RHBL4_TOXGO
ID RHBL4_TOXGO Reviewed; 641 AA.
AC Q695T8; Q66TP4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Rhomboid-like protease 4;
DE EC=3.4.21.105;
GN Name=ROM4;
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].
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], ABSENCE OF PROTEASE ACTIVITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=RH; TISSUE=Tachyzoite;
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: Putative serine protease involved in intramembrane
CC proteolysis and the subsequent release of polypeptides from their
CC membrane anchors. {ECO:0000250}.
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=Uniformly
CC distributed at the surface of intracellular and extracellular
CC tachyzoites.
CC -!- DEVELOPMENTAL STAGE: Detected in tachyzoites and in bradyzoites.
CC {ECO:0000269|PubMed:15753289}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
CC -!- CAUTION: Has no detectable protease activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU11320.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY596193; AAT29067.1; -; mRNA.
DR EMBL; AY704175; AAU11320.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q695T8; -.
DR MEROPS; S54.022; -.
DR VEuPathDB; ToxoDB:TGARI_268590; -.
DR VEuPathDB; ToxoDB:TGCAST_268590; -.
DR VEuPathDB; ToxoDB:TGCOUG_268590; -.
DR VEuPathDB; ToxoDB:TGDOM2_268590; -.
DR VEuPathDB; ToxoDB:TGFOU_268590; -.
DR VEuPathDB; ToxoDB:TGGT1_268590; -.
DR VEuPathDB; ToxoDB:TGMAS_268590; -.
DR VEuPathDB; ToxoDB:TGME49_268590; -.
DR VEuPathDB; ToxoDB:TGP89_268590; -.
DR VEuPathDB; ToxoDB:TGPRC2_268590; -.
DR VEuPathDB; ToxoDB:TGRH88_082680; -.
DR VEuPathDB; ToxoDB:TGRUB_268590; -.
DR VEuPathDB; ToxoDB:TGVAND_268590; -.
DR VEuPathDB; ToxoDB:TGVEG_268590; -.
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:0060352; P:cell adhesion molecule production; IMP:CACAO.
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 2: Evidence at transcript level;
KW Hydrolase; Membrane; Protease; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..641
FT /note="Rhomboid-like protease 4"
FT /id="PRO_0000239077"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 460
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="T -> A (in Ref. 2; AAU11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="K -> R (in Ref. 2; AAU11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="V -> VV (in Ref. 2; AAU11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="G -> D (in Ref. 2; AAU11320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 69660 MW; FD2B10DBD6872DC1 CRC64;
MVWTSAVVMA SPHGSASRAG SNRRTDGLSV NLGQDNTLKH DTPTETAPSA SPPRVAPAPI
PPKGGPAATP GKDGALDNRG SHDSVPPVAV AIPGREEVNA TASQKSVVAG ANSQPTPGTQ
SSKAPASDVD GSSKHGSPEH PDAGSPEVNA EGVPVEEALQ AIGDDDPLIH NLPDGVVGRR
APANPFNSSM YAKLRGKKKK HRPKVRDPKL NNNPLRGRLV VCISTTALLC WIYMWELIYN
FTSFNGRCVS PVMYPDYKLQ EAKQRQPYVI RYGYGGCEYN LGSLAYPRAS FGTSAGDKGW
PVDLVPNGSA GSAATSWDSP NARVLRHLGG LETNYIREYS ETFRLFTSMY MHGGWLHILI
NLSCQIQILW IIEPDWGFLR TTLLFFLGGI SGNLLSAVAD PCSITVGSSG SMYALLGALI
PYCVEYWKSI PRPGCILVFM IVVIIGILTG MAGFTDNYAH MGGALGGILW GFASITTVSA
CDKCTLGERM AMTPPFSWCV PKATQQKLLE RAKARKAEAI RRRKLQAIQK KKAGGARGKA
MYAVKMRLQE EGRPPCKMSF REWVIRGLCA AALFAYWLIL FLYLLDPSLY KSYSPPGQLK
FSGWLYCKCG TIVYQAPQTY GNLGRFWCFG SEKDAQYYLE P
