ID Q764K6_PLAFA Unreviewed; 416 AA. AC Q764K6; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-NOV-2024, entry version 53. DE RecName: Full=Circumsporozoite protein {ECO:0000256|RuleBase:RU369056}; DE Short=CS {ECO:0000256|RuleBase:RU369056}; DE Contains: DE RecName: Full=Circumsporozoite protein C-terminus {ECO:0000256|RuleBase:RU369056}; GN Name=csp {ECO:0000313|EMBL:BAD08405.1}; OS Plasmodium falciparum (malaria parasite P. falciparum). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=5833 {ECO:0000313|EMBL:BAD08405.1}; RN [1] {ECO:0000313|EMBL:BAD08405.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=96M320-74 {ECO:0000313|EMBL:BAD08405.1}; RX PubMed=14739451; DOI=10.1126/science.1092077; RA Tanabe K., Sakihama N., Kaneko A.; RT "Stable SNPs in malaria antigen genes in isolated populations."; RL Science 303:493-493(2004). RN [2] {ECO:0000313|EMBL:BAM85261.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Van96M307-105 {ECO:0000313|EMBL:BAM85263.1}, Van96M307-157 RC {ECO:0000313|EMBL:BAM85267.1}, Van96M308-276 RC {ECO:0000313|EMBL:BAM85265.1}, Van96M320-100 RC {ECO:0000313|EMBL:BAM85266.1}, Van96M320-153 RC {ECO:0000313|EMBL:BAM85268.1}, Van96M320-158 RC {ECO:0000313|EMBL:BAM85261.1}, Van96M320-57 RC {ECO:0000313|EMBL:BAM85262.1}, Van96M320-86 RC {ECO:0000313|EMBL:BAM85264.1}, Van97G220-105 RC {ECO:0000313|EMBL:BAM85274.1}, Van97G220-113 RC {ECO:0000313|EMBL:BAM85272.1}, Van97G220-13 RC {ECO:0000313|EMBL:BAM85277.1}, Van97G220-35 RC {ECO:0000313|EMBL:BAM85269.1}, Van97G220-59 RC {ECO:0000313|EMBL:BAM85271.1}, Van97G220-60 RC {ECO:0000313|EMBL:BAM85275.1}, Van97G316-78 RC {ECO:0000313|EMBL:BAM85273.1}, Van97G317-40 RC {ECO:0000313|EMBL:BAM85276.1}, Van97G317-65 RC {ECO:0000313|EMBL:BAM85270.1}, Van98M304-123 RC {ECO:0000313|EMBL:BAM85307.1}, Van98M304-167 RC {ECO:0000313|EMBL:BAM85310.1}, Van98M304-279 RC {ECO:0000313|EMBL:BAM85313.1}, Van98M304-65 RC {ECO:0000313|EMBL:BAM85312.1}, Van98M305-1 RC {ECO:0000313|EMBL:BAM85311.1}, Van98M305-10 RC {ECO:0000313|EMBL:BAM85302.1}, Van98M305-153 RC {ECO:0000313|EMBL:BAM85309.1}, Van98M305-170 RC {ECO:0000313|EMBL:BAM85303.1}, Van98M305-20 RC {ECO:0000313|EMBL:BAM85304.1}, Van98M305-211 RC {ECO:0000313|EMBL:BAM85301.1}, Van98M305-231 RC {ECO:0000313|EMBL:BAM85300.1}, Van98M305-41 RC {ECO:0000313|EMBL:BAM85305.1}, Van98M305-62 RC {ECO:0000313|EMBL:BAM85308.1}, Van98M305-68 RC {ECO:0000313|EMBL:BAM85306.1}, Van98P224-1 RC {ECO:0000313|EMBL:BAM85280.1}, Van98P224-11 RC {ECO:0000313|EMBL:BAM85289.1}, Van98P224-156 RC {ECO:0000313|EMBL:BAM85283.1}, Van98P224-17 RC {ECO:0000313|EMBL:BAM85290.1}, Van98P224-177 RC {ECO:0000313|EMBL:BAM85299.1}, Van98P224-200 RC {ECO:0000313|EMBL:BAM85293.1}, Van98P224-247 RC {ECO:0000313|EMBL:BAM85292.1}, Van98P224-30 RC {ECO:0000313|EMBL:BAM85284.1}, Van98P224-38 RC {ECO:0000313|EMBL:BAM85285.1}, Van98P224-44 RC {ECO:0000313|EMBL:BAM85287.1}, Van98P224-52 RC {ECO:0000313|EMBL:BAM85286.1}, Van98P224-6 RC {ECO:0000313|EMBL:BAM85282.1}, Van98P224-69 RC {ECO:0000313|EMBL:BAM85291.1}, Van98P225-18 RC {ECO:0000313|EMBL:BAM85281.1}, Van98P225-19 RC {ECO:0000313|EMBL:BAM85295.1}, Van98P225-23 RC {ECO:0000313|EMBL:BAM85297.1}, Van98P226-109 RC {ECO:0000313|EMBL:BAM85296.1}, Van98P226-243 RC {ECO:0000313|EMBL:BAM85288.1}, Van98P226-52 RC {ECO:0000313|EMBL:BAM85294.1}, Van98P226-53 RC {ECO:0000313|EMBL:BAM85279.1}, Van98P226-91 RC {ECO:0000313|EMBL:BAM85278.1}, and Van98P226-97 RC {ECO:0000313|EMBL:BAM85298.1}; RA Tanabe K., Mita T., Palacpac N.M.Q., Arisue N., Tougan T., Kawai S., RA Jombart T., Kobayashi F., Horii T.; RT "Within-population genetic diversity of Plasmodium falciparum vaccine RT candidate antigens reveals geographic distance from a Central sub-Saharan RT African origin."; RL Vaccine 31:1134-1139(2013). CC -!