ID   RESA_PLAFF              Reviewed;        1073 AA.
AC   P13830;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Ring-infected erythrocyte surface antigen;
DE   Flags: Precursor;
GN   Name=RESA;
OS   Plasmodium falciparum (isolate FC27 / Papua New Guinea).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=3537955; DOI=10.1093/nar/14.21.8265;
RA   Favaloro J.M., Coppel R.L., Corcoran L.M., Foote S.J., Brown G.V.,
RA   Anders R.F., Kemp D.J.;
RT   "Structure of the RESA gene of Plasmodium falciparum.";
RL   Nucleic Acids Res. 14:8265-8277(1986).
CC   -!- FUNCTION: May disrupt the normal intermolecular interactions of the
CC       cytoplasmic domain of band 3 and thereby facilitate the invagination of
CC       the red cell membrane which is necessary for the formation of the
CC       parasitophorous vacuole.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Probably located on the cytoplasmic face of the
CC       membrane where it associates with components of the membrane skeleton.
CC   -!- PTM: The Tyr residues in the variant tetrameric sequences in the RESA
CC       repeat are possibly phosphorylated (by homology with band 3).
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DR   EMBL; X04572; CAA28241.1; -; Genomic_DNA.
DR   EMBL; X05182; CAA28817.1; -; mRNA.
DR   PIR; A25526; A25526.
DR   PDB; 2MUA; NMR; -; A=181-200.
DR   PDBsum; 2MUA; -.
DR   AlphaFoldDB; P13830; -.
DR   BMRB; P13830; -.
DR   SMR; P13830; -.
DR   DrugBank; DB11638; Artenimol.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 6.10.280.180; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR026894; DnaJ_X.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR019111; PRESA_N.
DR   InterPro; IPR044885; PRESA_N_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF14308; DnaJ-X; 1.
DR   Pfam; PF09687; PRESAN; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Glycoprotein; Malaria; Membrane; Repeat;
KW   Signal.
FT   SIGNAL          1..65
FT   CHAIN           66..1073
FT                   /note="Ring-infected erythrocyte surface antigen"
FT                   /id="PRO_0000007271"
FT   DOMAIN          521..589
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          428..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..504
FT                   /note="Tandem repeats 1"
FT   REGION          891..1073
FT                   /note="Tandem repeats 2"
FT   REGION          894..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..444
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..926
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..1073
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        639
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        773
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        777
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   HELIX           184..199
FT                   /evidence="ECO:0007829|PDB:2MUA"
SQ   SEQUENCE   1073 AA;  124907 MW;  A4D3C37E10BA6D90 CRC64;
     MRPFHAYSWI FSQQYMGTKN VKEKNPTIYS FDDEEKRNEN KSFLKVLCSK RGVLPIIGIL
     YIILNGNLGY NGSSSSGVQF TDRCSRNLYG ETLPVNPYAD SENPIVVSQV FGLPFEKPTF
     TLESPPDIDH TNILGFNEKF MTDVNRYRYS NNYEAIPHIS EFNPLIVDKV LFDYNEKVDN
     LGRSGGDIIK KMQTLWDEIM DINKRKYDSL KEKLQKTYSQ YKVQYDMPKE AYESKWTQCI
     KLIDQGGENL EERLNSQFKN WYRQKYLNLE EYRRLTVLNQ IAWKALSNQI QYSCRKIMNS
     DISSFKHINE LKSLEHRAAK AAEAEMKKRA QKPKKKKSRR GWLCCGGGDI ETVEPQQEEP
     VQTVQEQQVN EYGDILPSLR ASITNSAINY YDTVKDGVYL DHETSDALYT DEDLLFDLEK
     QKYMDMLDTS EEESVEENEE EHTVDDEHVE EHTADDEHVE EPTVADDEHV EEPTVADEHV
     EEPTVAEEHV EEPTVAEEHV EEPASDVQQT SEAAPTIEIP DTLYYDILGV GVNADMNEIT
     ERYFKLAENY YPYQRSGSTV FHNFRKVNEA YQVLGDIDKK RWYNKYGYDG IKQVNFMNPS
     IFYLLSSLEK FKDFTGTPQI VTLLRFFFEK RLSMNDLENK SEHLLKFMEQ YQKEREAHVS
     EYLLNILQPC IAGDSKWNVP IITKLEGLKG SRFDIPILES LRWIFKHVAK THLKKSSKSA
     KKLQQRTQAN KQELANINNN LMSTLKEYLG SSEQMNSITY NFENINSNVD NGNQSKNISD
     LSYTDQKEIL EKIVSYIVDI SLYDIENTAL NAAEQLLSDN SVDEKTLKKR AQSLKKLSSI
     MERYAGGKRN DKKSKNFDTK DIVGYIMHGI STINTEMKNQ NENVPEHVQH NAEENVEHDA
     EENVEHDAEE NVEHDAEENV EHDAEENVEH DAEENVEENV EEVEENVEEN VEENVEENVE
     EVEENVEENV EENVEENVEE NVEENVEENV EENVEENVEE YDEENVEEVE ENVEENVEEN
     VEENVEENVE EVEENVEENV EENVEENVEE NVEENVEEYD EENVEEHNEE YDE