Full text data of RTN3
RTN3
(ASYIP, NSPL2)
[Confidence: high (present in two of the MS resources)]
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)
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)
hRBCD
IPI00028946
IPI00028946 Reticulon protein 3 Reticulon protein 3 membrane n/a n/a 2 n/a 2 1 1 3 2 n/a 3 2 n/a 2 n/a n/a n/a 1 1 1 integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00028946 Reticulon protein 3 Reticulon protein 3 membrane n/a n/a 2 n/a 2 1 1 3 2 n/a 3 2 n/a 2 n/a n/a n/a 1 1 1 integral membrane protein n/a found at its expected molecular weight found at molecular weight
Comments
Isoform O95197-2 was detected.
Isoform O95197-2 was detected.
UniProt
O95197
ID RTN3_HUMAN Reviewed; 1032 AA.
AC O95197; B3KQS2; B7Z308; B7Z4M0; F5H774; Q147U9; Q496K2; Q53GN3;
read moreAC Q59EP0; Q5UEP2; Q6T930; Q7RTM7; Q7RTM8; Q7RTN3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Reticulon-3;
DE AltName: Full=Homolog of ASY protein;
DE Short=HAP;
DE AltName: Full=Neuroendocrine-specific protein-like 2;
DE Short=NSP-like protein 2;
DE AltName: Full=Neuroendocrine-specific protein-like II;
DE Short=NSP-like protein II;
DE Short=NSPLII;
GN Name=RTN3; Synonyms=ASYIP, NSPL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10331947; DOI=10.1006/geno.1999.5807;
RA Moreira E.F., Jaworski C.J., Rodriguez I.R.;
RT "Cloning of a novel member of the reticulon gene family (RTN3): gene
RT structure and chromosomal localization to 11q13.";
RL Genomics 58:73-81(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION
RP WITH RTN4, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12811824; DOI=10.1002/jcp.10297;
RA Qi B., Qi Y., Watari A., Yoshioka N., Inoue H., Minemoto Y.,
RA Yamashita K., Sasagawa T., Yutsudo M.;
RT "Pro-apoptotic ASY/Nogo-B protein associates with ASYIP.";
RL J. Cell. Physiol. 196:312-318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=14986927;
RA Huang X., Yang H., Zhou Y., Liu J., Yin B., Peng X., Qiang B.,
RA Yuan J.;
RT "Overexpression of human reticulon 3 (hRTN3) in astrocytoma.";
RL Clin. Neuropathol. 23:1-7(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANT GLU-6.
RC TISSUE=Brain;
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
RT distribution in adult mouse brain.";
RL Brain Res. Mol. Brain Res. 138:236-243(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC TISSUE=Brain, and Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, Eye, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP IDENTIFICATION (ISOFORMS 3; 4 AND 5).
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 [12]
RP INTERACTION WITH BACE1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=15286784; DOI=10.1038/nm1088;
RA He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.;
RT "Reticulon family members modulate BACE1 activity and amyloid-beta
RT peptide generation.";
RL Nat. Med. 10:959-965(2004).
RN [13]
RP HOMODIMERIZATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16054885; DOI=10.1016/j.bbrc.2005.07.012;
RA Wakana Y., Koyama S., Nakajima K., Hatsuzawa K., Nagahama M., Tani K.,
RA Hauri H.-P., Melancon P., Tagaya M.;
RT "Reticulon 3 is involved in membrane trafficking between the
RT endoplasmic reticulum and Golgi.";
RL Biochem. Biophys. Res. Commun. 334:1198-1205(2005).
RN [14]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=15350194; DOI=10.1042/BJ20040458;
RA Di Scala F., Dupuis L., Gaiddon C., De Tapia M., Jokic N.,
RA Gonzalez de Aguilar J.-L., Raul J.-S., Ludes B., Loeffler J.-P.;
RT "Tissue specificity and regulation of the N-terminal diversity of
RT reticulon 3.";
RL Biochem. J. 385:125-134(2005).
RN [15]
RP INTERACTION WITH FADD, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17031492; DOI=10.1007/s10495-006-0082-0;
RA Xiang R., Liu Y., Zhu L., Dong W., Qi Y.;
RT "Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling
RT complexes.";
RL Apoptosis 11:1923-1932(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [17]
RP INTERACTION WITH BACE1 AND BACE2.
