Length | 3130 |
| Uniprot Accession Number | Q8IDX6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Reticulocyte-binding protein homolog 2a]: During the asexual blood stage, binds to a chymotrypsin sensitive, neuraminidase and trypsin resistant receptor on the surface of the host erythrocyte (PubMed:21628513). Despite its binding capacity, appears to be dispensable for merozoite invasion of host erythrocytes (PubMed:12606570, PubMed:21698217). {ECO:0000269|PubMed:12606570, ECO:0000269|PubMed:21628513, ECO:0000269|PubMed:21698217}.; FUNCTION: [Reticulocyte-binding protein homolog 2a 85 kDa form]: During the asexual blood stage, binds to a trypsin-resistant and chymotrypsin and neuraminidase sensitive receptor on the surface of the host erythrocyte. {ECO:0000269|PubMed:21698217}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Coiled coil (3); Compositional bias (2); Glycosylation (41); Region (4); Repeat (24); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cell junction;Cell membrane;Coiled coil;Cytoplasmic vesicle;Glycoprotein;Leucine-rich repeat;Membrane;Merozoite;Receptor;Reference proteome;Repeat;Secreted;Signal;Tight junction;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21628513, ECO:0000269|PubMed:21698217}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21628513}. Secreted {ECO:0000269|PubMed:21628513}. Cell junction, tight junction {ECO:0000269|PubMed:21628513}. Note=Localizes to the rhoptry neck at the apical end of the merozoite (PubMed:21628513, PubMed:12228308). During merozoite invasion, mainly localizes to the tight junction formed between the parasite and the host erythrocyte membranes and then moves with the tight junction to the posterior end as the parasite enters the erythrocyte (PubMed:21628513). Also, the different processed forms are released from the membrane following proteolytic cleavage (PubMed:21628513). {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21628513}.; SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2a 85 kDa form]: Secreted {ECO:0000269|PubMed:21698217}. Cell membrane {ECO:0000269|PubMed:21698217}; Peripheral membrane protein {ECO:0000269|PubMed:21698217}; Extracellular side {ECO:0000269|PubMed:21698217}. Note=In mature schizont, co-localizes to the apical end of the schizont and the merozoite with reticulocyte-binding protein homolog 2b 285 kDa form. During merozoite invasion, shed from the cell surface. {ECO:0000269|PubMed:21698217}.; SUBCELLULAR LOCATION: [Reticulocyte-binding protein homolog 2a 285 kDa form]: Secreted {ECO:0000269|PubMed:21698217}. Cell membrane {ECO:0000269|PubMed:21698217}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizont, co-localizes to the apical end of the schizont and the merozoite with reticulocyte-binding protein homolog 2b 85 kDa form. During merozoite invasion, shed from the cell surface. {ECO:0000269|PubMed:21698217}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically processed into multiple fragments following schizont rupture (PubMed:21628513, PubMed:12228308, PubMed:21698217). In the mature schizont stage prior to merozoite release, full length RH2b is processed post-Golgi into C-terminal 285 kDa and N-terminal 85 kDa forms (PubMed:21628513, PubMed:21698217). During merozoite invasion of host erythrocytes, further processing occurs generating a 140 kDa C-terminal form (PubMed:21628513). At the same time, the C-terminal transmembrane region is probably cleaved, probably by a rhomboid protease, to shed all the different processed protein forms from the membrane leaving a transmembrane 7 kDa form on the merozoite surface (PubMed:21628513, PubMed:21698217). {ECO:0000269|PubMed:12228308, ECO:0000269|PubMed:21628513, ECO:0000269|PubMed:21698217}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16267556; |
| Motif | |
| Gene Encoded By | |
| Mass | 370,436 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |