CSP_PLAFL
ID CSP_PLAFL Reviewed; 315 AA.
AC P05691;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Circumsporozoite protein {ECO:0000303|PubMed:2442154};
DE Short=CS {ECO:0000303|PubMed:2442154};
DE Contains:
DE RecName: Full=Circumsporozoite protein C-terminus {ECO:0000305};
DE Flags: Fragment;
GN Name=CSP {ECO:0000250|UniProtKB:P02893};
OS Plasmodium falciparum (isolate le5).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5840;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND REPEATS.
RX PubMed=2442154; DOI=10.1016/s0021-9258(18)45298-2;
RA la Cruz V.F., Lal A.A., McCutchan T.F.;
RT "Sequence variation in putative functional domains of the circumsporozoite
RT protein of Plasmodium falciparum. Implications for vaccine development.";
RL J. Biol. Chem. 262:11935-11939(1987).
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:2442154}.
CC -!- SIMILARITY: Belongs to the plasmodium circumsporozoite protein family.
CC {ECO:0000305}.
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; M17802; AAA29538.1; -; Genomic_DNA.
DR AlphaFoldDB; P05691; -.
DR SMR; P05691; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Glycoprotein; GPI-anchor; Lipoprotein; Malaria;
KW Membrane; Repeat; Sporozoite.
FT CHAIN <1..>315
FT /note="Circumsporozoite protein"
FT /id="PRO_0000217181"
FT CHAIN ?..>315
FT /note="Circumsporozoite protein C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT /id="PRO_0000455487"
FT REPEAT 107..110
FT /note="1"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 111..114
FT /note="2"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 115..118
FT /note="3"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 119..122
FT /note="4"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 123..126
FT /note="5"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 127..130
FT /note="6"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 131..134
FT /note="7"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 135..138
FT /note="8"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 139..142
FT /note="9"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 143..146
FT /note="10"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 147..150
FT /note="11"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 151..154
FT /note="12"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 155..158
FT /note="13"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 159..162
FT /note="14"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 163..166
FT /note="15"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 167..170
FT /note="16"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 171..174
FT /note="17"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 175..178
FT /note="18"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 179..182
FT /note="19"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 183..186
FT /note="20"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 187..190
FT /note="21"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 191..194
FT /note="22"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 195..198
FT /note="23"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 199..202
FT /note="24"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 203..206
FT /note="25"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 207..210
FT /note="26"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 211..214
FT /note="27"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 215..218
FT /note="28"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 219..222
FT /note="29"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 223..226
FT /note="30"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 227..230
FT /note="31"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 231..234
FT /note="32"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 235..238
FT /note="33"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 239..242
FT /note="34"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 243..246
FT /note="35"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 247..250
FT /note="36"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 251..254
FT /note="37"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 255..258
FT /note="38"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 259..262
FT /note="39"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REPEAT 263..266
FT /note="40"
FT /evidence="ECO:0000305|PubMed:2442154"
FT REGION 53..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..95
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 96..100
FT /note="Region I; contains the proteolytic cleavage site"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT REGION 107..266
FT /note="40 X 4 AA tandem repeats of P-N-[AV]-[ND]"
FT /evidence="ECO:0000305|PubMed:2442154"
FT COMPBIAS 65..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 315
SQ SEQUENCE 315 AA; 33649 MW; A334DB11FA7FD777 CRC64;
EALFQEYQCY GSSSNTRVLN ELNYDNAGTN LYNELEMNYY GKQENWYSLK KNSRSLGEND
DGNNNNGDNG REGKDEDKRD GNNEDNEKLR KPKHKKLKQP ADGNPDPNAN PNVDPNANPN
VDPNANPNVD PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNVDPN
ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN
ANPNANPNAN PNANPNANPN ANPNANPNKN NQGNGQGHNM PNDPNRNVDE NANGNNAVKN
NNNEEPSDQH IEKYL
