SPCS2_PLAF7
ID SPCS2_PLAF7 Reviewed; 179 AA.
AC Q9NFA0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Signal peptidase complex subunit 2 {ECO:0000303|PubMed:30127496};
DE Short=PfSPC25 {ECO:0000303|PubMed:30127496};
GN Name=SPC25 {ECO:0000303|PubMed:30127496};
GN ORFNames=PF3D7_0320700 {ECO:0000312|EMBL:CAB92303.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=10448855; DOI=10.1038/22964;
RA Bowman S., Lawson D., Basham D., Brown D., Chillingworth T., Churcher C.M.,
RA Craig A., Davies R.M., Devlin K., Feltwell T., Gentles S., Gwilliam R.,
RA Hamlin N., Harris D., Holroyd S., Hornsby T., Horrocks P., Jagels K.,
RA Jassal B., Kyes S., McLean J., Moule S., Mungall K.L., Murphy L.,
RA Oliver K., Quail M.A., Rajandream M.A., Rutter S., Skelton J., Squares R.,
RA Squares S., Sulston J.E., Whitehead S., Woodward J.R., Newbold C.,
RA Barrell B.G.;
RT "The complete nucleotide sequence of chromosome 3 of Plasmodium
RT falciparum.";
RL Nature 400:532-538(1999).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [3] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, IDENTIFICATION IN
RP A COMPLEX WITH PMV, INTERACTION WITH PMV AND SEC11, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30127496; DOI=10.1038/s41564-018-0219-2;
RA Marapana D.S., Dagley L.F., Sandow J.J., Nebl T., Triglia T., Pasternak M.,
RA Dickerman B.K., Crabb B.S., Gilson P.R., Webb A.I., Boddey J.A.,
RA Cowman A.F.;
RT "Plasmepsin V cleaves malaria effector proteins in a distinct endoplasmic
RT reticulum translocation interactome for export to the erythrocyte.";
RL Nat. Microbiol. 3:1010-1022(2018).
CC -!- FUNCTION: Component of the signal peptidase complex (SPC) which
CC catalyzes the cleavage of N-terminal signal sequences from nascent
CC proteins as they are translocated into the lumen of the endoplasmic
CC reticulum (PubMed:30127496). Enhances the enzymatic activity of SPC and
CC facilitates the interactions between different components of the
CC translocation site (By similarity). Also, regulatory component of the
CC CSP25-plasmepsin PMV complex which cleaves the pentameric localization
CC motif RxLxE/Q/D (termed Plasmodium export element (PEXEL)) located
CC downstream of the N-terminal secretory signal sequence of several
CC proteins (PubMed:30127496). {ECO:0000250|UniProtKB:Q04969,
CC ECO:0000269|PubMed:30127496}.
CC -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC catalytic subunit SEC11/SPC21 and three accessory subunits SPC25,
CC SPC3/SPC22, SPC1/SPC12 (PubMed:30127496). The complex induces a local
CC thinning of the ER membrane which is used to measure the length of the
CC signal peptide (SP) h-region of protein substrates (By similarity).
CC This ensures the selectivity of the complex towards h-regions shorter
CC than 18-20 amino acids (By similarity). Within the complex, interacts
CC with SEC11/SPC21 (PubMed:30127496). Component of a complex composed of
CC SPC25 and PMV; the interaction is mediated via the transmembrane
CC domains (PubMed:30127496). The complex interacts with the SEC61
CC channel-forming translocon complex and is involved in the recognition
CC and import of PEXEL motif-containing proteins into the ER for
CC subsequent export (PubMed:30127496). {ECO:0000250|UniProtKB:P67812,
CC ECO:0000269|PubMed:30127496}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12368867}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Partially colocalizes with plasmepsin PMV in the
CC endoplasmic reticulum (PubMed:30127496). Partially colocalizes with
CC SEC11/SPC21 in the endoplasmic reticulum (PubMed:30127496).
CC {ECO:0000269|PubMed:30127496}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage;
CC expression is low at the ring stage and then increases through the
CC trophozoite and schizont stages (at protein level).
CC {ECO:0000269|PubMed:30127496}.
CC -!- DISRUPTION PHENOTYPE: Causes a severe growth defect in host
CC erythrocytes (PubMed:30127496). Export of protein containing a PEXEL
CC motif, including PIESP2, PTP3 and PTP2 is severely reduced at the ring
CC and trophozoite stages (PubMed:30127496). Similarly, export of RESA is
CC reduced at the schizont stage (PubMed:30127496).
CC {ECO:0000269|PubMed:30127496}.
CC -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR EMBL; AL844502; CAB92303.1; -; Genomic_DNA.
DR RefSeq; XP_001351277.1; XM_001351241.1.
DR AlphaFoldDB; Q9NFA0; -.
DR STRING; 5833.PFC0912w; -.
DR SwissPalm; Q9NFA0; -.
DR PRIDE; Q9NFA0; -.
DR EnsemblProtists; CAB92303; CAB92303; PF3D7_0320700.
DR GeneID; 814521; -.
DR KEGG; pfa:PF3D7_0320700; -.
DR VEuPathDB; PlasmoDB:PF3D7_0320700; -.
DR HOGENOM; CLU_1477887_0_0_1; -.
DR InParanoid; Q9NFA0; -.
DR OMA; EDIFMIL; -.
DR PhylomeDB; Q9NFA0; -.
DR Proteomes; UP000001450; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IDA:GeneDB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:GeneDB.
DR GO; GO:0015031; P:protein transport; TAS:GeneDB.
DR GO; GO:0006465; P:signal peptide processing; TAS:GeneDB.
DR InterPro; IPR009582; Spc2/SPCS2.
DR Pfam; PF06703; SPC25; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..179
FT /note="Signal peptidase complex subunit 2"
FT /id="PRO_0000453951"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..74
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 21012 MW; 4EAFF9C324B8A18F CRC64;
MSGNNVQEED STFHVSNLYS ETEIKKITQD FISEKIREQN FEEIVKYSNI RIFLSLVLIV
IGTYCSIFVQ YKKNPVIMIQ LLVAFFVVST TLIIFEYFFF DDVFMILRSN NGSLVKLYCR
LDVKKSTLIL AYKLNKNVFE TSFELKRLYN ENGYLMKPYA KNVVMNFLSA HGRTLKLKN
