RTN4_RAT
ID RTN4_RAT Reviewed; 1163 AA.
AC Q9JK11; Q9JK10; Q9R0D9; Q9WUE9; Q9WUF0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Reticulon-4;
DE AltName: Full=Foocen;
DE AltName: Full=Glut4 vesicle 20 kDa protein;
DE AltName: Full=Neurite outgrowth inhibitor;
DE Short=Nogo protein;
GN Name=Rtn4; Synonyms=Nogo;
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 C), AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Adipocyte;
RX PubMed=10231557; DOI=10.1016/s0167-4889(99)00033-6;
RA Morris N.J., Ross S.A., Neveu J.M., Lane W.S., Lienhard G.E.;
RT "Cloning and characterization of a 22 kDa protein from rat adipocytes: a
RT new member of the reticulon family.";
RL Biochim. Biophys. Acta 1450:68-76(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RX PubMed=10667796; DOI=10.1038/35000219;
RA Chen M.S., Huber A.B., Van der Haar M.E., Frank M., Schnell L.,
RA Spillmann A.A., Christ F., Schwab M.E.;
RT "Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen
RT for monoclonal antibody IN-1.";
RL Nature 403:434-439(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND B2).
RC STRAIN=Wistar Kyoto; TISSUE=Vascular smooth muscle;
RA Ito T., Schwartz S.M.;
RT "Cloning of a member of the reticulon gene family in rat: one of two minor
RT splice variants.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DOMAIN.
RX PubMed=12037567; DOI=10.1038/417547a;
RA GrandPre T., Li S., Strittmatter S.M.;
RT "Nogo-66 receptor antagonist peptide promotes axonal regeneration.";
RL Nature 417:547-551(2002).
RN [5]
RP INTERACTION WITH CNTNAP1.
RX PubMed=14592966; DOI=10.1093/emboj/cdg570;
RA Nie D.-Y., Zhou Z.-H., Ang B.-T., Teng F.Y.H., Xu G., Xiang T., Wang C.-Y.,
RA Zeng L., Takeda Y., Xu T.-L., Ng Y.K., Faivre-Sarrailh C., Popko B.,
RA Ling E.-A., Schachner M., Watanabe K., Pallen C.J., Tang B.L., Xiao Z.-C.;
RT "Nogo-A at CNS paranodes is a ligand of Caspr: possible regulation of K(+)
RT channel localization.";
RL EMBO J. 22:5666-5678(2003).
RN [6]
RP FUNCTION (ISOFORM A).
RX PubMed=12843238; DOI=10.1523/jneurosci.23-13-05393.2003;
RA Oertle T., van der Haar M.E., Bandtlow C.E., Robeva A., Burfeind P.,
RA Buss A., Huber A.B., Simonen M., Schnell L., Brosamle C., Kaupmann K.,
RA Vallon R., Schwab M.E.;
RT "Nogo-A inhibits neurite outgrowth and cell spreading with three discrete
RT regions.";
RL J. Neurosci. 23:5393-5406(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [8]
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 [9]
RP FUNCTION (ISOFORM A).
RX PubMed=20573699; DOI=10.1242/dev.048371;
RA Petrinovic M.M., Duncan C.S., Bourikas D., Weinman O., Montani L.,
RA Schroeter A., Maerki D., Sommer L., Stoeckli E.T., Schwab M.E.;
RT "Neuronal Nogo-A regulates neurite fasciculation, branching and extension
RT in the developing nervous system.";
RL Development 137:2539-2550(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-329; SER-333;
RP SER-425; THR-429; SER-689; SER-766; SER-830; THR-832 AND SER-922, 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: Required to induce the formation and stabilization of
CC endoplasmic reticulum (ER) tubules. They regulate membrane
CC morphogenesis in the ER by promoting tubular ER production. They
CC influence nuclear envelope expansion, nuclear pore complex formation
CC and proper localization of inner nuclear membrane proteins. However
CC each isoform have specific functions mainly depending on their tissue
CC expression specificities. {ECO:0000305}.
CC -!- FUNCTION: [Isoform A]: Developmental neurite growth regulatory factor
CC with a role as a negative regulator of axon-axon adhesion and growth,
CC and as a facilitator of neurite branching. Regulates neurite
CC fasciculation, branching and extension in the developing nervous
CC system. Involved in down-regulation of growth, stabilization of wiring
CC and restriction of plasticity in the adult CNS (PubMed:12037567,
CC PubMed:12843238, PubMed:20573699). Regulates the radial migration of
CC cortical neurons via an RTN4R-LINGO1 containing receptor complex. Acts
CC as a negative regulator of central nervous system angiogenesis.
