ID   EBA1_PLAFC              Reviewed;        1435 AA.
AC   P19214;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Erythrocyte-binding antigen 175;
DE            Short=EBA-175;
OS   Plasmodium falciparum (isolate Camp / Malaysia).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Camp Malaysia;
RX   PubMed=2204835; DOI=10.1016/0166-6851(90)90193-p;
RA   Sim B.K.L.;
RT   "Sequence conservation of a functional domain of erythrocyte binding
RT   antigen 175 in Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 41:293-296(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2229177; DOI=10.1083/jcb.111.5.1877;
RA   Sim B.K., Orlandi P.A., Haynes J.D., Klotz F.W., Carter J.M., Camus D.,
RA   Zegans M.E., Chulay J.D.;
RT   "Primary structure of the 175K Plasmodium falciparum erythrocyte binding
RT   antigen and identification of a peptide which elicits antibodies that
RT   inhibit malaria merozoite invasion.";
RL   J. Cell Biol. 111:1877-1884(1990).
RN   [3]
RP   FUNCTION IN BINDING ERYTHROCYTES.
RX   PubMed=3901257; DOI=10.1126/science.3901257;
RA   Camus D., Hadley T.J.;
RT   "A Plasmodium falciparum antigen that binds to host erythrocytes and
RT   merozoites.";
RL   Science 230:553-556(1985).
CC   -!- FUNCTION: Binds to host erythrocytes; may act as bridge between
CC       erythrocytes and merozoites. {ECO:0000269|PubMed:3901257}.
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DR   EMBL; X52524; CAA36756.1; -; Genomic_DNA.
DR   PIR; A37793; A37793.
DR   PDB; 2MTW; NMR; -; A=1221-1239.
DR   PDBsum; 2MTW; -.
DR   AlphaFoldDB; P19214; -.
DR   BMRB; P19214; -.
DR   SMR; P19214; -.
DR   IntAct; P19214; 1.
DR   TCDB; 9.B.367.1.4; the plasmodium falciparum virulence factor trafficking system (pfvfts) family.
DR   PRIDE; P19214; -.
DR   ABCD; P19214; 2 sequenced antibodies.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   Gene3D; 1.10.1740.170; -; 1.
DR   Gene3D; 1.20.1310.20; -; 2.
DR   InterPro; IPR042202; Duffy-ag-bd_sf.
DR   InterPro; IPR008602; Duffy-antigen-binding.
DR   InterPro; IPR021620; EBA-175_C.
DR   InterPro; IPR043057; EBA-175_C_sf.
DR   Pfam; PF05424; Duffy_binding; 2.
DR   Pfam; PF11556; EBA-175_VI; 1.
PE   1: Evidence at protein level;
KW   3D-structure.
FT   CHAIN           1..1435
FT                   /note="Erythrocyte-binding antigen 175"
FT                   /id="PRO_0000217183"
FT   REGION          159..1104
FT                   /note="Essential for binding to erythrocytes"
FT   REGION          756..1143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..799
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..884
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..965
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1036
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1097
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         1031
FT                   /note="E -> V (in strain: FCR-3 and ITG)"
FT   HELIX           1224..1233
FT                   /evidence="ECO:0007829|PDB:2MTW"
SQ   SEQUENCE   1435 AA;  167390 MW;  32A4309021B1C3D6 CRC64;
     MKCNISIYFF ASFFVLYFAK ARNEYDIKEN EKFLDVYKEK FNELDKKKYG NVQKTDKKIF
     TFIENKLDIL NNSKFNKRWK SYGTPDNIDK NMSLINKHNN EEMFNNNYQS FLSTSSLIKQ
     NKYVPINAVR VSRILSFLDS RINNGRNTSS NNEVLSNCRE KRKGMKWDCK KKNDRSNYVC
     IPDRRIQLCI VNLSIIKTYT KETMKDHFIE ASKKESQLLL KKNDNKYNSK FCNDLKNSFL
     DYGHLAMGND MDFGGYSTKA ENKIQEVFKG AHGEISEHKI KNFRKEWWNE FREKLWEAML
     SEHKNNINNC KNIPQEELQI TQWIKEWHGE FLLERDNRSK LPKSKCKNNT LYEACEKECI
     DPCMKYRDWI IRSKFEWHTL SKEYETQKVP KENAENYLIK ISENKNDAKV SLLLNNCDAE
     YSKYCDCKHT TTLVKSVLNG NDNTIKEKRE HIDLDDFSKF GCDKNSVDTN TKVWECKNPY
     ILSTKDVCVP PRRQELCLGN IDRIYDKNLL MIKEHILAIA IYESRILKRK YKNKDDKEVC
     KIINKTFADI RDIIGGTDYW NDLSNRKLVG KINTNSKYVH RNKKNDKLFR DEWWKVIKKD
     VWNVISWVFK DKTVCKEDDI ENIPQFFRWF SEWGDDYCQD KTKMIETLKV ECKEKPCEDD
     NCKSKCNSYK EWISKKKEEY NKQAKQYQEY QKGNNYKMYS EFKSIKPEVY LKKYSEKCSN
     LNFEDEFKEE LHSDYKNKCT MCPEVKDVPI SIIRNNEQTS QEAVPEENTE IAHRTETPSI
     SEGPKGNEQK ERDDDSLSKI SVSPENSRPE TDAKDTSNLL KLKGDVDISM PKAVIGSSPN
     DNINVTEQGD NISGVNSKPL SDDVRPDKKE LEDQNSDESE ETVVNHISKS PSINNGDDSG
     SGSATVSESS SSNTGLSIDD DRNGDTFVRT QDTANTEDVI RKENADKDED EKGADEERHS
     TSESLSSPEE KMLTDNEGGN SLNHEEVKEH TSNSDNVQQS GGIVNMNVEK ELKDTLENPS
     SSLDEGKAHE ELSEPNLSSD QDMSNTPGPL DNTSEETTER ISNNEYKVNE REDERTLTKE
     YEDIVLKSHM NRESDDGELY DENSDLSTVN DESEDAEAKM KGNDTSEMSH NSSQHIESDQ
     QKNDMKTVGD LGTTHVQNEI SVPVTGEIDE KLRESKESKI HKAEEERLSH TDIHKINPED
     RNSNTLHLKD IRNEENERHL TNQNINISQE RDLQKHGFHT MNNLHGDGVS ERSQINHSHH
     GNRQDRGGNS GNVLNMRSNN NNFNNIPSRY NLYDKKLDLD LYENRNDSTT KELIKKLAEI
     NKCENEISVK YCDHMIHEEI PLKTCTKEKT RNLCCAVSDY CMSYFTYDSE EYYNCTKREF
     DDPSYTCFRK EAFSSMIFKF LITNKIYYYF YTYKTAKVTI KKINFSLIFF FFFSF