RTN3_BOVIN
ID RTN3_BOVIN Reviewed; 256 AA.
AC Q08D83; A5D9B5; Q6IM68;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Reticulon-3;
GN Name=RTN3;
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] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Hereford; TISSUE=Brain cortex, and Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION (ISOFORM 2).
RX PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
RA Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
RT "A reticular rhapsody: phylogenic evolution and nomenclature of the
RT RTN/Nogo gene family.";
RL FASEB J. 17:1238-1247(2003).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08D83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08D83-2; Sequence=VSP_023770;
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DR EMBL; BT030534; ABQ12974.1; -; mRNA.
DR EMBL; BC123892; AAI23893.1; -; mRNA.
DR EMBL; BC149634; AAI49635.1; -; mRNA.
DR EMBL; BK001797; DAA01969.1; -; mRNA.
DR RefSeq; NP_872598.1; NM_182657.1. [Q08D83-2]
DR RefSeq; XP_015316795.1; XM_015461309.1.
DR RefSeq; XP_015325544.1; XM_015470058.1.
DR AlphaFoldDB; Q08D83; -.
DR SMR; Q08D83; -.
DR STRING; 9913.ENSBTAP00000054826; -.
DR PaxDb; Q08D83; -.
DR PRIDE; Q08D83; -.
DR Ensembl; ENSBTAT00000025564; ENSBTAP00000025564; ENSBTAG00000019204. [Q08D83-2]
DR Ensembl; ENSBTAT00000046142; ENSBTAP00000043467; ENSBTAG00000019204. [Q08D83-1]
DR GeneID; 359721; -.
DR KEGG; bta:359721; -.
DR CTD; 10313; -.
DR VEuPathDB; HostDB:ENSBTAG00000019204; -.
DR eggNOG; KOG1792; Eukaryota.
DR GeneTree; ENSGT00940000157482; -.
DR InParanoid; Q08D83; -.
DR OMA; KYQDHVD; -.
DR OrthoDB; 1106300at2759; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000019204; Expressed in occipital lobe and 103 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0071787; P:endoplasmic reticulum tubular network formation; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
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; Alternative splicing; Apoptosis; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT CHAIN 2..256
FT /note="Reticulon-3"
FT /id="PRO_0000280539"
FT TOPO_DOM 2..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 88..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 68..256
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..256
FT /note="Interaction with FADD"
FT /evidence="ECO:0000250"
FT REGION 224..226
FT /note="Interaction with BACE1"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..25
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 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT VAR_SEQ 49..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752, ECO:0000303|Ref.2"
FT /id="VSP_023770"
SQ SEQUENCE 256 AA; 27455 MW; D2F64DA8EC6F42F4 CRC64;
MAEPSAATQS PSVSSSSSGA ESSAPGGGSG SPGACPALGT KSCGSSCADS FVSSSSSQPV
SLFSTSQVHD LIFWRDVKKT GFVFGTTLIM LLSLAAFSVI SVVSYLILAL LSVTISFRVY
KSVIQAVQKS EEGHPFKAYL DVDITLSSEA FHNYVNAAMV HINRALKLII RLFLVEDLVD
SLKLAVFMWL MTYVGAVFNG ITLLILAELL VFSIPIVYEK YKTQIDHYVG IARDQTKSIV
EKIQAKLPGI AKKKAE
