RHDF1_BOVIN
ID RHDF1_BOVIN Reviewed; 856 AA.
AC A7YWH9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Inactive rhomboid protein 1;
DE Short=iRhom1;
DE AltName: Full=Rhomboid family member 1;
GN Name=RHBDF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-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; BC134588; AAI34589.1; -; mRNA.
DR RefSeq; NP_001098870.1; NM_001105400.1.
DR RefSeq; XP_010799092.1; XM_010800790.1.
DR RefSeq; XP_010799093.1; XM_010800791.2.
DR RefSeq; XP_015313883.1; XM_015458397.1.
DR RefSeq; XP_015313933.1; XM_015458447.1.
DR AlphaFoldDB; A7YWH9; -.
DR STRING; 9913.ENSBTAP00000026388; -.
DR MEROPS; S54.952; -.
DR PaxDb; A7YWH9; -.
DR Ensembl; ENSBTAT00000026388; ENSBTAP00000026388; ENSBTAG00000019805.
DR Ensembl; ENSBTAT00000085540; ENSBTAP00000063017; ENSBTAG00000019805.
DR GeneID; 529167; -.
DR KEGG; bta:529167; -.
DR CTD; 64285; -.
DR VEuPathDB; HostDB:ENSBTAG00000019805; -.
DR VGNC; VGNC:33933; RHBDF1.
DR eggNOG; KOG2290; Eukaryota.
DR GeneTree; ENSGT00940000156278; -.
DR HOGENOM; CLU_011531_1_1_1; -.
DR InParanoid; A7YWH9; -.
DR OMA; GGTENMA; -.
DR OrthoDB; 1253228at2759; -.
DR TreeFam; TF312988; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000019805; Expressed in fornix of vagina and 102 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: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; IBA:GO_Central.
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_0000340105"
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..21
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; 97270 MW; E84D195E12AD7B07 CRC64;
MGEARRDSSS SLQHKKPPWL KLDIPAVVPP AAEEPSFLQP LRRQAFLRSV SMPAEPARVP
SPHQEPRRPV LQRQMSITQT IRRGTADWFG VSKDSDSTQK WQRKSIRHCS QRYGKLKPQV
IRELDLPSQD NVSLTSTETP PPLYVGPCQL GMQKIVDPLA RGRAFRLADD AADGPSAPHT
PVTPGAASLC SFSSSRSGFN RLPRRRKRES VAKMSFRAAA ALVKGRSVRD GTLRRAQRRS
FTPASFLEED TADFPDELDT SFFAREGVLH EELSTYPDEV FESPSEAALK DWERAPEQVD
LTGGALDRSE LERSHLMLPL ERGWRKQKEG GAAAPQPKVR LRQEVVSTAG QRRGQRIAMP
VRKLFAREKR PYGLGMVGRL TNRTYRKRID SYVKRQIEDM DDHRPFFTYW LTFVHSLVTI
LAVCIYGVAP VGFSQHETVD SVLRNRGVYE NVKYVQQENF WIGPSSEALI HLGAKFSPCM
RQDPQVHSFI HAAREREKHS ACCVRNDRSG CVQTSEEECS STLAVWVKWP LHPSAPDLAG
QKRRYGSVCH QDPRVCDEPS SEDPHEWPDD ITKWPICTKS SAGNHTNHPH MDCVITGRPC
CIGTKGRCEI TSREYCDFMR GYFHEEATLC SQVHCMDDVC GLLPFLNPEV PDQFYRLWLS
LFLHAGVLHC LVSVCFQMTV LRDLEKLAGW HRIAIIYLLS GVTGNLASAI FLPYRAEVGP
AGSQFGILAC LFVELFQSWQ ILARPWRAFF KLLAVVLFLF TFGLLPWIDN FAHISGFISG
LFLSFAFLPY ISFGKFDLYR KRCQIIVFQL VFLGLLAGLV VLFYFYPVRC EWCEFLTCIP
FTDKFCEKYE LDAQLH
