RHOM_DROME
ID RHOM_DROME Reviewed; 355 AA.
AC P20350; Q9W0F2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein rhomboid;
DE EC=3.4.21.105 {ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:21439629};
DE AltName: Full=Protein veinlet;
GN Name=rho; Synonyms=Ve; ORFNames=CG1004;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2110920; DOI=10.1101/gad.4.2.190;
RA Bier E., Jan L.Y., Jan Y.N.;
RT "Rhomboid, a gene required for dorsoventral axis establishment and
RT peripheral nervous system development in Drosophila melanogaster.";
RL Genes Dev. 4:190-203(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF TRP-151;
RP ARG-152; ASN-169; GLY-215; SER-217 AND HIS-281.
RX PubMed=11672525; DOI=10.1016/s0092-8674(01)00525-6;
RA Urban S., Lee J.R., Freeman M.;
RT "Drosophila Rhomboid-1 defines a family of putative intramembrane serine
RT proteases.";
RL Cell 107:173-182(2001).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-216 AND SER-217.
RX PubMed=21439629; DOI=10.1016/j.cell.2011.02.047;
RA Zettl M., Adrain C., Strisovsky K., Lastun V., Freeman M.;
RT "Rhomboid family pseudoproteases use the ER quality control machinery to
RT regulate intercellular signaling.";
RL Cell 145:79-91(2011).
CC -!- FUNCTION: Acts early in embryonic development to establish position
CC along the dorsoventral axis and then again later to specify the fate of
CC neuronal precursor cells. Involved in EGF receptor signaling; cleaves
CC Spitz to release the active growth factor.
CC {ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:21439629}.
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 Evidence={ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:21439629};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- DEVELOPMENTAL STAGE: Early blastoderm stages and later during nervous
CC development.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; X52454; CAA36692.1; -; mRNA.
DR EMBL; AE014296; AAF47496.1; -; Genomic_DNA.
DR PIR; A34597; A34597.
DR RefSeq; NP_001261255.1; NM_001274326.1.
DR RefSeq; NP_523883.2; NM_079159.3.
DR AlphaFoldDB; P20350; -.
DR BioGRID; 63708; 66.
DR IntAct; P20350; 1.
DR MINT; P20350; -.
DR STRING; 7227.FBpp0305409; -.
DR MEROPS; S54.001; -.
DR TCDB; 9.B.104.2.1; the rhomboid protease (rhomboid) family.
DR PaxDb; P20350; -.
DR EnsemblMetazoa; FBtr0072694; FBpp0072578; FBgn0004635.
DR EnsemblMetazoa; FBtr0333207; FBpp0305409; FBgn0004635.
DR GeneID; 38168; -.
DR KEGG; dme:Dmel_CG1004; -.
DR CTD; 6010; -.
DR FlyBase; FBgn0004635; rho.
DR VEuPathDB; VectorBase:FBgn0004635; -.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_048023_0_1_1; -.
DR InParanoid; P20350; -.
DR OMA; FLHANWF; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; P20350; -.
DR SignaLink; P20350; -.
DR BioGRID-ORCS; 38168; 0 hits in 3 CRISPR screens.
DR ChiTaRS; rho; fly.
DR GenomeRNAi; 38168; -.
DR PRO; PR:P20350; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004635; Expressed in mesectoderm and 75 other tissues.
DR ExpressionAtlas; P20350; baseline and differential.
DR Genevisible; P20350; DM.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0031902; C:late endosome membrane; IDA:FlyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0001752; P:compound eye photoreceptor fate commitment; IGI:FlyBase.
DR GO; GO:0035225; P:determination of genital disc primordium; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0038004; P:epidermal growth factor receptor ligand maturation; IDA:FlyBase.
DR GO; GO:0061331; P:epithelial cell proliferation involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0007436; P:larval salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IEP:FlyBase.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0090317; P:negative regulation of intracellular protein transport; IMP:FlyBase.
DR GO; GO:0007438; P:oenocyte development; IMP:FlyBase.
DR GO; GO:0001742; P:oenocyte differentiation; IMP:FlyBase.
DR GO; GO:0043703; P:photoreceptor cell fate determination; IGI:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IDA:FlyBase.
DR GO; GO:0042749; P:regulation of circadian sleep/wake cycle; IMP:FlyBase.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0048865; P:stem cell fate commitment; IMP:FlyBase.
DR GO; GO:0035202; P:tracheal pit formation in open tracheal system; IMP:FlyBase.
DR GO; GO:0035311; P:wing cell fate specification; IMP:FlyBase.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR017213; Peptidase_S54_rhomboid_met.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR PIRSF; PIRSF037470; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Golgi apparatus; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="Protein rhomboid"
FT /id="PRO_0000206179"
FT TOPO_DOM 1..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..275
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..355
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:11672525"
FT ACT_SITE 281
FT /evidence="ECO:0000305|PubMed:11672525"
FT MUTAGEN 151
FT /note="W->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11672525"
FT MUTAGEN 152
FT /note="R->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11672525"
FT MUTAGEN 169
FT /note="N->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11672525"
FT MUTAGEN 215
FT /note="G->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11672525"
FT MUTAGEN 216
FT /note="A->P: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:21439629"
FT MUTAGEN 217
FT /note="S->A,C,T: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11672525,
FT ECO:0000269|PubMed:21439629"
FT MUTAGEN 281
FT /note="H->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11672525"
FT CONFLICT 4
FT /note="L -> P (in Ref. 1; CAA36692)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="A -> V (in Ref. 1; CAA36692)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="S -> T (in Ref. 1; CAA36692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 39330 MW; 2E0572D08831C5D0 CRC64;
MENLTQNVNE TKVDLGQEKE KEASQEEEHA TAAKETIIDI PAACSSSSNS SSYDTDCSTA
SSTCCTRQGE HIYMQREAIP ATPLPESEDI GLLKYVHRQH WPWFILVISI IEIAIFAYDR
YTMPAQNFGL PVPIPSDSVL VYRPDRRLQV WRFFSYMFLH ANWFHLGFNI VIQLFFGIPL
EVMHGTARIG VIYMAGVFAG SLGTSVVDSE VFLVGASGGV YALLAAHLAN ITLNYAHMKS
ASTQLGSVVI FVSCDLGYAL YTQYFDGSAF AKGPQVSYIA HLTGALAGLT IGFLVLKNFG
HREYEQLIWW LALGVYCAFT VFAIVFNLIN TVTAQLMEEQ GEVITQHLLH DLGVS
