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Reticulon-3 (Homolog of ASY protein) (HAP) (Neuroendocrine-specific protein-like 2) (NSP-like protein 2) (Neuroendocrine-specific protein-like II) (NSP-like protein II) (NSPLII)

 RTN3_HUMAN              Reviewed;        1032 AA.
O95197; B3KQS2; B7Z308; B7Z4M0; F5H774; Q147U9; Q496K2; Q53GN3;
Q59EP0; Q5UEP2; Q6T930; Q7RTM7; Q7RTM8; Q7RTN3;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
23-MAY-2018, entry version 166.
RecName: Full=Reticulon-3;
AltName: Full=Homolog of ASY protein;
Short=HAP;
AltName: Full=Neuroendocrine-specific protein-like 2;
Short=NSP-like protein 2;
AltName: Full=Neuroendocrine-specific protein-like II;
Short=NSP-like protein II;
Short=NSPLII;
Name=RTN3; Synonyms=ASYIP, NSPL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), AND TISSUE
SPECIFICITY.
TISSUE=Retina;
PubMed=10331947; DOI=10.1006/geno.1999.5807;
Moreira E.F., Jaworski C.J., Rodriguez I.R.;
"Cloning of a novel member of the reticulon gene family (RTN3): gene
structure and chromosomal localization to 11q13.";
Genomics 58:73-81(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION
WITH RTN4, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12811824; DOI=10.1002/jcp.10297;
Qi B., Qi Y., Watari A., Yoshioka N., Inoue H., Minemoto Y.,
Yamashita K., Sasagawa T., Yutsudo M.;
"Pro-apoptotic ASY/Nogo-B protein associates with ASYIP.";
J. Cell. Physiol. 196:312-318(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
PubMed=14986927;
Huang X., Yang H., Zhou Y., Liu J., Yin B., Peng X., Qiang B.,
Yuan J.;
"Overexpression of human reticulon 3 (hRTN3) in astrocytoma.";
Clin. Neuropathol. 23:1-7(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
VARIANT GLU-6.
TISSUE=Brain;
PubMed=15946766; DOI=10.1016/j.molbrainres.2005.04.020;
Cai Y., Saiyin H., Lin Q., Zhang P., Tang L., Pan X., Yu L.;
"Identification of a new RTN3 transcript, RTN3-A1, and its
distribution in adult mouse brain.";
Brain Res. Mol. Brain Res. 138:236-243(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
TISSUE=Brain, and Corpus callosum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain, Eye, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
IDENTIFICATION (ISOFORMS 3; 4 AND 5).
PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
"A reticular rhapsody: phylogenic evolution and nomenclature of the
RTN/Nogo gene family.";
FASEB J. 17:1238-1247(2003).
[12]
INTERACTION WITH BACE1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=15286784; DOI=10.1038/nm1088;
He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.;
"Reticulon family members modulate BACE1 activity and amyloid-beta
peptide generation.";
Nat. Med. 10:959-965(2004).
[13]
HOMODIMERIZATION, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16054885; DOI=10.1016/j.bbrc.2005.07.012;
Wakana Y., Koyama S., Nakajima K., Hatsuzawa K., Nagahama M., Tani K.,
Hauri H.-P., Melancon P., Tagaya M.;
"Reticulon 3 is involved in membrane trafficking between the
endoplasmic reticulum and Golgi.";
Biochem. Biophys. Res. Commun. 334:1198-1205(2005).
[14]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
PubMed=15350194; DOI=10.1042/BJ20040458;
Di Scala F., Dupuis L., Gaiddon C., De Tapia M., Jokic N.,
Gonzalez de Aguilar J.-L., Raul J.-S., Ludes B., Loeffler J.-P.;
"Tissue specificity and regulation of the N-terminal diversity of
reticulon 3.";
Biochem. J. 385:125-134(2005).
[15]
INTERACTION WITH FADD, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17031492; DOI=10.1007/s10495-006-0082-0;
Xiang R., Liu Y., Zhu L., Dong W., Qi Y.;
"Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling
complexes.";
Apoptosis 11:1923-1932(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[17]
INTERACTION WITH BACE1 AND BACE2.
PubMed=16965550; DOI=10.1111/j.1460-9568.2006.05005.x;
Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.;
"Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its
ability to produce amyloid beta-protein.";
Eur. J. Neurosci. 24:1237-1244(2006).
[18]
HOMODIMERIZATION, INTERACTION WITH BACE1 AND RTN4, AND SUBCELLULAR
LOCATION.
