CSP_PLAYO
ID CSP_PLAYO Reviewed; 367 AA.
AC P06914;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Circumsporozoite protein {ECO:0000303|PubMed:3102479};
DE Short=CS {ECO:0000250|UniProtKB:P02893};
DE Contains:
DE RecName: Full=Circumsporozoite protein C-terminus {ECO:0000305};
DE Flags: Precursor;
GN Name=CSP {ECO:0000303|PubMed:3102479};
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REPEATS.
RX PubMed=3102479; DOI=10.1016/s0021-9258(18)61449-8;
RA Lal A.A., de la Cruz V.F., Welsh J.A., Charoenvit Y., Maloy W.L.,
RA McCutchan T.F.;
RT "Structure of the gene encoding the circumsporozoite protein of Plasmodium
RT yoelii. A rodent model for examining antimalarial sporozoite vaccines.";
RL J. Biol. Chem. 262:2937-2940(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140 AND 260-367, AND POLYMORPHISM.
RX PubMed=3287156; DOI=10.1016/0166-6851(88)90176-4;
RA de la Cruz V.F., Lal A.A., McCutchan T.F.;
RT "Variation among circumsporozoite protein genes from rodent malarias.";
RL Mol. Biochem. Parasitol. 28:31-38(1988).
CC -!- FUNCTION: Essential sporozoite protein (By similarity). In the mosquito
CC vector, required for sporozoite development in the oocyst, migration
CC through the vector hemolymph and entry into the vector salivary glands
CC (By similarity). In the vertebrate host, required for sporozoite
CC migration through the host dermis and infection of host hepatocytes (By
CC similarity). Binds to highly sulfated heparan sulfate proteoglycans
CC (HSPGs) on the surface of host hepatocytes (By similarity).
CC {ECO:0000250|UniProtKB:P02893, ECO:0000250|UniProtKB:P23093}.
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:0000250|UniProtKB:P23093}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19597};
CC Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:P23093}. Note=Localizes to the cytoplasm and the
CC cell membrane in oocysts at day 6 post infection and then gradually
CC distributes over the entire cell surface of the sporoblast and the
CC budding sporozoites. {ECO:0000250|UniProtKB:P23093}.
CC -!- DOMAIN: The N-terminus is involved in the initial binding to heparan
CC sulfate proteoglycans (HSPGs) on the surface of host hepatocytes (By
CC similarity). The N-terminus masks the TSP type-1 (TSR) domain which
CC maintains the sporozoites in a migratory state, enabling them to
CC complete their journey to the salivary gland in the mosquito vector and
CC then to the host liver. The unmasking of the TSP type-1 (TSR) domain
CC when the sporozoite interacts with the host hepatocyte also protects
CC sporozoites from host antibodies (By similarity).
CC {ECO:0000250|UniProtKB:P23093, ECO:0000250|UniProtKB:Q7K740}.
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:0000250|UniProtKB:P23093}.
CC -!- DOMAIN: The GPI-anchor is essential for cell membrane localization and
CC for sporozoite formation inside the oocyst.
CC {ECO:0000250|UniProtKB:P23093}.
CC -!- PTM: During host cell invasion, proteolytically cleaved at the cell
CC membrane in the region I by a papain-like cysteine protease of parasite
CC origin (By similarity). Cleavage is triggered by the sporozoite contact
CC with highly sulfated heparan sulfate proteoglycans (HSPGs) present on
CC the host hepatocyte cell surface (By similarity). Cleavage exposes the
CC TSP type-1 (TSR) domain and is required for productive invasion of host
CC hepatocytes but not for adhesion to the host cell membrane (By
CC similarity). Cleavage is dispensable for sporozoite development in the
CC oocyst, motility and for traversal of host and vector cells (By
CC similarity). {ECO:0000250|UniProtKB:P02893,
CC ECO:0000250|UniProtKB:P23093}.
CC -!- PTM: O-glycosylated; maybe by POFUT2. {ECO:0000250|UniProtKB:P19597}.
