RHDF2_CANLF
ID RHDF2_CANLF Reviewed; 827 AA.
AC Q00M95;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Inactive rhomboid protein 2;
DE Short=iRhom2;
DE AltName: Full=Rhomboid family member 2;
DE AltName: Full=Rhomboid veinlet-like protein 6;
GN Name=RHBDF2; Synonyms=RHBDL6;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=16859891; DOI=10.1016/j.ygeno.2006.05.013;
RA Goldstein O., Zangerl B., Pearce-Kelling S., Sidjanin D.J., Kijas J.W.,
RA Felix J., Acland G.M., Aguirre G.D.;
RT "Linkage disequilibrium mapping in domestic dog breeds narrows the
RT progressive rod-cone degeneration interval and identifies ancestral
RT disease-transmitting chromosome.";
RL Genomics 88:541-550(2006).
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:Q80WQ6}.
CC -!- SUBUNIT: Interacts with EGF (By similarity). Interacts (via cytoplasmic
CC N-terminus) with FRMD8/iTAP; this interaction leads to mutual protein
CC stabilization. Interacts with ADAM17/TACE (By similarity).
CC {ECO:0000250|UniProtKB:Q6PJF5, ECO:0000250|UniProtKB:Q80WQ6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane
CC {ECO:0000250|UniProtKB:Q6PJF5}.
CC -!- TISSUE SPECIFICITY: Detected in retina and spleen.
CC {ECO:0000269|PubMed:16859891}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family. {ECO:0000305}.
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DR EMBL; DQ336163; ABC74872.1; -; mRNA.
DR RefSeq; NP_001070906.1; NM_001077438.1.
DR RefSeq; XP_005624022.1; XM_005623965.2.
DR RefSeq; XP_013971670.1; XM_014116195.1.
DR AlphaFoldDB; Q00M95; -.
DR STRING; 9612.ENSCAFP00000007595; -.
DR MEROPS; S54.953; -.
DR PaxDb; Q00M95; -.
DR Ensembl; ENSCAFT00030002732; ENSCAFP00030002436; ENSCAFG00030001522.
DR GeneID; 483332; -.
DR KEGG; cfa:483332; -.
DR CTD; 79651; -.
DR eggNOG; KOG2290; Eukaryota.
DR HOGENOM; CLU_011531_1_1_1; -.
DR InParanoid; Q00M95; -.
DR OMA; IKRSFAY; -.
DR OrthoDB; 1253228at2759; -.
DR TreeFam; TF312988; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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 Cell membrane; Endoplasmic reticulum; Growth factor binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..827
FT /note="Inactive rhomboid protein 2"
FT /id="PRO_0000341937"
FT TOPO_DOM 1..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..631
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..686
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..744
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 766..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..827
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJF5"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJF5"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WQ6"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WQ6"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJF5"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJF5"
SQ SEQUENCE 827 AA; 93610 MW; 7E93F39DC8AC2D93 CRC64;
MDSTDKNGES VSSVSSSRLQ SRKPPNLSIT IPPPEASAPG EQASMLPQRP RNPAYMKSVS
LQEQRGRWQE GSSEKRPGFR RQASLSQSIR KGTAQWFGVS GDWEAKRQHW QRRSLHHCSV
RYGRLKASCQ RDLELPSQEV PSFQGTESPK PCKMPKIVDP LARGRAFRHP DEVDRPHAPH
PPLTPGVLSL TSFTSVRSGH SHLPRRKRMS VAHMSFQAAA ALLKGRSVLD ATGQRCRVVK
RSFAYPSFLE EDVVDGADTF DSSFFSKEEM SSMPDDVFES PPLSASYFRG IPRSASPVSP
DGVQIPLKEY GRPPVAGTRR GKRIASKVKH FAFDRKKRHY GLGVVGNWLN RSYRRSISST
VQRQLESFDS HRPYFTYWLT FVHIIITLLV ICTYGIAPVG FAQHVTTQLV LRNKGVYESV
KYIQQENFWI GPSSIDLIHL GAKFSPCIRK DQQIEQLVLR ERDLERDSGC CVQNDHSGCI
QTQRKDCSET LATFVKWQDD TGPPMDKSDL GQKRTSGAVC HQDPRTCEEP ASSGAHIWPD
DITKWPICTE QAKSNRTGFL HMDCQIKGRP CCISTKGSCE ITTREYCEFM HGYFHEEATL
CSQVHCLDKV CGLLPFLNPE VPDQFYRLWL SLFLHAGVVH CLVSVVFQMT ILRDLEKLAG
WHRIAIIFIL SGITGNLASA IFLPYRAEVG PAGSQFGLLA CLFVELFQSW QLLERPWKAF
LNLSAIVLFL FICGLLPWID NIAHIFGFLS GLLLAFAFLP YITFGTSDKY RKRALILVSL
LVFAGLFASL VIWLYVYPIN WPWIEYLTCF PFTSRFCEKY ELDQVLH