RX PubMed=16965550; DOI=10.1111/j.1460-9568.2006.05005.x;
RA Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.;
RT "Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its
RT ability to produce amyloid beta-protein.";
RL Eur. J. Neurosci. 24:1237-1244(2006).
RN [18]
RP HOMODIMERIZATION, INTERACTION WITH BACE1 AND RTN4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16979658; DOI=10.1016/j.jmb.2006.07.094;
RA He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.;
RT "Mapping of interaction domains mediating binding between BACE1 and
RT RTN/Nogo proteins.";
RL J. Mol. Biol. 363:625-634(2006).
RN [19]
RP INDUCTION BY ER STRESS, INTERACTION WITH BCL2, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=17191123; DOI=10.1007/s10495-006-0574-y;
RA Wan Q., Kuang E., Dong W., Zhou S., Xu H., Qi Y., Liu Y.;
RT "Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response
RT to endoplasmic reticulum stress.";
RL Apoptosis 12:319-328(2007).
RN [20]
RP INTERACTION WITH COXSACKIEVIRUS A16 P2C; POLIOVIRUS P2C AND
RP ENTEROVIRUS 71 P2C, AND SUBCELLULAR LOCATION.
RX PubMed=17182608; DOI=10.1074/jbc.M611145200;
RA Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
RA Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
RT "Reticulon 3 binds the 2C protein of enterovirus 71 and is required
RT for viral replication.";
RL J. Biol. Chem. 282:5888-5898(2007).
RN [21]
RP TOPOLOGY.
RX PubMed=17699523; DOI=10.1074/jbc.M704181200;
RA He W., Shi Q., Hu X., Yan R.;
RT "The membrane topology of RTN3 and its effect on binding of RTN3 to
RT BACE1.";
RL J. Biol. Chem. 282:29144-29151(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-650, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP INTERACTION WITH ATL2.
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
RT tubular ER network.";
RL Cell 138:549-561(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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.
CC May favor BCL2 translocation to the mitochondria upon endoplasmic
CC reticulum stress. In case of enteroviruses infection, RTN3 may be
CC involved in the viral replication or pathogenesis.
CC -!- SUBUNIT: Homodimer. Interacts with ATL1 (By similarity). Interacts
CC with RTN4. Isoform 3 interacts with BACE1, BACE2, BCL2 and FADD.
CC Interacts with Coxsackievirus A16, enterovirus 71 and poliovirus
CC P2C proteins. Interacts with ATL2.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=A1, A4b;
CC IsoId=O95197-1; Sequence=Displayed;
CC Name=2; Synonyms=A2, A3b;
CC IsoId=O95197-2; Sequence=VSP_023759;
CC Name=3; Synonyms=B1, A1;
CC IsoId=O95197-3; Sequence=VSP_023759, VSP_023760;
CC Name=4; Synonyms=B2, A2;
CC IsoId=O95197-4; Sequence=VSP_023760;
CC Name=5;
CC IsoId=O95197-5; Sequence=VSP_023759, VSP_023760, VSP_023761;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=O95197-6; Sequence=VSP_045319, VSP_045320;
CC Name=7;
CC IsoId=O95197-7; Sequence=VSP_047008;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Isoform 3 is widely expressed, with highest
CC levels in brain, where it is enriched in neuronal cell bodies from
CC gray matter (at protein level). Three times more abundant in
CC macula than in peripheral retina. Isoform 1 is expressed at high
CC levels in brain and at low levels in skeletal muscle. Isoform 2 is
CC only found in melanoma.
CC -!- INDUCTION: By endoplasmic reticulum stress (at protein level).
CC -!- SIMILARITY: Contains 1 reticulon domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93008.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AF059524; AAC99319.1; -; mRNA.
DR EMBL; AF059529; AAD20951.1; -; Genomic_DNA.
DR EMBL; AF059525; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF059526; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF059527; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF059528; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF119297; AAD26810.1; -; mRNA.
DR EMBL; AY427821; AAR02474.1; -; mRNA.
DR EMBL; AY750848; AAU81930.1; -; mRNA.
DR EMBL; AP000753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP006289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK297529; BAH12606.1; -; mRNA.
DR EMBL; AB209771; BAD93008.1; ALT_INIT; mRNA.
DR EMBL; AK075412; BAG52134.1; -; mRNA.
DR EMBL; AK222898; BAD96618.1; -; mRNA.
