RTN3_RAT
ID RTN3_RAT Reviewed; 940 AA.
AC Q6RJR6; Q6P6R3; Q8VBU0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Reticulon-3;
GN Name=Rtn3;
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 [MRNA] (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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15946766; DOI=10.1016/j.molbrainres.2005.04.020;
RA Cai Y., Saiyin H., Lin Q., Zhang P., Tang L., Pan X., Yu L.;
RT "Identification of a new RTN3 transcript, RTN3-A1, and its distribution in
RT adult mouse brain.";
RL Brain Res. Mol. Brain Res. 138:236-243(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Gong J.-Y., Zhang X.;
RT "A neuron-specific gene, reticulon 3, is upregulated in satellite cells of
RT rat dorsal root ganglion after peripheral axotomy.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver, and Prostate;
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 [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14746891; DOI=10.1016/j.neulet.2003.11.009;
RA Kumamaru E., Kuo C.-H., Fujimoto T., Kohama K., Zeng L.-H., Taira E.,
RA Tanaka H., Toyoda T., Miki N.;
RT "Reticulon3 expression in rat optic and olfactory systems.";
RL Neurosci. Lett. 356:17-20(2004).
RN [6]
RP INTERACTION WITH ATL1.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-209; SER-212;
RP SER-249; THR-572; SER-575 AND SER-576, AND IDENTIFICATION BY MASS
RP 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: 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. Isoform 2 interacts with
CC BACE1, BACE2, BCL2 and FADD. Interacts with ATL2. Interacts with TMEM33
CC (By similarity). Interacts with ATL1 (PubMed:19665976). Interacts with
CC ZFYVE27 and with KIF5A in a ZFYVE27-dependent manner (By similarity).
CC Interacts with DDX58. Interacts with TRIM25 (By similarity).
CC {ECO:0000250|UniProtKB:O95197, ECO:0000250|UniProtKB:Q9ES97,
CC ECO:0000269|PubMed:19665976}.
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=Q6RJR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6RJR6-2; Sequence=VSP_023771;
CC -!- TISSUE SPECIFICITY: Present in olfactory bulb, olfactory epithelium and
CC retina (at protein level). {ECO:0000269|PubMed:14746891}.
CC -!- DEVELOPMENTAL STAGE: In the optic nerve, expressed more abundantly in
CC the embryo than in the adult. {ECO:0000269|PubMed:14746891}.
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DR EMBL; AY164698; AAP47276.1; -; mRNA.
DR EMBL; AY496443; AAR89918.1; -; mRNA.
DR EMBL; AF442357; AAL35353.1; -; mRNA.
DR EMBL; AF442358; AAL35354.1; -; mRNA.
DR EMBL; BC062068; AAH62068.1; -; mRNA.
DR EMBL; BC107448; AAI07449.1; -; mRNA.
DR RefSeq; NP_001009953.2; NM_001009953.3. [Q6RJR6-2]
DR RefSeq; NP_543185.2; NM_080909.3. [Q6RJR6-1]
DR AlphaFoldDB; Q6RJR6; -.
DR SMR; Q6RJR6; -.
DR BioGRID; 250879; 1.
DR IntAct; Q6RJR6; 2.
DR MINT; Q6RJR6; -.
DR STRING; 10116.ENSRNOP00000028785; -.
DR iPTMnet; Q6RJR6; -.
DR PhosphoSitePlus; Q6RJR6; -.
DR SwissPalm; Q6RJR6; -.
DR jPOST; Q6RJR6; -.
DR PaxDb; Q6RJR6; -.
DR PRIDE; Q6RJR6; -.
DR Ensembl; ENSRNOT00000028785; ENSRNOP00000028785; ENSRNOG00000021202. [Q6RJR6-1]
DR GeneID; 140945; -.
DR KEGG; rno:140945; -.
DR UCSC; RGD:620988; rat. [Q6RJR6-1]
DR CTD; 10313; -.
DR RGD; 620988; Rtn3.
DR eggNOG; KOG1792; Eukaryota.
DR GeneTree; ENSGT00940000157482; -.
DR HOGENOM; CLU_011704_0_0_1; -.
DR InParanoid; Q6RJR6; -.
DR OMA; SXAYLDV; -.
DR OrthoDB; 423549at2759; -.
DR PhylomeDB; Q6RJR6; -.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:Q6RJR6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021202; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q6RJR6; baseline and differential.
DR Genevisible; Q6RJR6; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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:0045202; C:synapse; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISO:RGD.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
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 1: Evidence at protein 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..940
FT /note="Reticulon-3"
FT /id="PRO_0000280541"
FT TOPO_DOM 2..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 772..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 853..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 880..902
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 903..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 752..940
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 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..940
FT /note="Interaction with FADD"
FT /evidence="ECO:0000250"
FT REGION 908..910
FT /note="Interaction with BACE1"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..643
FT /note="Basic and acidic 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:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES97"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES97"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES97"
FT VAR_SEQ 49..751
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12832288,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_023771"
FT CONFLICT 26
FT /note="Missing (in Ref. 1; AAP47276 and 2; AAL35353/
FT AAL35354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 940 AA; 101517 MW; 701B0CF84473D36B CRC64;
MAESSAATQS PSVSSSSSGA EPSTLGGGGG SPGACPALGA KSCGSSCAVG LSSLCSDEPP
SKIMTSSFLS SSEIYNPDPT TPLGSETLGS HLVAKDGKDP LVLLDKKTLD SPQGTNKDRV
DTPVSLAADI PCSHPSIPDS FPEQPTFLSK ETDPTEEWVV KNQEPKNPSE VPSGEDRSAL
DLGQRKAEHI CTHSLSPSEP AVASVEKDSP ESPFEVIIDK ATFDREFKDL YKESTDDLGG
WAAHGDRESP ADLLEMNDKV FPLRNKEAGR YPSSALLGRQ FSHTTAALEE VSRCVNDMHN
FTNEILTWDL DPQAKQQADK SPCTTESTGL DRSEHRSEIP VINLKTSPQQ KMPVCSFNGS
TPITRSTGDW TETFTEGKPV KGYLSSTKEA GGKGVPDSSQ PISGSGAATV EVTLPDLRGT
WPNSVLGEVT EVDSSGESDD TVIEDTTENP SVKNNKVLPE KSDSLPSAAV KTSERENKET
TSHETVRSEM YENSEQQQAH AETPTQRSLE GQMSPQVPNM LNEVIPENLA MTDTTRVCSA
APPSVLSETG FSLTVPASAK SESLLGKNVE DTDGSSPEDL MAALTGTEEK GTVDKEKGDV
LEAVLEKIAN VKNTLPVELL HENKLSSSET KNTKSKYSEH SRETNGGAPK VSSDLEQEQL
TIRAIKELGA KQVQAERMSP GGKLKRTFDP QSGPQNSSDI LEHTDITTGS DLGIPKKPTI
IKDTRIDSIS SLTKTETVNK HVLARLLSDF PVHDLIFWRD VKKTGFVFGT TLIMLLSLAA
FSVISVVSYL ILALLSVTIS FRVYKSVIQA VQKSEEGHPF KAYLDVDITL SSEAFHSYMN
AAMVHVNKAL KLIIRLFLVE DLVDSLKLAV FMWLMTYVGA VFNGITLLIL AELLVFSVPI
VYEKYKTQID HYVGIARDQT KSIVEKIQAK LPGIAKKKAE