PubMed=16979658; DOI=10.1016/j.jmb.2006.07.094;
He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.;
"Mapping of interaction domains mediating binding between BACE1 and
RTN/Nogo proteins.";
J. Mol. Biol. 363:625-634(2006).
[19]
INDUCTION BY ER STRESS, INTERACTION WITH BCL2, SUBCELLULAR LOCATION,
AND FUNCTION.
PubMed=17191123; DOI=10.1007/s10495-006-0574-y;
Wan Q., Kuang E., Dong W., Zhou S., Xu H., Qi Y., Liu Y.;
"Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response
to endoplasmic reticulum stress.";
Apoptosis 12:319-328(2007).
[20]
INTERACTION WITH COXSACKIEVIRUS A16 P2C; POLIOVIRUS P2C AND
ENTEROVIRUS 71 P2C, AND SUBCELLULAR LOCATION.
PubMed=17182608; DOI=10.1074/jbc.M611145200;
Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
"Reticulon 3 binds the 2C protein of enterovirus 71 and is required
for viral replication.";
J. Biol. Chem. 282:5888-5898(2007).
[21]
TOPOLOGY.
PubMed=17699523; DOI=10.1074/jbc.M704181200;
He W., Shi Q., Hu X., Yan R.;
"The membrane topology of RTN3 and its effect on binding of RTN3 to
BACE1.";
J. Biol. Chem. 282:29144-29151(2007).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-650, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[24]
INTERACTION WITH ATL2.
PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
Rapoport T.A., Blackstone C.;
"A class of dynamin-like GTPases involved in the generation of the
tubular ER network.";
Cell 138:549-561(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
INTERACTION WITH ZFYVE27 AND KIF5A.
PubMed=21976701; DOI=10.1091/mbc.E11-01-0068;
Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
"Protrudin serves as an adaptor molecule that connects KIF5 and its
cargoes in vesicular transport during process formation.";
Mol. Biol. Cell 22:4602-4620(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-229; SER-246;
SER-316 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
SUBCELLULAR LOCATION.
PubMed=24262037; DOI=10.1042/BJ20131186;
Yamamoto Y., Yoshida A., Miyazaki N., Iwasaki K., Sakisaka T.;
"Arl6IP1 has the ability to shape the mammalian ER membrane in a
reticulon-like fashion.";
Biochem. J. 458:69-79(2014).
[32]
FUNCTION.
PubMed=25612671;
Urade T., Yamamoto Y., Zhang X., Ku Y., Sakisaka T.;
"Identification and characterization of TMEM33 as a reticulon-binding
protein.";
Kobe J. Med. Sci. 60:E57-E65(2014).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[34]
INTERACTION WITH WEST NILE VIRUS PROTEIN NS4A, AND SUBCELLULAR
LOCATION.
PubMed=29117567; DOI=10.1016/j.celrep.2017.10.055;
Aktepe T.E., Liebscher S., Prier J.E., Simmons C.P., Mackenzie J.M.;
"The host protein reticulon 3.1A is utilized by flaviviruses to
facilitate membrane remodelling.";
Cell Rep. 21:1639-1654(2017).
-!- FUNCTION: May be involved in membrane trafficking in the early
secretory pathway. Inhibits BACE1 activity and amyloid precursor
protein processing. May induce caspase-8 cascade and apoptosis.
May favor BCL2 translocation to the mitochondria upon endoplasmic
reticulum stress. In case of enteroviruses infection, RTN3 may be
involved in the viral replication or pathogenesis. Induces the
formation of endoplasmic reticulum tubules (PubMed:25612671).
{ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885,
ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123,
ECO:0000269|PubMed:25612671}.
-!- SUBUNIT: Homodimer. Interacts with ATL1 (By similarity). Interacts
with RTN4. Isoform 3 interacts with BACE1, BACE2, BCL2 and FADD.
Interacts with ATL2. Interacts with TMEM33 (By similarity).
Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-dependent
manner (PubMed:21976701). {ECO:0000250|UniProtKB:Q9ES97,
ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:15286784,
ECO:0000269|PubMed:16965550, ECO:0000269|PubMed:16979658,
ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17191123,
ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:21976701}.
-!- SUBUNIT: (Microbial infection) Interacts with Coxsackievirus A16,
enterovirus 71 and poliovirus P2C proteins (PubMed:17182608).
Interacts with protein West Nile virus NS4A (PubMed:29117567).
{ECO:0000269|PubMed:17182608, ECO:0000269|PubMed:29117567}.