DR EMBL; AK295361; BAH12044.1; -; mRNA.
DR EMBL; CH471076; EAW74170.1; -; Genomic_DNA.
DR EMBL; BC000634; AAH00634.1; -; mRNA.
DR EMBL; BC010556; AAH10556.1; -; mRNA.
DR EMBL; BC011394; AAH11394.1; -; mRNA.
DR EMBL; BC022993; AAH22993.1; -; mRNA.
DR EMBL; BC100822; AAI00823.1; -; mRNA.
DR EMBL; BC100823; AAI00824.1; -; mRNA.
DR EMBL; BC105981; AAI05982.1; -; mRNA.
DR EMBL; BC105982; AAI05983.1; -; mRNA.
DR EMBL; BC118628; AAI18629.1; -; mRNA.
DR EMBL; BC118550; AAI18551.1; -; mRNA.
DR EMBL; BK001685; DAA01931.1; -; mRNA.
DR EMBL; BK001681; DAA01941.1; -; mRNA.
DR EMBL; BK001684; DAA01943.1; -; mRNA.
DR RefSeq; NP_001252518.1; NM_001265589.1.
DR RefSeq; NP_001252519.1; NM_001265590.1.
DR RefSeq; NP_001252520.1; NM_001265591.1.
DR RefSeq; NP_006045.1; NM_006054.3.
DR RefSeq; NP_958831.1; NM_201428.2.
DR RefSeq; NP_958832.1; NM_201429.2.
DR RefSeq; NP_958833.1; NM_201430.2.
DR UniGene; Hs.743229; -.
DR ProteinModelPortal; O95197; -.
DR SMR; O95197; 894-959.
DR IntAct; O95197; 12.
DR MINT; MINT-5000642; -.
DR PhosphoSite; O95197; -.
DR PaxDb; O95197; -.
DR PRIDE; O95197; -.
DR DNASU; 10313; -.
DR Ensembl; ENST00000339997; ENSP00000344106; ENSG00000133318.
DR Ensembl; ENST00000341307; ENSP00000340903; ENSG00000133318.
DR Ensembl; ENST00000354497; ENSP00000346492; ENSG00000133318.
DR Ensembl; ENST00000356000; ENSP00000348279; ENSG00000133318.
DR Ensembl; ENST00000377819; ENSP00000367050; ENSG00000133318.
DR Ensembl; ENST00000537981; ENSP00000440874; ENSG00000133318.
DR Ensembl; ENST00000540798; ENSP00000442733; ENSG00000133318.
DR GeneID; 10313; -.
DR KEGG; hsa:10313; -.
DR UCSC; uc010rmu.2; human.
DR CTD; 10313; -.
DR GeneCards; GC11P063448; -.
DR H-InvDB; HIX0021346; -.
DR HGNC; HGNC:10469; RTN3.
DR HPA; HPA015649; -.
DR HPA; HPA015650; -.
DR MIM; 604249; gene.
DR neXtProt; NX_O95197; -.
DR PharmGKB; PA34882; -.
DR eggNOG; NOG303514; -.
DR HOVERGEN; HBG093922; -.
DR InParanoid; O95197; -.
DR OMA; KGRISTW; -.
DR OrthoDB; EOG7CZK7J; -.
DR ChiTaRS; RTN3; human.
DR GeneWiki; RTN3; -.
DR GenomeRNAi; 10313; -.
DR NextBio; 39085; -.
DR PRO; PR:O95197; -.
DR ArrayExpress; O95197; -.
DR Bgee; O95197; -.
DR Genevestigator; O95197; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR003388; Reticulon.
DR PANTHER; PTHR10994; PTHR10994; 1.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1032 Reticulon-3.
FT /FTId=PRO_0000168163.
FT TOPO_DOM 2 863 Cytoplasmic (Potential).
FT INTRAMEM 864 887 Helical; (Potential).
FT TOPO_DOM 888 947 Cytoplasmic (Potential).
FT INTRAMEM 948 968 Helical; (Potential).
FT TOPO_DOM 969 972 Cytoplasmic (Potential).
FT INTRAMEM 973 993 Helical; (Potential).
FT TOPO_DOM 994 1032 Cytoplasmic (Potential).
FT DOMAIN 844 1032 Reticulon.
FT REGION 987 1032 Interaction with FADD.
FT REGION 1000 1002 Interaction with BACE1.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 649 649 Phosphoserine.
