RHDF1_RAT
ID RHDF1_RAT Reviewed; 856 AA.
AC Q499S9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Inactive rhomboid protein 1;
DE Short=iRhom1;
DE AltName: Full=Rhomboid family member 1;
GN Name=Rhbdf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC099777; AAH99777.1; -; mRNA.
DR RefSeq; NP_001025205.1; NM_001030034.1.
DR RefSeq; XP_008765802.1; XM_008767580.1.
DR RefSeq; XP_017452723.1; XM_017597234.1.
DR RefSeq; XP_017452724.1; XM_017597235.1.
DR AlphaFoldDB; Q499S9; -.
DR STRING; 10116.ENSRNOP00000027965; -.
DR GlyGen; Q499S9; 1 site.
DR iPTMnet; Q499S9; -.
DR PhosphoSitePlus; Q499S9; -.
DR PaxDb; Q499S9; -.
DR PRIDE; Q499S9; -.
DR Ensembl; ENSRNOT00000027965; ENSRNOP00000027965; ENSRNOG00000020594.
DR GeneID; 303008; -.
DR KEGG; rno:303008; -.
DR UCSC; RGD:1305075; rat.
DR CTD; 64285; -.
DR RGD; 1305075; Rhbdf1.
DR eggNOG; KOG2290; Eukaryota.
DR GeneTree; ENSGT00940000156278; -.
DR HOGENOM; CLU_011531_1_1_1; -.
DR InParanoid; Q499S9; -.
DR OMA; GGTENMA; -.
DR OrthoDB; 1253228at2759; -.
DR PhylomeDB; Q499S9; -.
DR TreeFam; TF312988; -.
DR PRO; PR:Q499S9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000020594; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q499S9; RN.
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: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 GO; GO:0050708; P:regulation of protein secretion; ISO:RGD.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Growth factor binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..856
FT /note="Inactive rhomboid protein 1"
FT /id="PRO_0000340110"
FT TOPO_DOM 1..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..656
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..715
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..773
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..856
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..20
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 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96CC6"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 97262 MW; B62626B0AD0B131B CRC64;
MSEARRDSTS SLQRKKPPWL KLDIPAVVPP AAEEPSFLQP LRRQAFLRSV SMPAETARVP
SPHHEPRRLA LQRQTSITQT IRRGTADWFG VSKDSDSTQK WQRKSIRHCS QRYGKLKPQV
IRELDLPSQD NVSLTSTETP PPLYVGPCQL GMQKIIDPLA RGRAFRMADD TADGLSAPHT
PVTPGAASLC SFSSSRSGFN RLPRRRKRES VAKMSFRAAA ALVKGRSIRD GTLRRGQRRS
FTPASFLEED MVDFPDELDT SFFAREGVLH EELSTYPDEV FESPSEAALK DWEKAPDQAD
LTGGALDRSE LERSHLMLPL ERGWRKQKEG GTLAPQPKVR LRQEVVSAAG PRRGQRIAVP
VRKLFAREKR PYGLGMVGRL TNRTYRKRID SYVKRQIEDM DDHRPFFTYW LTFVHSLVTI
LAVCIYGIAP VGFSQHETVD SVLRKRGVYE NVKYVQQENF WIGPSSEALI HLGAKFSPCM
RQDPQVHNFI LAAREREKHS ACCVRNDRSG CVQTSKEECS STLAVWVKWP VHPSAPDLAG
NKRQFGSVCH QDPRVCDEPS SEDPHEWPED ITKWPICTKN SAGNHTNHPH MDCVITGRPC
CIGTKGRCEI TSREYCDFMK GYFHEEATLC SQVHCMDDVC GLLPFLNPEV PDQFYRLWLS
LFLHAGILHC LVSVCFQMTV LRDLEKLAGW HRIAIIYLLS GVTGNLASAI FLPYRAEVGP
AGSQFGILAC LFVELFQSWQ ILARPWRAFF KLLAVVLFLF AFGLLPWIDN FAHISGFVSG
LFLSFAFLPY ISFGKFDLYR KRCQIIIFQA VFLGLLAGLV VLFYFYPVRC EWCEFLTCIP
FTDKFCEKYE LDAQLH
