P20350 (RHOM_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein rhomboid
EC=3.4.21.105

Alternative name(s):
Protein veinlet

Gene names

Name:	rho
Synonyms:	Ve
ORF Names:	CG1004

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Developmental protein Hydrolase Protease Serine protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis 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 cell-cell adhesion Inferred from mutant phenotype PubMed 16831830. Source: FlyBase cytokinesis Inferred from mutant phenotype PubMed 12975351. 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 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 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 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW salivary gland boundary specification Non-traceable author statement PubMed 11598957. 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_component	Golgi 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 to membrane Inferred from sequence model Ref.4. Source: FlyBase plasma membrane Inferred from sequence or structural similarity Ref.1. Source: FlyBase
Molecular_function	serine-type endopeptidase activity Inferred from direct assay Ref.4. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 355	355	Protein rhomboid		PRO_0000206179
Regions
	Topological domain	1 – 98	98	Cytoplasmic Potential
	Transmembrane	99 – 119	21	Helical; Potential
	Topological domain	120 – 162	43	Lumenal Potential
	Transmembrane	163 – 183	21	Helical; Potential
	Topological domain	184 – 188	5	Cytoplasmic Potential
	Transmembrane	189 – 209	21	Helical; Potential
	Topological domain	210	1	Lumenal Potential
	Transmembrane	211 – 231	21	Helical; Potential
	Topological domain	232 – 244	13	Cytoplasmic Potential
	Transmembrane	245 – 265	21	Helical; Potential
	Topological domain	266 – 275	10	Lumenal Potential
	Transmembrane	276 – 296	21	Helical; Potential
	Topological domain	297 – 308	12	Cytoplasmic Potential
	Transmembrane	309 – 329	21	Helical; Potential
	Topological domain	330 – 355	26	Lumenal Potential
Sites
	Active site	217	1	Nucleophile
	Active site	281	1
Experimental info
	Mutagenesis	151	1	W → A: Abolishes protease activity. Ref.4
	Mutagenesis	152	1	R → A: Abolishes protease activity. Ref.4
	Mutagenesis	169	1	N → A: Abolishes protease activity. Ref.4
	Mutagenesis	215	1	G → A: Abolishes protease activity. Ref.4
	Mutagenesis	216	1	A → P: Abolishes protease activity. Ref.5
	Mutagenesis	217	1	S → A, C or T: Abolishes protease activity. Ref.4 Ref.5
	Mutagenesis	281	1	H → A: Abolishes protease activity. Ref.4
	Sequence conflict	4	1	L → P in CAA36692. Ref.1
	Sequence conflict	33	1	A → V in CAA36692. Ref.1
	Sequence conflict	46	1	S → T in CAA36692. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P20350 [UniParc]. Last modified March 5, 2002. Version 2. Checksum: 2E0572D08831C5D0	FASTA	355	39,330
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	A34597.
RefSeq	NP_001261255.1. NM_001274326.1. NP_523883.2. NM_079159.3.
UniGene	Dm.808.
3D structure databases
ProteinModelPortal	P20350.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4508920.
Protein family/group databases
MEROPS	S54.001.
Proteomic databases
PRIDE	P20350.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0072694; FBpp0072578; FBgn0004635. FBtr0333207; FBpp0305409; FBgn0004635.
GeneID	38168.
KEGG	dme:Dmel_CG1004.
Organism-specific databases
CTD	6010.
FlyBase	FBgn0004635. rho.
Phylogenomic databases
eggNOG	NOG300180.
GeneTree	ENSGT00390000005726.
InParanoid	P20350.
KO	K02857.
OMA	MHGTARI.
OrthoDB	EOG4X3FGZ.
PhylomeDB	P20350.
Gene expression databases
Bgee	P20350.
GermOnline	CG1004. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002610. Peptidase_S54_rhomboid. IPR022764. Peptidase_S54_rhomboid_dom. IPR017213. Peptidase_S54_rhomboid_met. [Graphical view]
PANTHER	PTHR22936. PTHR22936. 1 hit.
Pfam	PF01694. Rhomboid. 1 hit. [Graphical view]
PIRSF	PIRSF037470. Rhomboid. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	RHO. drosophila.
GenomeRNAi	38168.
NextBio	807306.

Entry information

Entry name

RHOM_DROME

Accession

Primary (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:	April 3, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project