-!- INTERACTION:
O14735:CDIPT; NbExp=3; IntAct=EBI-740467, EBI-358858;
Q9ULP0-2:NDRG4; NbExp=3; IntAct=EBI-11525735, EBI-11978907;
Q969Q6:PPP2R3C; NbExp=3; IntAct=EBI-740467, EBI-2561661;
P43378:PTPN9; NbExp=4; IntAct=EBI-740467, EBI-742898;
Q6IQ43:PTPN9; NbExp=3; IntAct=EBI-740467, EBI-10250413;
Q13596:SNX1; NbExp=3; IntAct=EBI-740467, EBI-2822329;
P54274:TERF1; NbExp=2; IntAct=EBI-740467, EBI-710997;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:15286784,
ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:16979658,
ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17182608,
ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:24262037,
ECO:0000269|PubMed:29117567}; Multi-pass membrane protein
{ECO:0000255}. Golgi apparatus membrane
{ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885,
ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:29117567}; Multi-
pass membrane protein {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=A1, A4b;
IsoId=O95197-1; Sequence=Displayed;
Name=2; Synonyms=A2, A3b;
IsoId=O95197-2; Sequence=VSP_023759;
Name=3; Synonyms=B1, A1;
IsoId=O95197-3; Sequence=VSP_023759, VSP_023760;
Name=4; Synonyms=B2, A2;
IsoId=O95197-4; Sequence=VSP_023760;
Name=5;
IsoId=O95197-5; Sequence=VSP_023759, VSP_023760, VSP_023761;
Note=No experimental confirmation available.;
Name=6;
IsoId=O95197-6; Sequence=VSP_045319, VSP_045320;
Name=7;
IsoId=O95197-7; Sequence=VSP_047008;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Isoform 3 is widely expressed, with highest
levels in brain, where it is enriched in neuronal cell bodies from
gray matter (at protein level). Three times more abundant in
macula than in peripheral retina. Isoform 1 is expressed at high
levels in brain and at low levels in skeletal muscle. Isoform 2 is
only found in melanoma. {ECO:0000269|PubMed:10331947,
ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:14986927,
ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:15946766}.
-!- INDUCTION: By endoplasmic reticulum stress (at protein level).
{ECO:0000269|PubMed:17191123}.
-!- SEQUENCE CAUTION:
Sequence=BAD93008.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF059524; AAC99319.1; -; mRNA.
EMBL; AF059529; AAD20951.1; -; Genomic_DNA.
EMBL; AF059525; AAD20951.1; JOINED; Genomic_DNA.
EMBL; AF059526; AAD20951.1; JOINED; Genomic_DNA.
EMBL; AF059527; AAD20951.1; JOINED; Genomic_DNA.
EMBL; AF059528; AAD20951.1; JOINED; Genomic_DNA.
EMBL; AF119297; AAD26810.1; -; mRNA.
EMBL; AY427821; AAR02474.1; -; mRNA.
EMBL; AY750848; AAU81930.1; -; mRNA.
EMBL; AP000753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP006289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK297529; BAH12606.1; -; mRNA.
EMBL; AB209771; BAD93008.1; ALT_INIT; mRNA.
EMBL; AK075412; BAG52134.1; -; mRNA.
EMBL; AK222898; BAD96618.1; -; mRNA.
EMBL; AK295361; BAH12044.1; -; mRNA.
EMBL; CH471076; EAW74170.1; -; Genomic_DNA.
EMBL; BC000634; AAH00634.1; -; mRNA.
EMBL; BC010556; AAH10556.1; -; mRNA.
EMBL; BC011394; AAH11394.1; -; mRNA.
EMBL; BC022993; AAH22993.1; -; mRNA.
EMBL; BC100822; AAI00823.1; -; mRNA.
EMBL; BC100823; AAI00824.1; -; mRNA.
EMBL; BC105981; AAI05982.1; -; mRNA.
EMBL; BC105982; AAI05983.1; -; mRNA.
EMBL; BC118628; AAI18629.1; -; mRNA.
EMBL; BC118550; AAI18551.1; -; mRNA.
EMBL; BK001685; DAA01931.1; -; mRNA.
EMBL; BK001681; DAA01941.1; -; mRNA.
EMBL; BK001684; DAA01943.1; -; mRNA.
