FRMD8_RAT
ID FRMD8_RAT Reviewed; 466 AA.
AC Q5U2R3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=FERM domain-containing protein 8;
GN Name=Frmd8;
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=Heart;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-440, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Promotes the cell surface stability of iRhom1/RHBDF1 and
CC iRhom2/RHBDF2 and prevents their degradation via the endolysosomal
CC pathway. By acting on iRhoms, involved in ADAM17-mediated shedding of
CC TNF, amphiregulin/AREG, HBEGF and TGFA from the cell surface (By
CC similarity). Negatively regulates Wnt signaling, possibly by
CC antagonizing the recruitment of AXIN1 to LRP6 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZ67}.
CC -!- SUBUNIT: Interacts with iRhom1/RHBDF1 and iRhom2/RHBDF2 (via
CC cytoplasmic N-termini); this interaction leads to mutual protein
CC stabilization. Interacts with ADAM17; this interaction is indirect and
CC mediated by iRhom proteins (By similarity). Interacts with LRP6; this
CC interaction affects LRP6-binding to AXIN1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZ67}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BZ67}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9BZ67}.
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DR EMBL; BC085896; AAH85896.1; -; mRNA.
DR RefSeq; NP_001008349.1; NM_001008348.1.
DR AlphaFoldDB; Q5U2R3; -.
DR SMR; Q5U2R3; -.
DR STRING; 10116.ENSRNOP00000028331; -.
DR iPTMnet; Q5U2R3; -.
DR PhosphoSitePlus; Q5U2R3; -.
DR PaxDb; Q5U2R3; -.
DR PRIDE; Q5U2R3; -.
DR Ensembl; ENSRNOT00000113145; ENSRNOP00000095691; ENSRNOG00000020881.
DR GeneID; 309172; -.
DR KEGG; rno:309172; -.
DR UCSC; RGD:1310323; rat.
DR CTD; 83786; -.
DR RGD; 1310323; Frmd8.
DR eggNOG; KOG4335; Eukaryota.
DR GeneTree; ENSGT00530000063721; -.
DR HOGENOM; CLU_032351_0_0_1; -.
DR InParanoid; Q5U2R3; -.
DR OMA; GSHYRAY; -.
DR OrthoDB; 1068540at2759; -.
DR PhylomeDB; Q5U2R3; -.
DR TreeFam; TF317921; -.
DR PRO; PR:Q5U2R3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020881; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q5U2R3; baseline and differential.
DR Genevisible; Q5U2R3; RN.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF00373; FERM_M; 1.
DR SMART; SM00295; B41; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..466
FT /note="FERM domain-containing protein 8"
FT /id="PRO_0000295780"
FT DOMAIN 30..377
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ67"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ67"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ67"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UFK8"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ67"
SQ SEQUENCE 466 AA; 51782 MW; 40EC0764715C5222 CRC64;
MEGAEGNAGQ PGPAERSHRS SVSSVGARAA DVLVYLADDT VVPLAVENLS SISAHELHRA
VREVLQLPDM ALEAFALWLV SPLLEVQLKP KHQPYKLGRQ WPELLLRFTD ASDDDIAMDE
PSLQFRRNVF FPKRRELQVH DEEVLRLLYE EAKGNVLTAR YPCDLEDCEV LGGLVCRVQL
GPYQPGQPAA CTVREKLDSF LPAHLCKRGH GLFAAFRGRG AKTGPCEQGL LNAYRQVKEM
AGGDSERETT LGSHYRAYLL KCHELPFYGC AFFHGEVDKP TQGFLHRGGR KPVTVAISLE
GVHVIDNREK HVLLGLRFQE LSWDHTSPEE EEPVLWLEFD GDSEGTPVNK LLRIYSKQAE
LMSVLIEYCI ELSQAAEPAL PQESASGPQE APSPSSAPTQ RPKLRRQGSV VCSRIQHLST
IDYVEDGSGI KRVKPKRTTS FFSRQLSSSH GSYTVVQPND NSPEQG