FT MOD_RES 650 650 Phosphoserine.
FT VAR_SEQ 48 843 Missing (in isoform 6).
FT /FTId=VSP_045319.
FT VAR_SEQ 48 159 Missing (in isoform 7).
FT /FTId=VSP_047008.
FT VAR_SEQ 48 66 Missing (in isoform 2, isoform 3 and
FT isoform 5).
FT /FTId=VSP_023759.
FT VAR_SEQ 67 843 Missing (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_023760.
FT VAR_SEQ 914 1032 AYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDL
FT VDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYE
FT KYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE ->
FT PRLITMLASPEIRPSQLLKRSKQNSLESPKKRQNKYMETRN
FT ATVTKTPFNSYNVVTCTMKENTQCQLEPAFQAFFLIWCFLP
FT SFPFNPQYQAQKLMD (in isoform 6).
FT /FTId=VSP_045320.
FT VAR_SEQ 999 1032 TQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE -> DPS
FT KTPWNRQKKGRISTWKPEMQQLLKHHLIVITSLLVL (in
FT isoform 5).
FT /FTId=VSP_023761.
FT VARIANT 6 6 A -> E (in dbSNP:rs11551944).
FT /FTId=VAR_031164.
FT VARIANT 501 501 D -> H (in dbSNP:rs7936660).
FT /FTId=VAR_057713.
FT CONFLICT 871 871 A -> V (in Ref. 4; BAD93008).
SQ 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
//
ID RTN3_HUMAN Reviewed; 1032 AA.
AC O95197; B3KQS2; B7Z308; B7Z4M0; F5H774; Q147U9; Q496K2; Q53GN3;
read moreAC Q59EP0; Q5UEP2; Q6T930; Q7RTM7; Q7RTM8; Q7RTN3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Reticulon-3;
DE AltName: Full=Homolog of ASY protein;
DE Short=HAP;
DE AltName: Full=Neuroendocrine-specific protein-like 2;
DE Short=NSP-like protein 2;
DE AltName: Full=Neuroendocrine-specific protein-like II;
DE Short=NSP-like protein II;
DE Short=NSPLII;
GN Name=RTN3; Synonyms=ASYIP, NSPL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10331947; DOI=10.1006/geno.1999.5807;
RA Moreira E.F., Jaworski C.J., Rodriguez I.R.;
RT "Cloning of a novel member of the reticulon gene family (RTN3): gene
RT structure and chromosomal localization to 11q13.";
RL Genomics 58:73-81(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION
RP WITH RTN4, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12811824; DOI=10.1002/jcp.10297;
RA Qi B., Qi Y., Watari A., Yoshioka N., Inoue H., Minemoto Y.,
RA Yamashita K., Sasagawa T., Yutsudo M.;
RT "Pro-apoptotic ASY/Nogo-B protein associates with ASYIP.";
RL J. Cell. Physiol. 196:312-318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=14986927;
RA Huang X., Yang H., Zhou Y., Liu J., Yin B., Peng X., Qiang B.,
RA Yuan J.;
RT "Overexpression of human reticulon 3 (hRTN3) in astrocytoma.";
RL Clin. Neuropathol. 23:1-7(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANT GLU-6.
RC TISSUE=Brain;
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
RT distribution in adult mouse brain.";
RL Brain Res. Mol. Brain Res. 138:236-243(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC TISSUE=Brain, and Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, Eye, and Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP IDENTIFICATION (ISOFORMS 3; 4 AND 5).
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 [12]
RP INTERACTION WITH BACE1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=15286784; DOI=10.1038/nm1088;
RA He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.;
RT "Reticulon family members modulate BACE1 activity and amyloid-beta
RT peptide generation.";
RL Nat. Med. 10:959-965(2004).
RN [13]
RP HOMODIMERIZATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16054885; DOI=10.1016/j.bbrc.2005.07.012;
RA Wakana Y., Koyama S., Nakajima K., Hatsuzawa K., Nagahama M., Tani K.,
RA Hauri H.-P., Melancon P., Tagaya M.;
RT "Reticulon 3 is involved in membrane trafficking between the
RT endoplasmic reticulum and Golgi.";
RL Biochem. Biophys. Res. Commun. 334:1198-1205(2005).
