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P20350 (RHOM_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Protein rhomboid

EC=3.4.21.105
Alternative name(s):
Protein veinlet
Gene names
Name:rho
Synonyms:Ve
ORF Names:CG1004
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts early in embryonic development to establish position along the dorsoventral axis and then again later to specify the fate of neuronal precursor cells. Involved in EGF receptor signaling; cleaves Spitz to release the active growth factor. Ref.4 Ref.5

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

Golgi apparatus membrane; Multi-pass membrane protein.

Developmental stage

Early blastoderm stages and later during nervous development.

Sequence similarities

Belongs to the peptidase S54 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Hydrolase
Protease
Serine protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from mutant phenotype PubMed 17164414. Source: FlyBase

behavioral response to ethanol

Inferred from mutant phenotype PubMed 18435628PubMed 19464045. Source: FlyBase

brain development

Inferred from mutant phenotype PubMed 12646129. Source: FlyBase

branched duct epithelial cell fate determination, open tracheal system

Traceable author statement PubMed 10684581. Source: FlyBase

determination of genital disc primordium

Inferred from mutant phenotype PubMed 15893978. Source: FlyBase

epidermal growth factor receptor signaling pathway

Traceable author statement PubMed 9631645. Source: FlyBase

epithelial cell proliferation involved in Malpighian tubule morphogenesis

Inferred from mutant phenotype PubMed 9637680. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 16648592. Source: FlyBase

imaginal disc-derived wing vein morphogenesis

Inferred from mutant phenotype PubMed 15766758PubMed 16299391PubMed 16308331. Source: FlyBase

imaginal disc-derived wing vein specification

Inferred from mutant phenotype PubMed 11023875PubMed 16308331. Source: FlyBase

larval salivary gland morphogenesis

Inferred from mutant phenotype PubMed 19064711. Source: FlyBase

learning or memory

Inferred from mutant phenotype PubMed 12593794. Source: FlyBase

leg disc proximal/distal pattern formation

Traceable author statement PubMed 12181552. Source: FlyBase

maintenance of epithelial integrity, open tracheal system

Inferred from mutant phenotype PubMed 16831830. Source: FlyBase

morphogenesis of a branching structure

Non-traceable author statement PubMed 11063940. Source: FlyBase

negative regulation of gene expression

Inferred from mutant phenotype PubMed 11023875. Source: FlyBase

oenocyte development

Inferred from mutant phenotype PubMed 12050142. Source: FlyBase

olfactory learning

Inferred from mutant phenotype PubMed 12593794. Source: FlyBase

open tracheal system development

Traceable author statement PubMed 11063940PubMed 11598957PubMed 12791296PubMed 14570584PubMed 14624839. Source: FlyBase

ovarian follicle cell development

Traceable author statement PubMed 10822261. Source: FlyBase

peptide bond cleavage involved in epidermal growth factor receptor ligand maturation

Inferred from genetic interaction PubMed 11672524Ref.4. Source: FlyBase

peripheral nervous system development

Traceable author statement PubMed 8060613. Source: FlyBase

positive regulation of epidermal growth factor receptor signaling pathway

Traceable author statement PubMed 10449356. Source: FlyBase

regulation of epidermal growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.5. Source: UniProtKB

salivary gland boundary specification

Non-traceable author statement PubMed 11598957. Source: FlyBase

salivary gland development

Traceable author statement PubMed 12742168. Source: FlyBase

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 16831830. Source: FlyBase

stem cell fate commitment

Inferred from mutant phenotype PubMed 20463031. Source: FlyBase

tracheal pit formation in open tracheal system

Traceable author statement PubMed 12791296PubMed 14570584. Source: FlyBase

wing cell fate specification

Inferred from mutant phenotype PubMed 16308331. Source: FlyBase

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11672524Ref.4. Source: FlyBase

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

apical part of cell

Inferred from direct assay PubMed 20957186. Source: FlyBase

integral component of membrane

Inferred from sequence model Ref.4. Source: FlyBase

plasma membrane

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

   Molecular_functionserine-type endopeptidase activity

Inferred from direct assay Ref.4. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Protein rhomboid
PRO_0000206179

Regions

Topological domain1 – 9898Cytoplasmic Potential
Transmembrane99 – 11921Helical; Potential
Topological domain120 – 16243Lumenal Potential
Transmembrane163 – 18321Helical; Potential
Topological domain184 – 1885Cytoplasmic Potential
Transmembrane189 – 20921Helical; Potential
Topological domain2101Lumenal Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 24413Cytoplasmic Potential
Transmembrane245 – 26521Helical; Potential
Topological domain266 – 27510Lumenal Potential
Transmembrane276 – 29621Helical; Potential
Topological domain297 – 30812Cytoplasmic Potential
Transmembrane309 – 32921Helical; Potential
Topological domain330 – 35526Lumenal Potential