CC -!- POLYMORPHISM: The sequence of the repeats varies across Plasmodium
CC species and strains. {ECO:0000269|PubMed:3287156}.
CC -!- SIMILARITY: Belongs to the plasmodium circumsporozoite protein family.
CC {ECO:0000305}.
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DR EMBL; J02695; AAA29558.1; -; Genomic_DNA.
DR EMBL; M18821; AAA29559.1; -; Genomic_DNA.
DR EMBL; M22698; AAA29560.1; -; Genomic_DNA.
DR AlphaFoldDB; P06914; -.
DR SMR; P06914; -.
DR IntAct; P06914; 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR003067; Crcmsprzoite.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01303; CRCMSPRZOITE.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Malaria; Membrane; Repeat; Signal; Sporozoite.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..344
FT /note="Circumsporozoite protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024536"
FT CHAIN ?..344
FT /note="Circumsporozoite protein C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT /id="PRO_0000455509"
FT PROPEP 345..367
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455510"
FT REPEAT 139..144
FT /note="1-1"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 145..150
FT /note="1-2"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 151..156
FT /note="1-3"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 157..162
FT /note="1-4"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 163..168
FT /note="1-5"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 169..174
FT /note="1-6"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 175..180
FT /note="1-7"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 181..186
FT /note="1-8"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 187..192
FT /note="1-9"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 193..198
FT /note="1-10"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 199..204
FT /note="1-11"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 205..210
FT /note="1-12"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 211..216
FT /note="1-13"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 217..222
FT /note="1-14"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 223..228
FT /note="1-15"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 229..232
FT /note="2-1; approximate"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 233..236
FT /note="2-2"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 237..240
FT /note="2-3"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 241..244
FT /note="2-4"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 245..248
FT /note="2-5"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 249..252
FT /note="2-6"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 253..256
FT /note="2-7"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REPEAT 257..260
FT /note="2-8; approximate"
FT /evidence="ECO:0000305|PubMed:3102479"
FT DOMAIN 294..345
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 72..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..121
FT /note="Required for the binding to heparan sulfate
FT proteoglycans (HSPGs) on the surface of host hepatocytes"
FT /evidence="ECO:0000250|UniProtKB:Q7K740"
FT REGION 126..130
FT /note="Region I; contains the proteolytic cleavage site"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT REGION 139..228
FT /note="15 X 6 AA tandem repeats of Q-G-P-G-A-P"
FT /evidence="ECO:0000305|PubMed:3102479"
FT REGION 229..260
FT /note="8 X 4 AA approximate tandem repeats of Q-Q-P-P"
FT /evidence="ECO:0000305|PubMed:3102479"
FT COMPBIAS 72..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 344
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250|UniProtKB:P19597"
FT DISULFID 306..339
FT /evidence="ECO:0000250|UniProtKB:Q7K740"
FT DISULFID 310..344
FT /evidence="ECO:0000250|UniProtKB:Q7K740"
SQ SEQUENCE 367 AA; 38888 MW; 1EA56AFF7FFCB5E3 CRC64;
MKKCTILVVA SLLLVDSLLP GYGQNKSVQA QRNLNELCYN EENDNKLYHV LNSKNGKIYN
RNIVNRLLGD ALNGKPEEKK DDPPKDGNKD DLPKEEKKDD LPKEEKKDDP PKDPKKDDPP
KEAQNKLNQP VVADENVDQG PGAPQGPGAP QGPGAPQGPG APQGPGAPQG PGAPQGPGAP
QGPGAPQGPG APQGPGAPQG PGAPQGPGAP QGPGAPQGPG APQGPGAPQE PPQQPPQQPP
QQPPQQPPQQ PPQQPPQQPR PQPDGNNNNN NNNGNNNEDS YVPSAEQILE FVKQISSQLT
EEWSQCSVTC GSGVRVRKRK NVNKQPENLT LEDIDTEICK MDKCSSIFNI VSNSLGFVIL
LVLVFFN