CC Inhibits spreading, migration and sprouting of primary brain
CC microvascular endothelial cells (MVECs). Also induces the retraction of
CC MVECs lamellipodia and filopodia in a ROCK pathway-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q99P72,
CC ECO:0000269|PubMed:12037567, ECO:0000269|PubMed:12843238,
CC ECO:0000269|PubMed:20573699}.
CC -!- FUNCTION: [Isoform B]: Mainly function in endothelial cells and
CC vascular smooth muscle cells, is also involved in immune system
CC regulation (By similarity). Modulator of vascular remodeling, promotes
CC the migration of endothelial cells but inhibits the migration of
CC vascular smooth muscle cells. Regulates endothelial sphingolipid
CC biosynthesis with direct effects on vascular function and blood
CC pressure. Inhibits serine palmitoyltransferase, SPTLC1, the rate-
CC limiting enzyme of the novo sphingolipid biosynthetic pathway, thereby
CC controlling production of endothelial sphingosine-1-phosphate (S1P).
CC Required to promote macrophage homing and functions such as
CC cytokine/chemokine gene expression involved in angiogenesis,
CC arteriogenesis and tissue repair. Mediates ICAM1 induced
CC transendothelial migration of leukocytes such as monocytes and
CC neutrophils and acute inflammation. Necessary for immune responses
CC triggered by nucleic acid sensing TLRs, such as TLR9, is required for
CC proper TLR9 location to endolysosomes. Also involved in immune response
CC to LPS. Plays a role in liver regeneration through the modulation of
CC hepatocytes proliferation (By similarity). Reduces the anti-apoptotic
CC activity of Bcl-xl and Bcl-2. This is likely consecutive to their
CC change in subcellular location, from the mitochondria to the
CC endoplasmic reticulum, after binding and sequestration. With isoform C,
CC inhibits BACE1 activity and amyloid precursor protein processing (By
CC similarity). {ECO:0000250|UniProtKB:Q99P72,
CC ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- FUNCTION: [Isoform C]: Regulates cardiomyocyte apoptosis upon hypoxic
CC conditions (By similarity). With isoform B, inhibits BACE1 activity and
CC amyloid precursor protein processing (By similarity).
CC {ECO:0000250|UniProtKB:Q99P72, ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- SUBUNIT: Binds to RTN4R (By similarity). Interacts with ATL1
CC (PubMed:19665976). Interacts with TMEM170A (By similarity). Interacts
CC with RTN4IP1 (By similarity). {ECO:0000250|UniProtKB:Q99P72,
CC ECO:0000250|UniProtKB:Q9NQC3, ECO:0000269|PubMed:19665976}.
CC -!- SUBUNIT: [Isoform A]: Interacts in trans with CNTNAP1
CC (PubMed:14592966). Interacts with REEP5 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NQC3, ECO:0000269|PubMed:14592966}.
CC -!- SUBUNIT: [Isoform B]: Homodimer (By similarity). Interacts with
CC BAD/Bcl-xl and BCL2. Interact with RTN3 (By similarity). Interacts with
CC NGBR (By similarity). Interacts with SPTLC1 (By similarity). Interacts
CC with GRAMD4 (By similarity). Interacts with CDH5 (By similarity).
CC Interacts with BACE1 and BACE2 (By similarity). Interacts with REEP5
CC (By similarity). {ECO:0000250|UniProtKB:Q99P72,
CC ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- SUBUNIT: [Isoform C]: Interacts with BACE1 and BACE2 (By similarity).
CC Interacts with TMEM33 (By similarity). {ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- INTERACTION:
CC Q9JK11-1; Q6PST4: Atl1; NbExp=6; IntAct=EBI-919989, EBI-2410213;
CC Q9JK11-1; P48722: Hspa4l; Xeno; NbExp=6; IntAct=EBI-919989, EBI-8314699;
CC Q9JK11-1; O95136: S1PR2; Xeno; NbExp=2; IntAct=EBI-919989, EBI-10634606;
CC Q9JK11-1; P52592: S1pr2; Xeno; NbExp=3; IntAct=EBI-919989, EBI-16091339;
CC Q9JK11-3; Q8WXF7: ATL1; Xeno; NbExp=2; IntAct=EBI-920002, EBI-2410266;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass
CC membrane protein {ECO:0000255}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9NQC3}. Note=Anchored to the membrane of the
CC endoplasmic reticulum (ER) through 2 putative transmembrane domains.
CC Localizes throughout the ER tubular network. Co-localizes with TMEM33
CC at the ER sheets. {ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass
CC membrane protein {ECO:0000255}; Extracellular side
CC {ECO:0000250|UniProtKB:Q9NQC3}. Cell junction
CC {ECO:0000250|UniProtKB:Q9NQC3}. Note=Mainly located on endoplasmic
CC reticulum tubules and sheet edges. Upon ICAM1 engagement, redistributed
CC toward endothelial junctions where interacts with CDH5.
