RTN3_PONAB
ID RTN3_PONAB Reviewed; 236 AA.
AC Q5RBL9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Reticulon-3;
GN Name=RTN3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in membrane trafficking in the early
CC secretory pathway. Inhibits BACE1 activity and amyloid precursor
CC protein processing. May induce caspase-8 cascade and apoptosis. May
CC favor BCL2 translocation to the mitochondria upon endoplasmic reticulum
CC stress. Induces the formation of endoplasmic reticulum tubules. Acts
CC also as an inflammation-resolving regulator by interacting with both
CC TRIM25 and RIG-I/DDX58, subsequently impairing DDX58 'Lys-63'-linked
CC polyubiquitination leading to IRF3 and NF-kappa-B inhibition.
CC {ECO:0000250|UniProtKB:O95197}.
CC -!- SUBUNIT: Homodimer. Interacts with RTN4. Interacts with BACE1, BACE2,
CC BCL2 and FADD. Interacts with ATL1 and ATL2. Interacts with TMEM33.
CC Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner.
CC Interacts with DDX58. Interacts with TRIM25.
CC {ECO:0000250|UniProtKB:O95197, ECO:0000250|UniProtKB:Q9ES97}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95197}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O95197};
CC Multi-pass membrane protein {ECO:0000255}.
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DR EMBL; CR858619; CAH90841.1; -; mRNA.
DR RefSeq; NP_001125479.1; NM_001132007.1.
DR AlphaFoldDB; Q5RBL9; -.
DR SMR; Q5RBL9; -.
DR STRING; 9601.ENSPPYP00000003614; -.
DR GeneID; 100172388; -.
DR KEGG; pon:100172388; -.
DR CTD; 10313; -.
DR eggNOG; KOG1792; Eukaryota.
DR HOGENOM; CLU_048580_1_0_1; -.
DR InParanoid; Q5RBL9; -.
DR OrthoDB; 1106300at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT CHAIN 2..236
FT /note="Reticulon-3"
FT /id="PRO_0000280540"
FT TOPO_DOM 2..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..236
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..236
FT /note="Interaction with FADD"
FT /evidence="ECO:0000250"
FT REGION 204..206
FT /note="Interaction with BACE1"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
SQ SEQUENCE 236 AA; 25509 MW; 3B8F726292629FF9 CRC64;
MAEPSAATQS PSISSSSSGA EPSAPGGGGS PGACPALGTK SCSSSCAVHD LIFWRDVKKT
GFVFGTTLIM LLSLAAFSVI SVVSYLILAL LSVTISFRIY KSVIQAVQKS EEGHPFKAYL
DVDITLSSEA FHNYMNAAMV HINRALKLII RLFLVEDLVD SLKLAVFMWL MTYVGAVFNG
ITLLILAELL IFSVPIVYEK YKTQIDHYVG IARDQTKSIV EKIQAKLPGI AKKKAE
