RHOM2_CAEEL
ID RHOM2_CAEEL Reviewed; 435 AA.
AC P34356;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Inactive rhomboid-related protein 2 {ECO:0000305};
GN Name=rom-2 {ECO:0000303|PubMed:15455032, ECO:0000312|WormBase:C48B4.2};
GN ORFNames=C48B4.2 {ECO:0000312|WormBase:C48B4.2};
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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 [3]
RP 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: Probable inactive serine protease.
CC {ECO:0000303|PubMed:15455032}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not affect vulva
CC development. Does not suppress 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}.
CC -!- CAUTION: Although it belongs to the S54 peptidase family, the active
CC site Ser-235 is replaced by an alanine residue, suggesting that it has
CC no serine peptidase activity. {ECO:0000305}.
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DR EMBL; BX284603; CAA82377.2; -; Genomic_DNA.
DR PIR; S40723; S40723.
DR RefSeq; NP_499120.2; NM_066719.2.
DR AlphaFoldDB; P34356; -.
DR STRING; 6239.C48B4.2; -.
DR PaxDb; P34356; -.
DR EnsemblMetazoa; C48B4.2.1; C48B4.2.1; WBGene00004401.
DR UCSC; C48B4.2; c. elegans.
DR WormBase; C48B4.2; CE37757; WBGene00004401; rom-2.
DR eggNOG; KOG2289; Eukaryota.
DR GeneTree; ENSGT00940000166075; -.
DR HOGENOM; CLU_048023_1_1_1; -.
DR InParanoid; P34356; -.
DR OMA; RILWWIC; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; P34356; -.
DR PRO; PR:P34356; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004401; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR Pfam; PF01694; Rhomboid; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..435
FT /note="Inactive rhomboid-related protein 2"
FT /id="PRO_0000206181"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..49
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 435 AA; 49635 MW; 68819D8DD6DFFCCB CRC64;
MDDKWRESAP VNDIEASSWI RIFRAFDTDH DGLIQCEEMQ KTIRDSTYSF GFDHYELQKM
SLYLEMREGK PVDFADFCYL MSKCKGYRLR EYLFRAALTV TPKNQRIHVF SELQRYKCVP
PPIFLIFLSI VQLAFYLYYV VDSSEGVWLS GPIPTMSPLI VSQYHLPELW RLFTYCLINV
GIFHIIFNIL IQLAIGVPLE LVHRWRIYIL YFMGVLFGSI LSLALDPTVF LCGGAAGSFS
LIASHITTIA TNFKEMENAT CRLPILIVFA ALDYVLAVYQ RFFAPRIDKV SMYGHLGGLV
AGILFTFILF RGSKPSRFYT VSFWVSLVLS GFFIAICITL IAAPRTTVQE IIKNQSFKNN
ATRCSVQIGI NCISWTSNFL IFDHIFHVSY SHVLLISNAV SNSLYPTTSP PSILIVLCSS
PGFPILSMGF PLYKY