- FUNCTION: Essential sporozoite protein. In the mosquito vector, CC required for sporozoite development in the oocyst, migration through CC the vector hemolymph and entry into the vector salivary glands. In the CC vertebrate host, required for sporozoite migration through the host CC dermis and infection of host hepatocytes. Binds to highly sulfated CC heparan sulfate proteoglycans (HSPGs) on the surface of host CC hepatocytes. {ECO:0000256|ARBA:ARBA00045806, CC ECO:0000256|RuleBase:RU369056}. CC -!- FUNCTION: [Circumsporozoite protein C-terminus]: In the vertebrate CC host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on CC the surface of host hepatocytes and is required for sporozoite invasion CC of the host hepatocytes. {ECO:0000256|RuleBase:RU369056}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU369056}; CC Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU369056}. Cytoplasm CC {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU369056}. CC Note=Localizes to the cytoplasm and the cell membrane in oocysts at day CC 6 post infection and then gradually distributes over the entire cell CC surface of the sporoblast and the budding sporozoites. CC {ECO:0000256|RuleBase:RU369056}. CC -!- DOMAIN: The GPI-anchor is essential for cell membrane localization and CC for sporozoite formation inside the oocyst. CC {ECO:0000256|RuleBase:RU369056}. CC -!- DOMAIN: The N-terminus is involved in the initial binding to heparan CC sulfate proteoglycans (HSPGs) on the surface of host hepatocytes. The CC N-terminus masks the TSP type-1 (TSR) domain which maintains the CC sporozoites in a migratory state, enabling them to complete their CC journey to the salivary gland in the mosquito vector and then to the CC host liver. The unmasking of the TSP type-1 (TSR) domain when the CC sporozoite interacts with the host hepatocyte also protects sporozoites CC from host antibodies. {ECO:0000256|RuleBase:RU369056}. CC -!- DOMAIN: The TSP type-1 (TSR) domain is required for sporozoite CC development and invasion. CSP has two conformational states, an CC adhesive conformation in which the TSP type-1 (TSR) domain is exposed CC and a nonadhesive conformation in which the TSR is masked by the N- CC terminus. TSR-exposed conformation occurs during sporozoite development CC in the oocyst in the mosquito vector and during host hepatocyte CC invasion. TSR-masked conformation occurs during sporozoite migration CC through the hemolymph to salivary glands in the mosquito vector and in CC the host dermis. {ECO:0000256|RuleBase:RU369056}. CC -!- SIMILARITY: Belongs to the plasmodium circumsporozoite protein family. CC {ECO:0000256|ARBA:ARBA00006241, ECO:0000256|RuleBase:RU369056}. 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; AB116603; BAD08405.1; -; Genomic_DNA. DR EMBL; AB715539; BAM85261.1; -; Genomic_DNA. DR EMBL; AB715540; BAM85262.1; -; Genomic_DNA. DR EMBL; AB715541; BAM85263.1; -; Genomic_DNA. DR EMBL; AB715542; BAM85264.1; -; Genomic_DNA. DR EMBL; AB715543; BAM85265.1; -; Genomic_DNA. DR EMBL; AB715544; BAM85266.1; -; Genomic_DNA. DR EMBL; AB715545; BAM85267.1; -; Genomic_DNA. DR EMBL; AB715546; BAM85268.1; -; Genomic_DNA. DR EMBL; AB715547; BAM85269.1; -; Genomic_DNA. DR EMBL; AB715548; BAM85270.1; -; Genomic_DNA. DR EMBL; AB715549; BAM85271.1; -; Genomic_DNA. DR EMBL; AB715550; BAM85272.1; -; Genomic_DNA. DR EMBL; AB715551; BAM85273.1; -; Genomic_DNA. DR EMBL; AB715552; BAM85274.1; -; Genomic_DNA. DR EMBL; AB715553; BAM85275.1; -; Genomic_DNA. DR EMBL; AB715554; BAM85276.1; -; Genomic_DNA. DR