PLM5_PLAFX
ID PLM5_PLAFX Reviewed; 597 AA.
AC A0A0L7K812;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Plasmepsin V {ECO:0000303|PubMed:16024107};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q8I6Z5};
DE AltName: Full=Plasmepsin 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=PMV {ECO:0000303|PubMed:16024107};
GN ORFNames=PFHG_00958 {ECO:0000312|EMBL:KOB59201.1};
OS Plasmodium falciparum (isolate HB3).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=137071 {ECO:0000312|Proteomes:UP000054289};
RN [1] {ECO:0000312|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB3 {ECO:0000312|Proteomes:UP000054289};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND LACK OF PROPEPTIDE
RP PROCESSING.
RX PubMed=16024107; DOI=10.1016/j.molbiopara.2005.05.015;
RA Klemba M., Goldberg D.E.;
RT "Characterization of plasmepsin V, a membrane-bound aspartic protease
RT homolog in the endoplasmic reticulum of Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 143:183-191(2005).
CC -!- FUNCTION: During the asexual blood stage, plays an essential role in
CC the export of several proteins into the host erythrocytes by cleaving
CC the pentameric localization motif RxLxE/Q/D (termed Plasmodium export
CC element (PEXEL)) located downstream of the N-terminal secretory signal
CC sequence (By similarity). Specifically, cleaves after the leucine
CC residue in the RxLxE/Q/D (or RxLxxE) motif of exported proteins
CC including RESA, EMP2, EMP3, KAHRP, RIF/Rifin and STEVOR (By
CC similarity). Also, by regulating protein export, plays an essential
CC role in gametocyte development and thus parasite transmission to the
CC mosquito vector (By similarity). {ECO:0000250|UniProtKB:Q8I6Z5,
CC ECO:0000250|UniProtKB:W7JPD9}.
CC -!- SUBUNIT: Component of a complex composed of SPC25 and PMV; the
CC interaction is mediated via the transmembrane domains. The complex
CC interacts with the SEC61 channel-forming translocon complex and is
CC involved in the recognition and import of PEXEL motif-containing
CC proteins into the ER for subsequent export.
CC {ECO:0000250|UniProtKB:Q8I6Z5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16024107}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q8I6Z5}. Note=During gametogenesis, localizes to
CC the perinuclear ER in stage I-II gametocytes, and relocalizes towards
CC the cell periphery as the ER redistributes in the cell in stage III-IV
CC gametocytes (By similarity). Partially colocalizes with SPC25 in the
CC endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:W7JPD9}.
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:16024107}.
CC -!- DOMAIN: The transmembrane domain is essential for localization to the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8I6Z5}.
CC -!- PTM: It is not clear if the zymogen has a cleavable propeptide
CC (PubMed:16024107). In vitro, appears to be cleaved between Asn-87 and
CC Ala-88 (By similarity). Cleavage of the putative propeptide is
CC dispensable for catalytic activity (By similarity).
CC {ECO:0000250|UniProtKB:Q8I6Z5, ECO:0000269|PubMed:16024107}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000255|RuleBase:RU000454}.
CC -!- CAUTION: It is unclear if PMV is glycosylated as other members of the
CC same enzyme family, ie. PMI and PMII, are not. {ECO:0000305}.
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DR EMBL; CH671932; KOB59201.1; -; Genomic_DNA.
DR SMR; A0A0L7K812; -.
DR EnsemblProtists; KOB59201; KOB59201; PFHG_00958.
DR VEuPathDB; PlasmoDB:PfHB3_130029900; -.
DR Proteomes; UP000054289; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06096; Plasmepsin_5; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033866; Plasmepsin_5.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR47966; PTHR47966; 2.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Coiled coil; Disulfide bond; Endoplasmic reticulum;
KW Hydrolase; Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..597
FT /note="Plasmepsin V"
FT /id="PRO_0000453927"
FT TOPO_DOM 1..551
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8I6Z5"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8I6Z5"
FT DOMAIN 107..521
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..88
FT /evidence="ECO:0000255"
FT COMPBIAS 58..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DISULFID 135..218
FT /evidence="ECO:0000250|UniProtKB:A5K302"
FT DISULFID 138..141
FT /evidence="ECO:0000250|UniProtKB:A5K302"
FT DISULFID 162..173
FT /evidence="ECO:0000250|UniProtKB:A5K302"
FT DISULFID 167..178
FT /evidence="ECO:0000250|UniProtKB:A5K302"
FT DISULFID 266..525
FT /evidence="ECO:0000250|UniProtKB:A5K302"
FT DISULFID 396..441
FT /evidence="ECO:0000250|UniProtKB:A5K302"
FT DISULFID 450..486
FT /evidence="ECO:0000250|UniProtKB:A5K302"
SQ SEQUENCE 597 AA; 69308 MW; 455D949A0898ED3F CRC64;
MNNYFLRKEN FFILFCFVFV SIFFVSNVTI IKCNNVENKI DNVGKKIENV GKKIGDMENK
NDNVENKNDN VENKNDNVGN KNDNVKNASS DLYKYKLYGD IDEYAYYFLD IDIGKPSQRI
SLILDTGSSS LSFPCNGCKD CGIHMEKPYN LNYSKTSSIL YCNKSNCPYG LKCVGNKCEY
LQSYCEGSQI YGFYFSDIVT LPSYNNKKKI SFEKLMGCHM HEESLFLHQQ ATGVLGFSLT
KPNGVPTFVD LLFKHTPSLK PIYSICVSEH GGELIIGGYE PDYFLSNQKE KQKMDKSDNN
SSNKGNVSIK LKNNDKNDDE ENNSKDVIVS NNVEDIVWQA ITRKYYYYIK IYGLDLYGTN
IMDKKELDML VDSGSTFTHI PENIYNQINY YLDILCIHDM TNIYEINKRL KLTNESLNKP
LVYFEDFKTA LKNIIQNENL CIKIVDGVQC WKSLENLPNL YITLSNNYKM IWKPSSYLYK
KESFWCKGLE KQVNNKPILG LTFFKNKQVI FDLQQNQIAF IESKCPSNLT SSRPRTFNEY
REKENIFLKV SYINLYCLWL LLALTILLSL ILYVRKMFYM DYFPLSDQNK SPIQEST
