SEC11_PLAF7
ID SEC11_PLAF7 Reviewed; 184 AA.
AC Q8IE14; Q2V8J6; Q2V8J7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000305};
DE Short=PfSPC21 {ECO:0000303|PubMed:30127496};
DE EC=3.4.21.89 {ECO:0000269|PubMed:18054093};
DE AltName: Full=Signal peptidase 21 kDa {ECO:0000303|PubMed:18054093};
DE Short=PfSP21 {ECO:0000303|PubMed:18054093};
GN Name=SEC11 {ECO:0000305}; Synonyms=SPC21 {ECO:0000303|PubMed:30127496};
GN ORFNames=PF3D7_1331300 {ECO:0000312|EMBL:CAD52453.1};
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|EMBL:ABB91446.1, ECO:0000312|EMBL:ABB91447.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, AND PHOSPHORYLATION.
RX PubMed=18054093; DOI=10.1016/j.molbiopara.2007.10.007;
RA Tuteja R., Pradhan A., Sharma S.;
RT "Plasmodium falciparum signal peptidase is regulated by phosphorylation and
RT required for intra-erythrocytic growth.";
RL Mol. Biochem. Parasitol. 157:137-147(2008).
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, INTERACTION WITH
RP SPC25, SUBCELLULAR LOCATION, 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: Catalytic component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum (PubMed:18054093, PubMed:30127496). Specifically
CC cleaves N-terminal signal peptides that contain a hydrophobic alpha-
CC helix (h-region) shorter than 18-20 amino acids (By similarity).
CC {ECO:0000250|UniProtKB:P67812, ECO:0000269|PubMed:18054093,
CC ECO:0000269|PubMed:30127496}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000269|PubMed:18054093};
CC -!- ACTIVITY REGULATION: Phosphorylation increases catalytic activity
CC (PubMed:18054093). Ca(2+) slightly increases catalytic activity in
CC vitro (PubMed:18054093). {ECO:0000269|PubMed:18054093}.
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). Within the complex, interacts
CC with SPC25 (PubMed:30127496). The complex induces a local thinning of
CC the ER membrane which is used to measure the length of the signal
CC peptide (SP) h-region of protein substrates (By similarity). This
CC ensures the selectivity of the complex towards h-regions shorter than
CC 18-20 amino acids (By similarity). The complex interacts with the SEC61
CC channel-forming translocon complex and is involved in the import of
CC classical signal sequence-containing proteins (PubMed:30127496).
CC {ECO:0000250|UniProtKB:P67812, ECO:0000269|PubMed:30127496}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18054093, ECO:0000269|PubMed:30127496}; Single-pass
CC type II membrane protein {ECO:0000250|UniProtKB:P13679}. Note=Partially
CC colocalizes with SPC25 in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:30127496}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage,
CC including ring, trophozoite and schizont stages (at protein level).
CC {ECO:0000269|PubMed:18054093, ECO:0000269|PubMed:30127496}.
CC -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC activity (By similarity). It may be accommodated as a transmembrane
CC helix in the thinned membrane environment of the complex, similarly to
CC the signal peptide in the complex substrates (By similarity).
CC {ECO:0000250|UniProtKB:P67812}.
CC -!- PTM: Phosphorylated (PubMed:18054093). Phosphorylation increases
CC catalytic activity (PubMed:18054093). {ECO:0000269|PubMed:18054093}.
CC -!- DISRUPTION PHENOTYPE: Causes a reduction in parasite growth in the host
CC erythrocyte (PubMed:30127496, PubMed:18054093). Reduces levels of the
CC mature form of SERA5 but not of PEXEL-containing proteins
CC (PubMed:30127496). {ECO:0000269|PubMed:18054093,
CC ECO:0000269|PubMed:30127496}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {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; DQ286434; ABB91446.1; -; mRNA.
DR EMBL; DQ286435; ABB91447.1; -; Genomic_DNA.
DR EMBL; AL844509; CAD52453.1; -; Genomic_DNA.
DR RefSeq; XP_001350045.1; XM_001350009.1.
DR AlphaFoldDB; Q8IE14; -.
DR SMR; Q8IE14; -.
DR STRING; 5833.MAL13P1.167; -.
DR MEROPS; S26.010; -.
DR SwissPalm; Q8IE14; -.
DR PRIDE; Q8IE14; -.
DR EnsemblProtists; CAD52453; CAD52453; PF3D7_1331300.
DR GeneID; 813720; -.
DR KEGG; pfa:PF3D7_1331300; -.
DR VEuPathDB; PlasmoDB:PF3D7_1331300; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000434300; -.
DR VEuPathDB; PlasmoDB:Pf7G8_130035800; -.
DR VEuPathDB; PlasmoDB:PfCD01_130036900; -.
DR VEuPathDB; PlasmoDB:PfDd2_130037200; -.
DR VEuPathDB; PlasmoDB:PfGA01_130037500; -.
DR VEuPathDB; PlasmoDB:PfGB4_130037300; -.
DR VEuPathDB; PlasmoDB:PfGN01_130038100; -.
DR VEuPathDB; PlasmoDB:PfHB3_130037700; -.
DR VEuPathDB; PlasmoDB:PfIT_130036600; -.
DR VEuPathDB; PlasmoDB:PfKE01_130037000; -.
DR VEuPathDB; PlasmoDB:PfKH01_130035600; -.
DR VEuPathDB; PlasmoDB:PfKH02_130034300; -.
DR VEuPathDB; PlasmoDB:PfML01_130035200; -.
DR VEuPathDB; PlasmoDB:PfNF135_130036100; -.
DR VEuPathDB; PlasmoDB:PfNF166_130036800; -.
DR VEuPathDB; PlasmoDB:PfNF54_130036500; -.
DR VEuPathDB; PlasmoDB:PfSD01_130038100; -.
DR VEuPathDB; PlasmoDB:PfSN01_130034400; -.
DR VEuPathDB; PlasmoDB:PfTG01_130037100; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; Q8IE14; -.
DR OMA; PYIGMLT; -.
DR PhylomeDB; Q8IE14; -.
DR Proteomes; UP000001450; Chromosome 13.
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; ISS:GeneDB.
DR GO; GO:0008233; F:peptidase activity; ISS:GeneDB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; ISS:GeneDB.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR027245; Sec11.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF6; PTHR10806:SF6; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Phosphoprotein; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..184
FT /note="Signal peptidase complex catalytic subunit SEC11"
FT /id="PRO_0000453952"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P13679"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..184
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P13679"
FT REGION 170..181
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 63
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT CONFLICT 81
FT /note="K -> E (in Ref. 1; ABB91446)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> N (in Ref. 1; ABB91447)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="I -> M (in Ref. 1; ABB91447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 21125 MW; 9C9AD8348BD5E0D0 CRC64;
MDFIKEQYNS LVLDLRKTFR NKRDGLSHIL NVICLLLNAL MIWKLLVVFT GCESPVVVVL
SGSMEPGYYR GDTLALYHPP KIHAGDVVVY QINGRDIPIV HRILSLHTSK DNKFHLLSKG
DNNNIDDRGL YDPHQYWLEN EHVLGLSVGY TPYIGILTIW INEYPVVKWA IVSIMLIMIL
MGYE