CC {ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NQC3}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A; Synonyms=Nogo-A, NI-220-250;
CC IsoId=Q9JK11-1; Sequence=Displayed;
CC Name=B; Synonyms=Nogo-B, Foocen-M1;
CC IsoId=Q9JK11-2; Sequence=VSP_005658;
CC Name=C; Synonyms=Nogo-C, VP20;
CC IsoId=Q9JK11-3; Sequence=VSP_005656, VSP_005657;
CC Name=B2; Synonyms=Foocen-M2;
CC IsoId=Q9JK11-4; Sequence=VSP_005659;
CC -!- TISSUE SPECIFICITY: Isoforms A, B and C are present in optic nerve,
CC spinal cord and cerebral cortex. Isoforms A and B are present in dorsal
CC root ganglion, sciatic nerve and PC12 cells after longer exposure.
CC Isoforms B and C are detected in kidney, cartilage, skin, lung and
CC spleen. Isoform C is expressed at high level in skeletal muscle. In
CC adult animals isoform A is expressed mainly in the nervous system.
CC -!- DOMAIN: Three regions, residues 59-172, 544-725 and the loop 66 amino
CC acids, between the two transmembrane domains, known as Nogo-66 loop,
CC appear to be responsible for the inhibitory effect on neurite outgrowth
CC and the spreading of neurons. This Nogo-66 loop, mediates also the
CC binding of RTN4 to its receptor. {ECO:0000269|PubMed:12037567}.
CC -!- DOMAIN: [Isoform B]: N-terminal part, called Am-Nogo-B(1-200), is the
CC functional domain for RTN4B-mediated signaling in endothelial and
CC vascular smooth muscle cells. {ECO:0000250|UniProtKB:Q9NQC3}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Nerve regrowth: nipped by a
CC no-go - Issue 69 of April 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/069";
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DR EMBL; AF051335; AAF01564.1; -; mRNA.
DR EMBL; AJ242961; CAB71027.1; -; mRNA.
DR EMBL; AJ242962; CAB71028.1; -; mRNA.
DR EMBL; AJ242963; CAB71029.1; -; mRNA.
DR EMBL; AF132045; AAD31019.1; -; mRNA.
DR EMBL; AF132046; AAD31020.1; -; mRNA.
DR RefSeq; NP_114019.1; NM_031831.1. [Q9JK11-1]
DR RefSeq; XP_006251670.2; XM_006251608.2. [Q9JK11-2]
DR RefSeq; XP_006251671.1; XM_006251609.3. [Q9JK11-3]
DR RefSeq; XP_017454882.1; XM_017599393.1. [Q9JK11-4]
DR AlphaFoldDB; Q9JK11; -.
DR BMRB; Q9JK11; -.
DR SMR; Q9JK11; -.
DR BioGRID; 249825; 6.
DR DIP; DIP-37179N; -.
DR IntAct; Q9JK11; 16.
DR MINT; Q9JK11; -.
DR STRING; 10116.ENSRNOP00000006443; -.
DR iPTMnet; Q9JK11; -.
DR PhosphoSitePlus; Q9JK11; -.
DR jPOST; Q9JK11; -.
DR PaxDb; Q9JK11; -.
DR PRIDE; Q9JK11; -.
DR ABCD; Q9JK11; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000042965; ENSRNOP00000040760; ENSRNOG00000004621. [Q9JK11-3]
DR GeneID; 83765; -.
DR KEGG; rno:83765; -.
DR UCSC; RGD:620989; rat. [Q9JK11-1]
DR CTD; 57142; -.
DR RGD; 620989; Rtn4.
DR VEuPathDB; HostDB:ENSRNOG00000004621; -.
DR eggNOG; KOG1792; Eukaryota.
DR GeneTree; ENSGT00940000156568; -.
DR HOGENOM; CLU_048580_0_0_1; -.
DR InParanoid; Q9JK11; -.
DR OrthoDB; 212372at2759; -.
DR PhylomeDB; Q9JK11; -.
DR Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
DR PRO; PR:Q9JK11; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000004621; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; Q9JK11; baseline and differential.
DR Genevisible; Q9JK11; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0044294; C:dendritic growth cone; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:RGD.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007413; P:axonal fasciculation; IDA:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; ISO:RGD.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0120078; P:cell adhesion involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; ISO:RGD.
DR GO; GO:0022009; P:central nervous system vasculogenesis; ISS:UniProtKB.
DR GO; GO:0021801; P:cerebral cortex radial glia-guided migration; ISS:UniProtKB.