EMBL; AB715555; BAM85277.1; -; Genomic_DNA. DR EMBL; AB715556; BAM85278.1; -; Genomic_DNA. DR EMBL; AB715557; BAM85279.1; -; Genomic_DNA. DR EMBL; AB715558; BAM85280.1; -; Genomic_DNA. DR EMBL; AB715559; BAM85281.1; -; Genomic_DNA. DR EMBL; AB715560; BAM85282.1; -; Genomic_DNA. DR EMBL; AB715561; BAM85283.1; -; Genomic_DNA. DR EMBL; AB715562; BAM85284.1; -; Genomic_DNA. DR EMBL; AB715563; BAM85285.1; -; Genomic_DNA. DR EMBL; AB715564; BAM85286.1; -; Genomic_DNA. DR EMBL; AB715565; BAM85287.1; -; Genomic_DNA. DR EMBL; AB715566; BAM85288.1; -; Genomic_DNA. DR EMBL; AB715567; BAM85289.1; -; Genomic_DNA. DR EMBL; AB715568; BAM85290.1; -; Genomic_DNA. DR EMBL; AB715569; BAM85291.1; -; Genomic_DNA. DR EMBL; AB715570; BAM85292.1; -; Genomic_DNA. DR EMBL; AB715571; BAM85293.1; -; Genomic_DNA. DR EMBL; AB715572; BAM85294.1; -; Genomic_DNA. DR EMBL; AB715573; BAM85295.1; -; Genomic_DNA. DR EMBL; AB715574; BAM85296.1; -; Genomic_DNA. DR EMBL; AB715575; BAM85297.1; -; Genomic_DNA. DR EMBL; AB715576; BAM85298.1; -; Genomic_DNA. DR EMBL; AB715577; BAM85299.1; -; Genomic_DNA. DR EMBL; AB715578; BAM85300.1; -; Genomic_DNA. DR EMBL; AB715579; BAM85301.1; -; Genomic_DNA. DR EMBL; AB715580; BAM85302.1; -; Genomic_DNA. DR EMBL; AB715581; BAM85303.1; -; Genomic_DNA. DR EMBL; AB715582; BAM85304.1; -; Genomic_DNA. DR EMBL; AB715583; BAM85305.1; -; Genomic_DNA. DR EMBL; AB715584; BAM85306.1; -; Genomic_DNA. DR EMBL; AB715585; BAM85307.1; -; Genomic_DNA. DR EMBL; AB715586; BAM85308.1; -; Genomic_DNA. DR EMBL; AB715587; BAM85309.1; -; Genomic_DNA. DR EMBL; AB715588; BAM85310.1; -; Genomic_DNA. DR EMBL; AB715589; BAM85311.1; -; Genomic_DNA. DR EMBL; AB715590; BAM85312.1; -; Genomic_DNA. DR EMBL; AB715591; BAM85313.1; -; Genomic_DNA. DR AlphaFoldDB; Q764K6; -. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-UniRule. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1. DR InterPro; IPR003067; Crcmsprzoite. DR InterPro; IPR051860; Plasmodium_CSP_Invasion. DR InterPro; IPR000884; TSP1_rpt. DR InterPro; IPR036383; TSP1_rpt_sf. DR PANTHER; PTHR44826; SPORE COAT PROTEIN SP85; 1. DR PANTHER; PTHR44826:SF3; SPORE COAT PROTEIN SP85; 1. DR Pfam; PF00090; TSP_1; 1. DR PRINTS; PR01303; CRCMSPRZOITE. DR SMART; SM00209; TSP1; 1. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1. DR PROSITE; PS50092; TSP1; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|RuleBase:RU369056}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369056}; KW Disulfide bond {ECO:0000256|RuleBase:RU369056}; KW Glycoprotein {ECO:0000256|RuleBase:RU369056}; KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622, ECO:0000256|RuleBase:RU369056}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU369056}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369056}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|RuleBase:RU369056}; KW Sporozoite {ECO:0000256|ARBA:ARBA00022522, ECO:0000256|RuleBase:RU369056}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|RuleBase:RU369056" FT CHAIN 19..416 FT /note="Circumsporozoite protein" FT /evidence="ECO:0000256|RuleBase:RU369056" FT /id="PRO_5007710316" FT REGION 69..331 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..107 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..326 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 416 AA; 44788 MW; EF38EA17DF6D3FDF CRC64; MMRKLAILSV SSFLFVEALF QEYQCYGSSS NTRVLNELNY DNAGTNLYNE LEMNYYGKQE NWYSLKKNSR SLGENDDGNN NNGDNGREGK DEDKRDGNNE DNEKLRKPKH KKLKQPGDGN PDPNANPNVD PNANPNVDPN ANPNVDPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNKNNQGNGQ GHNMPNDPNR NVDENANANN AVKNNNNEEP SDKHIEQYLK KIQNSLSTEW SPCSVTCGNG IQVRIKPGSA NKPKDELDYE NDIEKKICKM EKCSSVFNVV NSSIGLIMVL SFLFLN //