RHBL2_MOUSE
ID RHBL2_MOUSE Reviewed; 302 AA.
AC A2AGA4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Rhomboid-related protein 2;
DE Short=RRP2;
DE EC=3.4.21.105;
DE Contains:
DE RecName: Full=Rhomboid-related protein 2, N-terminal fragment;
DE Short=NTF;
DE Contains:
DE RecName: Full=Rhomboid-related protein 2, C-terminal fragment;
DE Short=CTF;
GN Name=Rhbdl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-185 AND SER-186.
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: Involved in regulated intramembrane proteolysis and the
CC subsequent release of functional polypeptides from their membrane
CC anchors. Known substrate: EFNB3 (By similarity). {ECO:0000250}.
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:21439629};
CC -!- SUBCELLULAR LOCATION: [Rhomboid-related protein 2, C-terminal
CC fragment]: Cell membrane {ECO:0000250|UniProtKB:Q9NX52}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: Proteolytic processing of the proenzyme produces an N- and a C-
CC terminal fragment. The processing is required for activation of the
CC protease (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; AL683811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38873.1; -.
DR RefSeq; NP_898986.2; NM_183163.2.
DR RefSeq; XP_006503088.1; XM_006503025.3.
DR AlphaFoldDB; A2AGA4; -.
DR BioGRID; 231007; 1.
DR STRING; 10090.ENSMUSP00000054546; -.
DR MEROPS; S54.002; -.
DR PhosphoSitePlus; A2AGA4; -.
DR PaxDb; A2AGA4; -.
DR PRIDE; A2AGA4; -.
DR ProteomicsDB; 253268; -.
DR Antibodypedia; 31843; 96 antibodies from 24 providers.
DR DNASU; 230726; -.
DR Ensembl; ENSMUST00000053202; ENSMUSP00000054546; ENSMUSG00000043333.
DR Ensembl; ENSMUST00000106204; ENSMUSP00000101810; ENSMUSG00000043333.
DR GeneID; 230726; -.
DR KEGG; mmu:230726; -.
DR UCSC; uc008upx.1; mouse.
DR CTD; 54933; -.
DR MGI; MGI:3608413; Rhbdl2.
DR VEuPathDB; HostDB:ENSMUSG00000043333; -.
DR eggNOG; KOG2289; Eukaryota.
DR GeneTree; ENSGT00940000159442; -.
DR HOGENOM; CLU_048023_0_0_1; -.
DR InParanoid; A2AGA4; -.
DR OMA; VCCDQLM; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; A2AGA4; -.
DR TreeFam; TF313540; -.
DR BioGRID-ORCS; 230726; 1 hit in 74 CRISPR screens.
DR PRO; PR:A2AGA4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AGA4; protein.
DR Bgee; ENSMUSG00000043333; Expressed in lobe of prostate and 105 other tissues.
DR Genevisible; A2AGA4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP: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 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Rhomboid-related protein 2"
FT /id="PRO_0000408511"
FT CHAIN 1..?
FT /note="Rhomboid-related protein 2, N-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000408512"
FT CHAIN ?..302
FT /note="Rhomboid-related protein 2, C-terminal fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000408513"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Nucleophile"
FT ACT_SITE 249
FT /evidence="ECO:0000305"
FT MUTAGEN 185
FT /note="A->P: Reduces protease activity."
FT /evidence="ECO:0000269|PubMed:21439629"
FT MUTAGEN 186
FT /note="S->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:21439629"
SQ SEQUENCE 302 AA; 33735 MW; 3623D9206D486C57 CRC64;
MAVAHEMEME SVNLNMEREG KEEPEEEKMK GNGEGKDFPR SRKVHRIVSK WMLPEPVRRT
YLERANCLPP PLFIILISLA ELAVFIYYAV WKPQKQWITL DTGILESPLT YCPEKREEAW
RFISYMLVHA GVQHIVGNLL MQIVLGIPLE MVHKGLRVGL VYLAGVLAGS LASSIFDPLK
SLVGASGGVY ALMGGYFMNV IVNFREMIPA FGIVRLLVII LIVASDMGFA LYRRFFVPAN
GSPVSFAAHI AGGFAGMSIG YTVFSCFDKT LLKDPRFWIA IAAYVACLLF AVFFNIFLSP
AN