RN [14]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=15350194; DOI=10.1042/BJ20040458;
RA Di Scala F., Dupuis L., Gaiddon C., De Tapia M., Jokic N.,
RA Gonzalez de Aguilar J.-L., Raul J.-S., Ludes B., Loeffler J.-P.;
RT "Tissue specificity and regulation of the N-terminal diversity of
RT reticulon 3.";
RL Biochem. J. 385:125-134(2005).
RN [15]
RP INTERACTION WITH FADD, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17031492; DOI=10.1007/s10495-006-0082-0;
RA Xiang R., Liu Y., Zhu L., Dong W., Qi Y.;
RT "Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling
RT complexes.";
RL Apoptosis 11:1923-1932(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [17]
RP INTERACTION WITH BACE1 AND BACE2.
RX PubMed=16965550; DOI=10.1111/j.1460-9568.2006.05005.x;
RA Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.;
RT "Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its
RT ability to produce amyloid beta-protein.";
RL Eur. J. Neurosci. 24:1237-1244(2006).
RN [18]
RP HOMODIMERIZATION, INTERACTION WITH BACE1 AND RTN4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16979658; DOI=10.1016/j.jmb.2006.07.094;
RA He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.;
RT "Mapping of interaction domains mediating binding between BACE1 and
RT RTN/Nogo proteins.";
RL J. Mol. Biol. 363:625-634(2006).
RN [19]
RP INDUCTION BY ER STRESS, INTERACTION WITH BCL2, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=17191123; DOI=10.1007/s10495-006-0574-y;
RA Wan Q., Kuang E., Dong W., Zhou S., Xu H., Qi Y., Liu Y.;
RT "Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response
RT to endoplasmic reticulum stress.";
RL Apoptosis 12:319-328(2007).
RN [20]
RP INTERACTION WITH COXSACKIEVIRUS A16 P2C; POLIOVIRUS P2C AND
RP ENTEROVIRUS 71 P2C, AND SUBCELLULAR LOCATION.
RX PubMed=17182608; DOI=10.1074/jbc.M611145200;
RA Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H.,
RA Lin K.-H., Lai H.-C., Tang P., Horng J.-T.;
RT "Reticulon 3 binds the 2C protein of enterovirus 71 and is required
RT for viral replication.";
RL J. Biol. Chem. 282:5888-5898(2007).
RN [21]
RP TOPOLOGY.
RX PubMed=17699523; DOI=10.1074/jbc.M704181200;
RA He W., Shi Q., Hu X., Yan R.;
RT "The membrane topology of RTN3 and its effect on binding of RTN3 to
RT BACE1.";
RL J. Biol. Chem. 282:29144-29151(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-650, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP INTERACTION WITH ATL2.
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
RT tubular ER network.";
RL Cell 138:549-561(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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.
CC May favor BCL2 translocation to the mitochondria upon endoplasmic
CC reticulum stress. In case of enteroviruses infection, RTN3 may be
CC involved in the viral replication or pathogenesis.
CC -!- SUBUNIT: Homodimer. Interacts with ATL1 (By similarity). Interacts
CC with RTN4. Isoform 3 interacts with BACE1, BACE2, BCL2 and FADD.
CC Interacts with Coxsackievirus A16, enterovirus 71 and poliovirus
CC P2C proteins. Interacts with ATL2.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=A1, A4b;
CC IsoId=O95197-1; Sequence=Displayed;
CC Name=2; Synonyms=A2, A3b;
CC IsoId=O95197-2; Sequence=VSP_023759;
CC Name=3; Synonyms=B1, A1;
CC IsoId=O95197-3; Sequence=VSP_023759, VSP_023760;
CC Name=4; Synonyms=B2, A2;
CC IsoId=O95197-4; Sequence=VSP_023760;
CC Name=5;
CC IsoId=O95197-5; Sequence=VSP_023759, VSP_023760, VSP_023761;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=O95197-6; Sequence=VSP_045319, VSP_045320;
CC Name=7;
CC IsoId=O95197-7; Sequence=VSP_047008;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Isoform 3 is widely expressed, with highest
CC levels in brain, where it is enriched in neuronal cell bodies from
CC gray matter (at protein level). Three times more abundant in
CC macula than in peripheral retina. Isoform 1 is expressed at high
CC levels in brain and at low levels in skeletal muscle. Isoform 2 is
CC only found in melanoma.
CC -!- INDUCTION: By endoplasmic reticulum stress (at protein level).
CC -!- SIMILARITY: Contains 1 reticulon domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93008.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AF059524; AAC99319.1; -; mRNA.