Sites

Active site2171Nucleophile
Active site2811

Experimental info

Mutagenesis1511W → A: Abolishes protease activity. Ref.4
Mutagenesis1521R → A: Abolishes protease activity. Ref.4
Mutagenesis1691N → A: Abolishes protease activity. Ref.4
Mutagenesis2151G → A: Abolishes protease activity. Ref.4
Mutagenesis2161A → P: Abolishes protease activity. Ref.5
Mutagenesis2171S → A, C or T: Abolishes protease activity. Ref.4 Ref.5
Mutagenesis2811H → A: Abolishes protease activity. Ref.4
Sequence conflict41L → P in CAA36692. Ref.1
Sequence conflict331A → V in CAA36692. Ref.1
Sequence conflict461S → T in CAA36692. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P20350 [UniParc].

Last modified March 5, 2002. Version 2.
Checksum: 2E0572D08831C5D0

FASTA35539,330
        10         20         30         40         50         60 
MENLTQNVNE TKVDLGQEKE KEASQEEEHA TAAKETIIDI PAACSSSSNS SSYDTDCSTA 

        70         80         90        100        110        120 
SSTCCTRQGE HIYMQREAIP ATPLPESEDI GLLKYVHRQH WPWFILVISI IEIAIFAYDR 

       130        140        150        160        170        180 
YTMPAQNFGL PVPIPSDSVL VYRPDRRLQV WRFFSYMFLH ANWFHLGFNI VIQLFFGIPL 

       190        200        210        220        230        240 
EVMHGTARIG VIYMAGVFAG SLGTSVVDSE VFLVGASGGV YALLAAHLAN ITLNYAHMKS 

       250        260        270        280        290        300 
ASTQLGSVVI FVSCDLGYAL YTQYFDGSAF AKGPQVSYIA HLTGALAGLT IGFLVLKNFG 

       310        320        330        340        350 
HREYEQLIWW LALGVYCAFT VFAIVFNLIN TVTAQLMEEQ GEVITQHLLH DLGVS 

« Hide

References

« Hide 'large scale' references
[1]"Rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster."
Bier E., Jan L.Y., Jan Y.N.
Genes Dev. 4:190-203(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases."
Urban S., Lee J.R., Freeman M.
Cell 107:173-182(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-151; ARG-152; ASN-169; GLY-215; SER-217 AND HIS-281.
[5]"Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling."
Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.
Cell 145:79-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-216 AND SER-217.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52454 mRNA. Translation: CAA36692.1.
AE014296 Genomic DNA. Translation: AAF47496.1.
PIRA34597.
RefSeqNP_001261255.1. NM_001274326.1.
NP_523883.2. NM_079159.3.
UniGeneDm.808.

3D structure databases

ProteinModelPortalP20350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid63708. 27 interactions.
IntActP20350. 1 interaction.
MINTMINT-4508920.

Protein family/group databases

MEROPSS54.001.
TCDB9.B.104.2.1. the rhomboid protease (rhomboid) family.

Proteomic databases

PRIDEP20350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072694; FBpp0072578; FBgn0004635.
FBtr0333207; FBpp0305409; FBgn0004635.
GeneID38168.
KEGGdme:Dmel_CG1004.

Organism-specific databases

CTD6010.
FlyBaseFBgn0004635. rho.

Phylogenomic databases

eggNOGNOG300180.
InParanoidP20350.
KOK02857.
OMAELGFFTY.
OrthoDBEOG7SN8CK.
PhylomeDBP20350.

Enzyme and pathway databases

SignaLinkP20350.

Gene expression databases

BgeeP20350.

Family and domain databases

Gene3D1.20.1540.10. 1 hit.
InterProIPR002610. Peptidase_S54_rhomboid.
IPR022764. Peptidase_S54_rhomboid_dom.
IPR017213. Peptidase_S54_rhomboid_met.
[Graphical view]
PANTHERPTHR22936. PTHR22936. 1 hit.
PfamPF01694. Rhomboid. 1 hit.
[Graphical view]
PIRSFPIRSF037470. Rhomboid. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRHO. drosophila.
GenomeRNAi38168.
NextBio807306.
PROP20350.

Entry information

Entry nameRHOM_DROME
AccessionPrimary (citable) accession number: P20350
Secondary accession number(s): Q9W0F2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: March 5, 2002
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase