RHDF1_PAPAN
ID RHDF1_PAPAN Reviewed; 855 AA.
AC A9L8T6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Inactive rhomboid protein 1;
DE Short=iRhom1;
DE AltName: Full=Rhomboid family member 1;
GN Name=RHBDF1;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
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 (NOV-2007) 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; DP000504; ABX52099.1; -; Genomic_DNA.
DR RefSeq; NP_001162285.1; NM_001168814.1.
DR AlphaFoldDB; A9L8T6; -.
DR STRING; 9555.ENSPANP00000010197; -.
DR MEROPS; S54.952; -.
DR GeneID; 100137277; -.
DR CTD; 64285; -.
DR eggNOG; KOG2290; Eukaryota.
DR HOGENOM; CLU_011531_1_1_1; -.
DR OMA; GGTENMA; -.
DR OrthoDB; 1253228at2759; -.
DR Proteomes; UP000028761; Unplaced.
DR Bgee; ENSPANG00000000422; Expressed in lateral hypothalamic nucleus and 66 other tissues.
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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..855
FT /note="Inactive rhomboid protein 1"
FT /id="PRO_0000340109"
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; 97389 MW; 371C5B33C26483B4 CRC64;
MSEARRDSTS SLQRKKPPWL KLDIPSAVPP TAEEPSFLQP LRRQAFLRSV SMPAETAHIS
SPHHELRRSV LQRQTSITQT IRRGTADWFG VSKDSDSTQK WQRKSIRHCS QRYGKLKPQV
LRELDLPSQD NVSLTSTETP PPLYVGPCQL GMQKIIDPLA RGRAFRVADD TAEGLSAPHT
PVTPGAASLC SFSSSRSGFH RLPRRRKRES VAKMSFRAAA ALMKGRSVRD GTLRRAQRRS
FTPASFLEED TTDFPDELDT SFFAREGILH EELSTYPDEV FESPSEAALK DWEKAPEQAD
LTGGALDRSE LERSHLMLPL ERGWRKQKEG AAAPQPKVRL RQEVVSTAGP RRGQRIAVPV
RKLFAREKRP YGLGMVGRLT NRTYRKRIDS FVKRQIEDMD DHRPFFTYWL TFVHSLVTIL
AVCIYGIAPV GFSQHETVDS VLRNRGVYEN VKYVQQENFW IGPSSEALIH LGAKFSPCMR
QDPQVHSFIR SAREREKHSA CCVRNDRSGC VQTSEEECSS TLAVWVKWPI HPSAPELAGH
KRQFGSVCHQ DPRVCDEPSS EDPHEWPEDI TKWPICTKNS AGNHTNHPHM DCVITGRPCC
IGTKGRCEIT SREYCDFMRG YFHEEATLCS QVHCMDDVCG LLPFLNPEVP DQFYRLWLSL
FLHAGILHCL VSICFQMTVL RDLEKLAGWH RIAIIYLLSG VTGNLASAIF LPYRAEVGPA
GSQFGILACL FVELFQSWQI LARPWRAFFK LLAVVLFLFT FGLLPWIDNF AHISGFISGL
FLSFAFLPYI SFGKFDLYRK RCQIIIFQVV FLGLLAGLVV LFYFYPVRCE WCEFLTCIPF
TDKFCEKYEL DAQLH