DR EMBL; AF059529; AAD20951.1; -; Genomic_DNA.
DR EMBL; AF059525; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF059526; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF059527; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF059528; AAD20951.1; JOINED; Genomic_DNA.
DR EMBL; AF119297; AAD26810.1; -; mRNA.
DR EMBL; AY427821; AAR02474.1; -; mRNA.
DR EMBL; AY750848; AAU81930.1; -; mRNA.
DR EMBL; AP000753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP006289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK297529; BAH12606.1; -; mRNA.
DR EMBL; AB209771; BAD93008.1; ALT_INIT; mRNA.
DR EMBL; AK075412; BAG52134.1; -; mRNA.
DR EMBL; AK222898; BAD96618.1; -; mRNA.
DR EMBL; AK295361; BAH12044.1; -; mRNA.
DR EMBL; CH471076; EAW74170.1; -; Genomic_DNA.
DR EMBL; BC000634; AAH00634.1; -; mRNA.
DR EMBL; BC010556; AAH10556.1; -; mRNA.
DR EMBL; BC011394; AAH11394.1; -; mRNA.
DR EMBL; BC022993; AAH22993.1; -; mRNA.
DR EMBL; BC100822; AAI00823.1; -; mRNA.
DR EMBL; BC100823; AAI00824.1; -; mRNA.
DR EMBL; BC105981; AAI05982.1; -; mRNA.
DR EMBL; BC105982; AAI05983.1; -; mRNA.
DR EMBL; BC118628; AAI18629.1; -; mRNA.
DR EMBL; BC118550; AAI18551.1; -; mRNA.
DR EMBL; BK001685; DAA01931.1; -; mRNA.
DR EMBL; BK001681; DAA01941.1; -; mRNA.
DR EMBL; BK001684; DAA01943.1; -; mRNA.
DR RefSeq; NP_001252518.1; NM_001265589.1.
DR RefSeq; NP_001252519.1; NM_001265590.1.
DR RefSeq; NP_001252520.1; NM_001265591.1.
DR RefSeq; NP_006045.1; NM_006054.3.
DR RefSeq; NP_958831.1; NM_201428.2.
DR RefSeq; NP_958832.1; NM_201429.2.
DR RefSeq; NP_958833.1; NM_201430.2.
DR UniGene; Hs.743229; -.
DR ProteinModelPortal; O95197; -.
DR SMR; O95197; 894-959.
DR IntAct; O95197; 12.
DR MINT; MINT-5000642; -.
DR PhosphoSite; O95197; -.
DR PaxDb; O95197; -.
DR PRIDE; O95197; -.
DR DNASU; 10313; -.
DR Ensembl; ENST00000339997; ENSP00000344106; ENSG00000133318.
DR Ensembl; ENST00000341307; ENSP00000340903; ENSG00000133318.
DR Ensembl; ENST00000354497; ENSP00000346492; ENSG00000133318.
DR Ensembl; ENST00000356000; ENSP00000348279; ENSG00000133318.
DR Ensembl; ENST00000377819; ENSP00000367050; ENSG00000133318.
DR Ensembl; ENST00000537981; ENSP00000440874; ENSG00000133318.
DR Ensembl; ENST00000540798; ENSP00000442733; ENSG00000133318.
DR GeneID; 10313; -.
DR KEGG; hsa:10313; -.
DR UCSC; uc010rmu.2; human.
DR CTD; 10313; -.
DR GeneCards; GC11P063448; -.
DR H-InvDB; HIX0021346; -.
DR HGNC; HGNC:10469; RTN3.
DR HPA; HPA015649; -.
DR HPA; HPA015650; -.
DR MIM; 604249; gene.
DR neXtProt; NX_O95197; -.
DR PharmGKB; PA34882; -.
DR eggNOG; NOG303514; -.
DR HOVERGEN; HBG093922; -.
DR InParanoid; O95197; -.
DR OMA; KGRISTW; -.
DR OrthoDB; EOG7CZK7J; -.
DR ChiTaRS; RTN3; human.
DR GeneWiki; RTN3; -.
DR GenomeRNAi; 10313; -.
DR NextBio; 39085; -.
DR PRO; PR:O95197; -.
DR ArrayExpress; O95197; -.
DR Bgee; O95197; -.
DR Genevestigator; O95197; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR003388; Reticulon.
