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Q6GV23 (RHBL5_TOXGO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhomboid-like protease 5

EC=3.4.21.105
Alternative name(s):
Microneme protein protease 1
Short name=MPP-1
Gene names
Name:ROM5
Synonyms:MPP1
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length841 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease involved in intramembrane proteolysis. Cleaves microneme adhesins, such as MIC2. This step is essential for efficient invasion of host cells. Catalyzes intramembrane proteolysis of AMA1. Ref.2 Ref.3

Catalytic activity

Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.

Subcellular location

Membrane; Multi-pass membrane protein. Note: Detected primarily at the posterior surface of intracellular tachyzoites. Detected in patches on the cell surface of extracellular tachyzoites. Concentrated at the posterior end of tachyzoites after induction of microneme secretion prior to invasion of host cells. Ref.2

Developmental stage

Highly expressed in tachyzoites. Detected at low levels in bradyzoites and sporozoites. Ref.2

Sequence similarities

Belongs to the peptidase S54 family.

Sequence caution

The sequence AAT84606.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 841841Rhomboid-like protease 5
PRO_0000239078

Regions

Transmembrane323 – 34321Helical; Potential
Transmembrane464 – 48421Helical; Potential
Transmembrane492 – 51221Helical; Potential
Transmembrane526 – 54621Helical; Potential
Transmembrane571 – 59020Helical; Potential
Transmembrane673 – 69321Helical; Potential
Compositional bias99 – 15052Ser-rich

Sites

Active site5311Nucleophile By similarity
Active site5851 By similarity

Experimental info

Mutagenesis5311S → A: Loss of activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6GV23 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 455856A0DB72BFFC

FASTA84192,102
        10         20         30         40         50         60 
MSSKGGSSRL GSKDLKKMTS RTERELRDSG RVRGEVERVE KRLRATAKVK EQPPTGDYKR 

        70         80         90        100        110        120 
RALASPGETA APTFLVDSRG IPRKTSSTAP RKATLRPASS SPRLASSSRP TESTLPSSSS 

       130        140        150        160        170        180 
RALQGASSSS SSRPRRLHES ASGRGGSGGS AGELRQEKKR LPELEAAEAA PASCVVELRD 

       190        200        210        220        230        240 
VTARKGRTSP ATPPETAGSS VCGQGSHART AEKLEEGTAS HRDGSRRGSV DAETWATPGD 

       250        260        270        280        290        300 
GSSSHEFESS PQREERMQPQ ETGRRELSSE PRSGDLTKNG GDGGPRRHSC AWRKWREHMI 

       310        320        330        340        350        360 
QSFDITTHPF PPRGDGSPRR GKFLMIFLTS SVLFFVFLQE LVLNVTTFNG RCMSPVLYPS 

       370        380        390        400        410        420 
HDAPESERTP RVISFGYGAC EHNLGVSLFR REETKKDPRG RWTPGPLTER CASGRCASDD 

       430        440        450        460        470        480 
GWPSDLVQRG RAQRSPAAFD SPNPRVFSSL GALDTNKVRN YGEMFRVVWG MFLHGGWMHL 

       490        500        510        520        530        540 
LLNVSCQAQT LWILEPAWGF LRTLSLWIVG GVSGSLLSAV ANPCTVTVGS SGAFYGLLGA 

       550        560        570        580        590        600 
LVPFSIEYWD HIASPAWFLF CVSVLVMVAQ FGNMVGVQGV DNNAHLGGLI GGLLFGFATI 

       610        620        630        640        650        660 
RSVHAFRWQG VAERMASSTL FWWMFPAEKR RSLREDNLQR VAREREERSS GRIPPPKFVW 

       670        680        690        700        710        720 
KFRGHEREWC VRFAAAVGLV TFWSVLWLYL LVPSYYESLS SPPGNFSFLG STGCHCCRVQ 

       730        740        750        760        770        780 
PFPGEEDKLP AFHPVRVNRG LFWCFVSEGV ANLFCGRSSA LNRGADVYGQ TRQFEEALGD 

       790        800        810        820        830        840 
LPSARAGEAP LRIAKEEGES ASVWQRLVKS AKKTYNAVLG NTTTPAAPSA AELAQQTRAG 


Q 

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References

[1]"Host cell invasion by the apicomplexans: the significance of microneme protein proteolysis."
Dowse T., Soldati D.
Curr. Opin. Microbiol. 7:388-396(2004) [PubMed: 15358257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: RH.
[2]"A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma."
Brossier F., Jewett T.J., Sibley L.D., Urban S.
Proc. Natl. Acad. Sci. U.S.A. 102:4146-4151(2005) [PubMed: 15753289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-841, FUNCTION, MUTAGENESIS OF SER-531, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[3]"Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii."
Opitz C., Di Cristina M., Reiss M., Ruppert T., Crisanti A., Soldati D.
EMBO J. 21:1577-1585(2002) [PubMed: 11927542] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY634626 mRNA. Translation: AAT47708.1.
AY587208 mRNA. Translation: AAT84606.1. Different initiation.

3D structure databases

ProteinModelPortalQ6GV23.
ModBaseSearch...

Protein family/group databases

MEROPSS54.023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR017092. Pept_S54_Rhomboid-like_Rom4/5.
IPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
[Graphical view]
PANTHERPTHR22936. Peptidase_S54_rhomboid. 1 hit.
PfamPF01694. Rhomboid. 1 hit.
[Graphical view]
PIRSFPIRSF037023. Rhomboid-like_ROM4_ROM5. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRHBL5_TOXGO
AccessionPrimary (citable) accession number: Q6GV23
Secondary accession number(s): Q696L8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 19, 2004
Last modified: November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families