RHBL1_TOXGO
ID RHBL1_TOXGO Reviewed; 293 AA.
AC Q695U0; Q696L6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Rhomboid-like protease 1;
DE EC=3.4.21.105;
GN Name=ROM1;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=RH;
RX PubMed=15358257; DOI=10.1016/j.mib.2004.06.013;
RA Dowse T., Soldati D.;
RT "Host cell invasion by the apicomplexans: the significance of microneme
RT protein proteolysis.";
RL Curr. Opin. Microbiol. 7:388-396(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15753289; DOI=10.1073/pnas.0407918102;
RA Brossier F., Jewett T.J., Sibley L.D., Urban S.;
RT "A spatially localized rhomboid protease cleaves cell surface adhesins
RT essential for invasion by Toxoplasma.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4146-4151(2005).
CC -!- FUNCTION: Serine protease involved in intramembrane proteolysis and the
CC subsequent release of polypeptides from their membrane anchors. Has no
CC detectable activity towards MIC2. {ECO:0000269|PubMed:15753289}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad
CC composed of serine and histidine that are contributed by different
CC transmembrane domains.; EC=3.4.21.105;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme
CC membrane {ECO:0000269|PubMed:15753289}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15753289}. Note=Detected in micronemes in
CC intracellular and extracellular tachyzoites, together with MIC2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q695U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q695U0-2; Sequence=VSP_019081;
CC -!- DEVELOPMENTAL STAGE: Detected in tachyzoites, bradyzoites and
CC sporozoites. {ECO:0000269|PubMed:15753289}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; AY596191; AAT29065.1; -; mRNA.
DR EMBL; AY587210; AAT84608.1; -; mRNA.
DR AlphaFoldDB; Q695U0; -.
DR SMR; Q695U0; -.
DR MEROPS; S54.019; -.
DR VEuPathDB; ToxoDB:TGARI_200290; -.
DR VEuPathDB; ToxoDB:TGCAST_200290; -.
DR VEuPathDB; ToxoDB:TGCOUG_200290; -.
DR VEuPathDB; ToxoDB:TGDOM2_200290; -.
DR VEuPathDB; ToxoDB:TGFOU_200290; -.
DR VEuPathDB; ToxoDB:TGGT1_200290; -.
DR VEuPathDB; ToxoDB:TGMAS_200290; -.
DR VEuPathDB; ToxoDB:TGME49_200290; -.
DR VEuPathDB; ToxoDB:TGP89_200290; -.
DR VEuPathDB; ToxoDB:TGPRC2_200290; -.
DR VEuPathDB; ToxoDB:TGRH88_083130; -.
DR VEuPathDB; ToxoDB:TGRUB_200290; -.
DR VEuPathDB; ToxoDB:TGVAND_200290; -.
DR VEuPathDB; ToxoDB:TGVEG_200290; -.
DR BRENDA; 3.4.21.105; 6411.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033163; C:microneme membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR002610; Peptidase_S54_rhomboid.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR PANTHER; PTHR22936; PTHR22936; 1.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Hydrolase; Membrane; Protease;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..293
FT /note="Rhomboid-like protease 1"
FT /id="PRO_0000239074"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 232
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15753289"
FT /id="VSP_019081"
SQ SEQUENCE 293 AA; 32839 MW; 6BA53255A59E3F1E CRC64;
MARVRTLADL RTEDEADEHT PLYNAETGSR DSDSTSSGGA APRSMPIRFL ELLFPHFSLK
SVVLAISIVD WIFYIVTVCL DTELPLIPAA NILVHFGANY PPLIKQGQVW RLLLPVFLHA
NFFHVFFNVF FQLRMGFTIE RRYGLLKFTG LYFASAIYGN LLSATAFFCN SLKVGASTAG
FGLIGIQICE MALTWHRMRH RDRMLTNMVS FVLLMVLLMF TLNGGSIDQM GHLGGLLCGF
SIGMLYNKEL NDKPVWYPWA SAAAIGILLA LPAACFPILY AVDRHCHRDL SYI