DR PANTHER; PTHR10994; PTHR10994; 1.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Complete proteome;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Host-virus interaction; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1032 Reticulon-3.
FT /FTId=PRO_0000168163.
FT TOPO_DOM 2 863 Cytoplasmic (Potential).
FT INTRAMEM 864 887 Helical; (Potential).
FT TOPO_DOM 888 947 Cytoplasmic (Potential).
FT INTRAMEM 948 968 Helical; (Potential).
FT TOPO_DOM 969 972 Cytoplasmic (Potential).
FT INTRAMEM 973 993 Helical; (Potential).
FT TOPO_DOM 994 1032 Cytoplasmic (Potential).
FT DOMAIN 844 1032 Reticulon.
FT REGION 987 1032 Interaction with FADD.
FT REGION 1000 1002 Interaction with BACE1.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 649 649 Phosphoserine.
FT MOD_RES 650 650 Phosphoserine.
FT VAR_SEQ 48 843 Missing (in isoform 6).
FT /FTId=VSP_045319.
FT VAR_SEQ 48 159 Missing (in isoform 7).
FT /FTId=VSP_047008.
FT VAR_SEQ 48 66 Missing (in isoform 2, isoform 3 and
FT isoform 5).
FT /FTId=VSP_023759.
FT VAR_SEQ 67 843 Missing (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_023760.
FT VAR_SEQ 914 1032 AYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDL
FT VDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYE
FT KYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE ->
FT PRLITMLASPEIRPSQLLKRSKQNSLESPKKRQNKYMETRN
FT ATVTKTPFNSYNVVTCTMKENTQCQLEPAFQAFFLIWCFLP
FT SFPFNPQYQAQKLMD (in isoform 6).
FT /FTId=VSP_045320.
FT VAR_SEQ 999 1032 TQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE -> DPS
FT KTPWNRQKKGRISTWKPEMQQLLKHHLIVITSLLVL (in
FT isoform 5).
FT /FTId=VSP_023761.
FT VARIANT 6 6 A -> E (in dbSNP:rs11551944).
FT /FTId=VAR_031164.
FT VARIANT 501 501 D -> H (in dbSNP:rs7936660).
FT /FTId=VAR_057713.
FT CONFLICT 871 871 A -> V (in Ref. 4; BAD93008).
SQ 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
//
MIM
604249
*RECORD*
*FIELD* NO
604249
*FIELD* TI
*604249 RETICULON 3; RTN3
;;NEUROENDOCRINE-SPECIFIC PROTEIN-LIKE 2; NSPL2
*FIELD* TX
read more
DESCRIPTION
The reticulons are a group of highly conserved genes with preferential
expression in neuroendocrine tissues (see, e.g., RTN1; 600865).
CLONING
During a subtraction cloning between macula and peripheral retina,
Moreira et al. (1999) isolated a novel member of the reticulon gene
family, which they designated reticulon-3. The mRNA for RTN3 was
approximately 3-fold more abundant in macula than in peripheral retina.
The 2,527-bp cDNA encodes a predicted 236-amino acid protein that shows
strong sequence similarity with other members of the RTN gene family
(see, e.g., 600865). Northern blot analysis showed that RTN3 is widely
expressed in human tissues, with highest expression in the brain.
GENE STRUCTURE
Moreira et al. (1999) determined that the RTN3 gene contains 7 exons and
spans more than 15 kb.
MAPPING
By use of somatic cell hybrid and radiation hybrid panels, Moreira et
al. (1999) mapped the RTN3 gene to 11q13, between markers D11S4535 and
D11S4627. Southern blot analysis identified the presence of at least one
pseudogene that was subsequently localized to chromosome 4.
GENE FUNCTION
He et al. (2004) found that BACE1 (604252) coimmunoprecipitated with
members of the reticulon family of proteins: RTN1, RTN2 (603183), RTN3,
and RTN4 (604475). BACE1 colocalized with RTN3 in neurons of human brain
gray matter, and with RTN4 in oligodendrocytes in white matter.
Overexpression of RTN3 in vitro inhibited BACE1 activity and decreased
amyloid precursor protein (APP; 104760) processing. The findings
suggested that reticulon proteins are negative modulators of BACE1
activity, and that RTN3 specifically blocks access of BACE1 to APP
within neurons.