CCDS; CCDS41664.1; -. [O95197-4]
CCDS; CCDS58141.1; -. [O95197-1]
CCDS; CCDS58142.1; -. [O95197-7]
CCDS; CCDS58143.1; -. [O95197-6]
CCDS; CCDS8048.1; -. [O95197-5]
CCDS; CCDS8049.1; -. [O95197-3]
CCDS; CCDS8050.1; -. [O95197-2]
RefSeq; NP_001252518.1; NM_001265589.1. [O95197-1]
RefSeq; NP_001252519.1; NM_001265590.1. [O95197-7]
RefSeq; NP_001252520.1; NM_001265591.1. [O95197-6]
RefSeq; NP_006045.1; NM_006054.3. [O95197-3]
RefSeq; NP_958831.1; NM_201428.2. [O95197-2]
RefSeq; NP_958832.1; NM_201429.2. [O95197-4]
RefSeq; NP_958833.1; NM_201430.2. [O95197-5]
UniGene; Hs.743229; -.
ProteinModelPortal; O95197; -.
SMR; O95197; -.
BioGrid; 115598; 29.
CORUM; O95197; -.
IntAct; O95197; 30.
MINT; O95197; -.
STRING; 9606.ENSP00000344106; -.
iPTMnet; O95197; -.
PhosphoSitePlus; O95197; -.
SwissPalm; O95197; -.
BioMuta; RTN3; -.
EPD; O95197; -.
MaxQB; O95197; -.
PaxDb; O95197; -.
PeptideAtlas; O95197; -.
PRIDE; O95197; -.
TopDownProteomics; O95197-2; -. [O95197-2]
TopDownProteomics; O95197-3; -. [O95197-3]
TopDownProteomics; O95197-4; -. [O95197-4]
DNASU; 10313; -.
Ensembl; ENST00000339997; ENSP00000344106; ENSG00000133318. [O95197-2]
Ensembl; ENST00000341307; ENSP00000340903; ENSG00000133318. [O95197-5]
Ensembl; ENST00000354497; ENSP00000346492; ENSG00000133318. [O95197-6]
Ensembl; ENST00000356000; ENSP00000348279; ENSG00000133318. [O95197-4]
Ensembl; ENST00000377819; ENSP00000367050; ENSG00000133318. [O95197-1]
Ensembl; ENST00000537981; ENSP00000440874; ENSG00000133318. [O95197-3]
Ensembl; ENST00000540798; ENSP00000442733; ENSG00000133318. [O95197-7]
GeneID; 10313; -.
KEGG; hsa:10313; -.
UCSC; uc001nxm.3; human. [O95197-1]
CTD; 10313; -.
DisGeNET; 10313; -.
EuPathDB; HostDB:ENSG00000133318.13; -.
GeneCards; RTN3; -.
H-InvDB; HIX0021346; -.
HGNC; HGNC:10469; RTN3.
HPA; HPA015649; -.
HPA; HPA015650; -.
MIM; 604249; gene.
neXtProt; NX_O95197; -.
OpenTargets; ENSG00000133318; -.
PharmGKB; PA34882; -.
eggNOG; KOG1792; Eukaryota.
eggNOG; ENOG410XPKH; LUCA.
GeneTree; ENSGT00390000009934; -.
HOVERGEN; HBG093922; -.
InParanoid; O95197; -.
KO; K20723; -.
OMA; LIHWRDP; -.
OrthoDB; EOG091G0TIO; -.
PhylomeDB; O95197; -.
TreeFam; TF105431; -.
Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
ChiTaRS; RTN3; human.
GeneWiki; RTN3; -.
GenomeRNAi; 10313; -.
PRO; PR:O95197; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000133318; -.
ExpressionAtlas; O95197; baseline and differential.
Genevisible; O95197; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071787; P:endoplasmic reticulum tubular network formation; IDA:UniProtKB.
GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR003388; Reticulon.
Pfam; PF02453; Reticulon; 1.
PROSITE; PS50845; RETICULON; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Complete proteome;
Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Stress response; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895}.
CHAIN 2 1032 Reticulon-3.
/FTId=PRO_0000168163.
TOPO_DOM 2 863 Cytoplasmic. {ECO:0000255}.
INTRAMEM 864 887 Helical. {ECO:0000255}.
TOPO_DOM 888 947 Cytoplasmic. {ECO:0000255}.
INTRAMEM 948 968 Helical. {ECO:0000255}.
TOPO_DOM 969 972 Cytoplasmic. {ECO:0000255}.
INTRAMEM 973 993 Helical. {ECO:0000255}.
TOPO_DOM 994 1032 Cytoplasmic. {ECO:0000255}.
DOMAIN 844 1032 Reticulon. {ECO:0000255|PROSITE-
ProRule:PRU00170}.
REGION 987 1032 Interaction with FADD.