DR GO; GO:0071787; P:endoplasmic reticulum tubular network formation; ISS:UniProtKB.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; ISS:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IDA:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
DR GO; GO:0070571; P:negative regulation of neuron projection regeneration; IMP:RGD.
DR GO; GO:2001213; P:negative regulation of vasculogenesis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR GO; GO:0021553; P:olfactory nerve development; IEP:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:1905653; P:positive regulation of artery morphogenesis; ISS:UniProtKB.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:1905580; P:positive regulation of ERBB3 signaling pathway; ISO:RGD.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; IDA:RGD.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; ISS:UniProtKB.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISS:UniProtKB.
DR GO; GO:1905523; P:positive regulation of macrophage migration; ISS:UniProtKB.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; ISO:RGD.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; ISO:RGD.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IDA:UniProtKB.
DR GO; GO:0051960; P:regulation of nervous system development; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR DisProt; DP01152; -.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Cell membrane;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1163
FT /note="Reticulon-4"
FT /id="PRO_0000168167"
FT TOPO_DOM 1..989
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 990..1010
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1011..1104
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1126..1163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 976..1163
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC3"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC3"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC3"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 832
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P72"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC3"
FT MOD_RES 1075
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC3"
FT VAR_SEQ 1..964
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10231557,
FT ECO:0000303|PubMed:10667796"
FT /id="VSP_005656"
FT VAR_SEQ 173..975
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10667796, ECO:0000303|Ref.3"
FT /id="VSP_005658"
FT VAR_SEQ 192..975
FT /note="Missing (in isoform B2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005659"
FT VAR_SEQ 965..975
FT /note="AVLSAELSKTS -> MDGQKKHWKDK (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10231557,
FT ECO:0000303|PubMed:10667796"
FT /id="VSP_005657"
FT CONFLICT 1130..1131
FT /note="Missing (in Ref. 3; AAD31020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1163 AA; 126388 MW; 8CB894B09E94F0B6 CRC64;
MEDIDQSSLV SSSTDSPPRP PPAFKYQFVT EPEDEEDEEE EEDEEEDDED LEELEVLERK
PAAGLSAAAV PPAAAAPLLD FSSDSVPPAP RGPLPAAPPA APERQPSWER SPAAPAPSLP
PAAAVLPSKL PEDDEPPARP PPPPPAGASP LAEPAAPPST PAAPKRRGSG SVDETLFALP
AASEPVIPSS AEKIMDLMEQ PGNTVSSGQE DFPSVLLETA ASLPSLSPLS TVSFKEHGYL
GNLSAVSSSE GTIEETLNEA SKELPERATN PFVNRDLAEF SELEYSEMGS SFKGSPKGES
AILVENTKEE VIVRSKDKED LVCSAALHSP QESPVGKEDR VVSPEKTMDI FNEMQMSVVA
PVREEYADFK PFEQAWEVKD TYEGSRDVLA ARANVESKVD RKCLEDSLEQ KSLGKDSEGR
NEDASFPSTP EPVKDSSRAY ITCASFTSAT ESTTANTFPL LEDHTSENKT DEKKIEERKA
QIITEKTSPK TSNPFLVAVQ DSEADYVTTD TLSKVTEAAV SNMPEGLTPD LVQEACESEL
NEATGTKIAY ETKVDLVQTS EAIQESLYPT AQLCPSFEEA EATPSPVLPD IVMEAPLNSL
LPSAGASVVQ PSVSPLEAPP PVSYDSIKLE PENPPPYEEA MNVALKALGT KEGIKEPESF
NAAVQETEAP YISIACDLIK ETKLSTEPSP DFSNYSEIAK FEKSVPEHAE LVEDSSPESE
PVDLFSDDSI PEVPQTQEEA VMLMKESLTE VSETVAQHKE ERLSASPQEL GKPYLESFQP
NLHSTKDAAS NDIPTLTKKE KISLQMEEFN TAIYSNDDLL SSKEDKIKES ETFSDSSPIE
IIDEFPTFVS AKDDSPKLAK EYTDLEVSDK SEIANIQSGA DSLPCLELPC DLSFKNIYPK
DEVHVSDEFS ENRSSVSKAS ISPSNVSALE PQTEMGSIVK SKSLTKEAEK KLPSDTEKED
RSLSAVLSAE LSKTSVVDLL YWRDIKKTGV VFGASLFLLL SLTVFSIVSV TAYIALALLS
VTISFRIYKG VIQAIQKSDE GHPFRAYLES EVAISEELVQ KYSNSALGHV NSTIKELRRL
FLVDDLVDSL KFAVLMWVFT YVGALFNGLT LLILALISLF SIPVIYERHQ VQIDHYLGLA
NKSVKDAMAK IQAKIPGLKR KAD
