RHOM1_CAEEL
ID RHOM1_CAEEL Reviewed; 356 AA.
AC Q19821;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Rhomboid-related protein 1;
DE EC=3.4.21.105 {ECO:0000250|UniProtKB:P20350};
GN Name=rom-1 {ECO:0000303|PubMed:15455032, ECO:0000312|WormBase:F26F4.3};
GN ORFNames=F26F4.3 {ECO:0000312|WormBase:F26F4.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15455032; DOI=10.1371/journal.pbio.0020334;
RA Dutt A., Canevascini S., Froehli-Hoier E., Hajnal A.;
RT "EGF signal propagation during C. elegans vulval development mediated by
RT ROM-1 rhomboid.";
RL PLoS Biol. 2:E334-E334(2004).
CC -!- FUNCTION: Serine protease which activates lin-3 isoform a in the
CC proximal vulva precursor cells (VPC) during vulva development to
CC transmit the inductive anchor cell signal to the distal VPCs.
CC {ECO:0000269|PubMed:15455032}.
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:0000250|UniProtKB:P20350};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: In L1 larvae, expressed in vulval precursor cells
CC (VPCs) and Pn.a-derived neurons. In L2 larvae, uniformly expressed in
CC all VPCs. In L3 larvae, expression decreases in all VPCs except P6.p.
CC In L4 larvae, expression decreases in descendants of P5.p, P6.p and
CC P7.p while expression remains high in descendants of P3.p, P4.p and
CC P8.p. In L4 larvae, expressed in the anchor cell and other cells in the
CC somatic gonad. {ECO:0000269|PubMed:15455032}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not affect vulva
CC development. Partially suppresses ectopic vulva formation in a let-60
CC (n1046) gain-of-function mutant background.
CC {ECO:0000269|PubMed:15455032}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; BX284603; CCD65751.1; -; Genomic_DNA.
DR PIR; T16172; T16172.
DR RefSeq; NP_498029.2; NM_065628.2.
DR AlphaFoldDB; Q19821; -.
DR STRING; 6239.F26F4.3; -.
DR MEROPS; S54.013; -.
DR EPD; Q19821; -.
DR PaxDb; Q19821; -.
DR PeptideAtlas; Q19821; -.
DR EnsemblMetazoa; F26F4.3.1; F26F4.3.1; WBGene00004400.
DR GeneID; 184989; -.
DR KEGG; cel:CELE_F26F4.3; -.
DR UCSC; F26F4.3; c. elegans.
DR CTD; 184989; -.
DR WormBase; F26F4.3; CE32392; WBGene00004400; rom-1.
DR eggNOG; KOG2289; Eukaryota.
DR HOGENOM; CLU_048023_1_0_1; -.
DR InParanoid; Q19821; -.
DR OMA; IWRIGPI; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q19821; -.
DR SignaLink; Q19821; -.
DR PRO; PR:Q19821; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004400; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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:0040026; P:positive regulation of vulval development; IGI:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Hydrolase; Membrane; Protease; Reference proteome; Serine protease;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..356
FT /note="Rhomboid-related protein 1"
FT /id="PRO_0000206180"
FT TRANSMEM 107..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20350"
FT ACT_SITE 293
FT /evidence="ECO:0000250|UniProtKB:P20350"
SQ SEQUENCE 356 AA; 40633 MW; A43B5128B3CB2FB8 CRC64;
MFSSEGKFRK TYRHQFNQLR TGDETEIPMS TLASRIETRK IPLTNGQIHA IKEAPDELVD
IDGFQKIVTS KAAQRSTIKR IMYDMADPIM SDSQKIEVHS YIDSYSWCPP PIFMLLITII
QVGIFFFYWE SDGGRSIWTD CAGCFVHHNH TAPGIFIFAP KLRGEAWRFT SYMFLHAGLN
HLLGNVIIQL LVGIPLEVAH KIWRIGPIYL LAVTSGSLLQ YAIDPNSLLV GASAGVYALI
FAHVANVILN WHEMPLRWIR VLVLFVFIFL DFGGAIHRRF YTNDCDSVSH LAHIAGAVTG
LFFGYVVLYN VVEHRIEKII RYVCLFLYSA FFATTIIFVI VRQPYSKNLW NNENCS
