RHDF1_PLEMO
ID RHDF1_PLEMO Reviewed; 855 AA.
AC B1MT31;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Inactive rhomboid protein 1;
DE Short=iRhom1;
DE AltName: Full=Rhomboid family member 1;
GN Name=RHBDF1;
OS Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC Pitheciidae; Callicebinae; Plecturocebus.
OX NCBI_TaxID=9523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth
CC factor (EGF) receptor ligands and TNF, thereby plays a role in sleep,
CC cell survival, proliferation, migration and inflammation. Does not
CC exhibit any protease activity on its own.
CC {ECO:0000250|UniProtKB:Q96CC6}.
CC -!- SUBUNIT: Homodimer, or homooligomer. Interacts with TGFA and HBEGF.
CC Interacts with EGF; may retain EGF in the endoplasmic reticulum and
CC regulates its degradation through the endoplasmic reticulum-associated
CC degradation (ERAD). Interacts (via cytoplasmic N-terminus) with
CC FRMD8/iTAP; this interaction leads to mutual protein stabilization.
CC Interacts with ADAM17/TACE. {ECO:0000250|UniProtKB:Q96CC6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96CC6}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96CC6};
CC Multi-pass membrane protein {ECO:0000255}. Note=Predominantly localized
CC in the endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q96CC6}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; DP000617; ACA51068.1; -; Genomic_DNA.
DR AlphaFoldDB; B1MT31; -.
DR MEROPS; S54.952; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR Gene3D; 1.20.1540.10; -; 1.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR022241; Rhomboid_SP.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF12595; Rhomboid_SP; 1.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Growth factor binding; Membrane; Phosphoprotein; Protein transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..855
FT /note="Inactive rhomboid protein 1"
FT /id="PRO_0000340107"
FT TOPO_DOM 1..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..655
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..714
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..772
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..855
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CC6"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIX5"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIX5"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIX5"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CC6"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 855 AA; 97273 MW; 2193FD49AACDE070 CRC64;
MSEARRDSTS SLQRKKPPWL KLDIPSAAPP AAEEPSFLQP LRRQVFLRSV SMPAETAHIS
SPHCELRRPV LQRQTSITQT IRRGAADWFG VSKESESTQK WQRKSIRHCS QRYGKLKPQV
LRELDLPSQD NVSLTSTETP PPLYVGPCQL GMQKIIDPLA RGRAFRVADD AAEGLSAPHT
PVTPGAASLC SFSSSRSGFH RLPRRRKRES VAKMSFRAAA ALMKGRSVRD GTLRRAQRRS
FTPASFLEED TTDFPDELDT SFFAREGILH EELSTYPDEV FESPSEAALK DWEKAPEQAD
LTGGALDRSE LERSHLMLPL ERGWRKQKEG AAAPQPKVRL RQEVVSTAGP RRGQRIAVPV
RKLFAREKRP YGLGMVGRLT NRTYRKRIDS FVKRQIEDMD DHRPFFTYWL TFVHSLVTVL
AVCIYGIAPV GFSQHETVDS VLRNRGVYEN VKYVQQENFW IGPSSEALIH LGAKFSPCMR
QDPQVHSFIR AAREREKHSA CCVRNDRSGC VQTSEEECSS TLAVWVKWPV HPSAPELAGH
KRQFGSVCHQ DPRVCDEPSS EDPHEWPEDI TRWPICTKNS AGNHTNHPHM DCVITGRPCC
IGTKGRCEIT SREYCDFMRG YFHEEATLCS QVHCMDDVCG LLPFLNPEVP DQFYRLWLSL
FLHAGILHCL VSICFQMTVL RDLEKLAGWH RIAIIYLLSG VTGNLASAIF LPYRAEVGPA
GSQFGILACL FVELFQSWQI LARPWRAFFK LLAVVLFLFT FGLLPWIDNF AHISGFISGL
FLSFAFLPYI SFGKFDLYRK RCQIIVFQVV FLGLLAGLVV LFYFYPVRCE WCEFLTCIPF
TDKFCEKYEL DAQLH