{ECO:0000269|PubMed:17031492}.
REGION 1000 1002 Interaction with BACE1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES97}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000250|UniProtKB:Q6RJR6}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES97}.
VAR_SEQ 48 843 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045319.
VAR_SEQ 48 159 Missing (in isoform 7). {ECO:0000305}.
/FTId=VSP_047008.
VAR_SEQ 48 66 Missing (in isoform 2, isoform 3 and
isoform 5). {ECO:0000303|PubMed:10331947,
ECO:0000303|PubMed:12811824,
ECO:0000303|PubMed:14986927,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15946766,
ECO:0000303|PubMed:16303743,
ECO:0000303|Ref.6}.
/FTId=VSP_023759.
VAR_SEQ 67 843 Missing (in isoform 3, isoform 4 and
isoform 5). {ECO:0000303|PubMed:10331947,
ECO:0000303|PubMed:12811824,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:14986927,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16303743,
ECO:0000303|Ref.6}.
/FTId=VSP_023760.
VAR_SEQ 914 1032 AYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDL
VDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYE
KYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE ->
PRLITMLASPEIRPSQLLKRSKQNSLESPKKRQNKYMETRN
ATVTKTPFNSYNVVTCTMKENTQCQLEPAFQAFFLIWCFLP
SFPFNPQYQAQKLMD (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045320.
VAR_SEQ 999 1032 TQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE -> DPS
KTPWNRQKKGRISTWKPEMQQLLKHHLIVITSLLVL (in
isoform 5). {ECO:0000305}.
/FTId=VSP_023761.
VARIANT 6 6 A -> E (in dbSNP:rs11551944).
{ECO:0000269|PubMed:15946766}.
/FTId=VAR_031164.
VARIANT 501 501 D -> H (in dbSNP:rs7936660).
/FTId=VAR_057713.
CONFLICT 871 871 A -> V (in Ref. 4; BAD93008).
{ECO:0000305}.
SEQUENCE 1032 AA; 112611 MW; 26B372B82BFC6361 CRC64;
MAEPSAATQS HSISSSSFGA EPSAPGGGGS PGACPALGTK SCSSSCADSF VSSSSSQPVS
LFSTSQEGLS SLCSDEPSSE IMTSSFLSSS EIHNTGLTIL HGEKSHVLGS QPILAKEGKD
HLDLLDMKKM EKPQGTSNNV SDSSVSLAAG VHCDRPSIPA SFPEHPAFLS KKIGQVEEQI
DKETKNPNGV SSREAKTALD ADDRFTLLTA QKPPTEYSKV EGIYTYSLSP SKVSGDDVIE
KDSPESPFEV IIDKAAFDKE FKDSYKESTD DFGSWSVHTD KESSEDISET NDKLFPLRNK
EAGRYPMSAL LSRQFSHTNA ALEEVSRCVN DMHNFTNEIL TWDLVPQVKQ QTDKSSDCIT
KTTGLDMSEY NSEIPVVNLK TSTHQKTPVC SIDGSTPITK STGDWAEASL QQENAITGKP
VPDSLNSTKE FSIKGVQGNM QKQDDTLAEL PGSPPEKCDS LGSGVATVKV VLPDDHLKDE
MDWQSSALGE ITEADSSGES DDTVIEDITA DTSFENNKIQ AEKPVSIPSA VVKTGEREIK
EIPSCEREEK TSKNFEELVS DSELHQDQPD ILGRSPASEA ACSKVPDTNV SLEDVSEVAP
EKPITTENPK LPSTVSPNVF NETEFSLNVT TSAYLESLHG KNVKHIDDSS PEDLIAAFTE
TRDKGIVDSE RNAFKAISEK MTDFKTTPPV EVLHENESGG SEIKDIGSKY SEQSKETNGS
EPLGVFPTQG TPVASLDLEQ EQLTIKALKE LGERQVEKST SAQRDAELPS EEVLKQTFTF
APESWPQRSY DILERNVKNG SDLGISQKPI TIRETTRVDA VSSLSKTELV KKHVLARLLT
DFSVHDLIFW RDVKKTGFVF GTTLIMLLSL AAFSVISVVS YLILALLSVT ISFRIYKSVI
QAVQKSEEGH PFKAYLDVDI TLSSEAFHNY MNAAMVHINR ALKLIIRLFL VEDLVDSLKL
AVFMWLMTYV GAVFNGITLL ILAELLIFSV PIVYEKYKTQ IDHYVGIARD QTKSIVEKIQ
AKLPGIAKKK AE


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