RHBL5_TOXGO
ID RHBL5_TOXGO Reviewed; 841 AA.
AC Q6GV23; Q696L8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Rhomboid-like protease 5;
DE EC=3.4.21.105;
DE AltName: Full=Microneme protein protease 1;
DE Short=MPP-1;
GN Name=ROM5; Synonyms=MPP1;
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].
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] OF 161-841, FUNCTION, MUTAGENESIS OF SER-531,
RP SUBCELLULAR LOCATION, AND 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).
RN [3]
RP FUNCTION.
RX PubMed=11927542; DOI=10.1093/emboj/21.7.1577;
RA Opitz C., Di Cristina M., Reiss M., Ruppert T., Crisanti A., Soldati D.;
RT "Intramembrane cleavage of microneme proteins at the surface of the
RT apicomplexan parasite Toxoplasma gondii.";
RL EMBO J. 21:1577-1585(2002).
CC -!- FUNCTION: Serine protease involved in intramembrane proteolysis.
CC Cleaves microneme adhesins, such as MIC2. This step is essential for
CC efficient invasion of host cells. Catalyzes intramembrane proteolysis
CC of AMA1. {ECO:0000269|PubMed:11927542, 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: Membrane {ECO:0000269|PubMed:15753289}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:15753289}. Note=Detected
CC primarily at the posterior surface of intracellular tachyzoites.
CC Detected in patches on the cell surface of extracellular tachyzoites.
CC Concentrated at the posterior end of tachyzoites after induction of
CC microneme secretion prior to invasion of host cells.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in tachyzoites. Detected at low
CC levels in bradyzoites and sporozoites. {ECO:0000269|PubMed:15753289}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT84606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY634626; AAT47708.1; -; mRNA.
DR EMBL; AY587208; AAT84606.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q6GV23; -.
DR MEROPS; S54.023; -.
DR EnsemblProtists; TGME49_294690-t26_1; TGME49_294690-t26_1; TGME49_294690.
DR VEuPathDB; ToxoDB:TGARI_294690; -.
DR VEuPathDB; ToxoDB:TGCAST_294690A; -.
DR VEuPathDB; ToxoDB:TGCAST_294690B; -.
DR VEuPathDB; ToxoDB:TGCOUG_294690; -.
DR VEuPathDB; ToxoDB:TGCOUG_395050; -.
DR VEuPathDB; ToxoDB:TGDOM2_294690A; -.
DR VEuPathDB; ToxoDB:TGDOM2_294690B; -.
DR VEuPathDB; ToxoDB:TGDOM2_294690C; -.
DR VEuPathDB; ToxoDB:TGFOU_294690A; -.
DR VEuPathDB; ToxoDB:TGFOU_294690B; -.
DR VEuPathDB; ToxoDB:TGGT1_294690; -.
DR VEuPathDB; ToxoDB:TGMAS_294690; -.
DR VEuPathDB; ToxoDB:TGME49_294690; -.
DR VEuPathDB; ToxoDB:TGP89_294690; -.
DR VEuPathDB; ToxoDB:TGPRC2_294690; -.
DR VEuPathDB; ToxoDB:TGRH88_019690; -.
DR VEuPathDB; ToxoDB:TGRUB_294690A; -.
DR VEuPathDB; ToxoDB:TGRUB_294690B; -.
DR VEuPathDB; ToxoDB:TGVAND_294690; -.
DR VEuPathDB; ToxoDB:TGVEG_294690; -.
DR OMA; GPQEPKD; -.
DR BRENDA; 3.4.21.105; 6411.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR017092; Pept_S54_Rhomboid-like_Rom4/5.
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 PIRSF; PIRSF037023; Rhomboid-like_ROM4_ROM5; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Protease; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..841
FT /note="Rhomboid-like protease 5"
FT /id="PRO_0000239078"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 531
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 585
FT /evidence="ECO:0000250"
FT MUTAGEN 531
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15753289"
SQ SEQUENCE 841 AA; 92102 MW; 455856A0DB72BFFC CRC64;
MSSKGGSSRL GSKDLKKMTS RTERELRDSG RVRGEVERVE KRLRATAKVK EQPPTGDYKR
RALASPGETA APTFLVDSRG IPRKTSSTAP RKATLRPASS SPRLASSSRP TESTLPSSSS
RALQGASSSS SSRPRRLHES ASGRGGSGGS AGELRQEKKR LPELEAAEAA PASCVVELRD
VTARKGRTSP ATPPETAGSS VCGQGSHART AEKLEEGTAS HRDGSRRGSV DAETWATPGD
GSSSHEFESS PQREERMQPQ ETGRRELSSE PRSGDLTKNG GDGGPRRHSC AWRKWREHMI
QSFDITTHPF PPRGDGSPRR GKFLMIFLTS SVLFFVFLQE LVLNVTTFNG RCMSPVLYPS
HDAPESERTP RVISFGYGAC EHNLGVSLFR REETKKDPRG RWTPGPLTER CASGRCASDD
GWPSDLVQRG RAQRSPAAFD SPNPRVFSSL GALDTNKVRN YGEMFRVVWG MFLHGGWMHL
LLNVSCQAQT LWILEPAWGF LRTLSLWIVG GVSGSLLSAV ANPCTVTVGS SGAFYGLLGA
LVPFSIEYWD HIASPAWFLF CVSVLVMVAQ FGNMVGVQGV DNNAHLGGLI GGLLFGFATI
RSVHAFRWQG VAERMASSTL FWWMFPAEKR RSLREDNLQR VAREREERSS GRIPPPKFVW
KFRGHEREWC VRFAAAVGLV TFWSVLWLYL LVPSYYESLS SPPGNFSFLG STGCHCCRVQ
PFPGEEDKLP AFHPVRVNRG LFWCFVSEGV ANLFCGRSSA LNRGADVYGQ TRQFEEALGD
LPSARAGEAP LRIAKEEGES ASVWQRLVKS AKKTYNAVLG NTTTPAAPSA AELAQQTRAG
Q