MOLECULAR GENETICS
Windpassinger et al. (2003) excluded RTN3 as the gene mutant in Silver
spastic paraplegia syndrome (270685), the locus for which maps to
11q12-q14, as no mutations in RTN3 were found on sequence analysis of at
least 2 affected individuals from each of 4 different families and 1
healthy control.
*FIELD* RF
1. He, W.; Lu, Y.; Qahwash, I.; Hu, X.-Y.; Chang, A.; Yan, R.: Reticulon
family members modulate BACE1 activity and amyloid-beta peptide generation. Nature
Med. 10: 959-965, 2004.
2. 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.
3. Windpassinger, C.; Wagner, K.; Petek, E.; Fischer, R.; Auer-Grumbach,
M.: Refinement of the 'Silver syndrome locus' on chromosome 11q12-q14
in four families and exclusion of eight candidate genes. Hum. Genet. 114:
99-109, 2003.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/27/2004
Victor A. McKusick - updated: 12/9/2003
*FIELD* CD
Wilson H. Y. Lo: 10/20/1999
*FIELD* ED
tkritzer: 09/28/2004
ckniffin: 9/27/2004
tkritzer: 12/16/2003
terry: 12/9/2003
carol: 10/20/1999
*RECORD*
*FIELD* NO
604249
*FIELD* TI
*604249 RETICULON 3; RTN3
;;NEUROENDOCRINE-SPECIFIC PROTEIN-LIKE 2; NSPL2
*FIELD* TX
read more
DESCRIPTION
The reticulons are a group of highly conserved genes with preferential
expression in neuroendocrine tissues (see, e.g., RTN1; 600865).
CLONING
During a subtraction cloning between macula and peripheral retina,
Moreira et al. (1999) isolated a novel member of the reticulon gene
family, which they designated reticulon-3. The mRNA for RTN3 was
approximately 3-fold more abundant in macula than in peripheral retina.
The 2,527-bp cDNA encodes a predicted 236-amino acid protein that shows
strong sequence similarity with other members of the RTN gene family
(see, e.g., 600865). Northern blot analysis showed that RTN3 is widely
expressed in human tissues, with highest expression in the brain.
GENE STRUCTURE
Moreira et al. (1999) determined that the RTN3 gene contains 7 exons and
spans more than 15 kb.
MAPPING
By use of somatic cell hybrid and radiation hybrid panels, Moreira et
al. (1999) mapped the RTN3 gene to 11q13, between markers D11S4535 and
D11S4627. Southern blot analysis identified the presence of at least one
pseudogene that was subsequently localized to chromosome 4.
GENE FUNCTION
He et al. (2004) found that BACE1 (604252) coimmunoprecipitated with
members of the reticulon family of proteins: RTN1, RTN2 (603183), RTN3,
and RTN4 (604475). BACE1 colocalized with RTN3 in neurons of human brain
gray matter, and with RTN4 in oligodendrocytes in white matter.
Overexpression of RTN3 in vitro inhibited BACE1 activity and decreased
amyloid precursor protein (APP; 104760) processing. The findings
suggested that reticulon proteins are negative modulators of BACE1
activity, and that RTN3 specifically blocks access of BACE1 to APP
within neurons.
MOLECULAR GENETICS
Windpassinger et al. (2003) excluded RTN3 as the gene mutant in Silver
spastic paraplegia syndrome (270685), the locus for which maps to
11q12-q14, as no mutations in RTN3 were found on sequence analysis of at
least 2 affected individuals from each of 4 different families and 1
healthy control.
*FIELD* RF
1. He, W.; Lu, Y.; Qahwash, I.; Hu, X.-Y.; Chang, A.; Yan, R.: Reticulon
family members modulate BACE1 activity and amyloid-beta peptide generation. Nature
Med. 10: 959-965, 2004.
2. 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.
3. Windpassinger, C.; Wagner, K.; Petek, E.; Fischer, R.; Auer-Grumbach,
M.: Refinement of the 'Silver syndrome locus' on chromosome 11q12-q14
in four families and exclusion of eight candidate genes. Hum. Genet. 114:
99-109, 2003.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/27/2004
Victor A. McKusick - updated: 12/9/2003
*FIELD* CD
Wilson H. Y. Lo: 10/20/1999
*FIELD* ED
tkritzer: 09/28/2004
ckniffin: 9/27/2004
tkritzer: 12/16/2003
terry: 12/9/2003
carol: 10/20/1999