RTN1_HUMAN
ID RTN1_HUMAN Reviewed; 776 AA.
AC Q16799; Q16800; Q16801; Q5BKZ4; Q9BQ59;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Reticulon-1;
DE AltName: Full=Neuroendocrine-specific protein;
GN Name=RTN1; Synonyms=NSP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RTN1-A; RTN1-B AND RTN1-C).
RC TISSUE=Lung carcinoma;
RX PubMed=7685762; DOI=10.1016/s0021-9258(19)38669-7;
RA Roebroek A.J.M., Van de Velde H.J.K., Van Bokhoven A., Broers J.L.V.,
RA Ramaekers F.C.S., Van de Ven W.J.M.;
RT "Cloning and expression of alternative transcripts of a novel
RT neuroendocrine-specific gene and identification of its 135-kDa
RT translational product.";
RL J. Biol. Chem. 268:13439-13447(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS RTN1-A AND RTN1-C).
RC TISSUE=Lung, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ALTERNATIVE SPLICING.
RX PubMed=8833145; DOI=10.1006/geno.1996.0105;
RA Roebroek A.J.M., Ayoubi T.A.Y., Van de Velde H.J.K., Schoenmakers E.F.P.M.,
RA Pauli I.G.L., Van de Ven W.J.M.;
RT "Genomic organization of the human NSP gene, prototype of a novel gene
RT family encoding reticulons.";
RL Genomics 32:191-199(1996).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9560466; DOI=10.1007/s004410051054;
RA Hens J., Nuydens R., Geerts H., Senden N.H., Van de Ven W.J.M.,
RA Roebroek A.J., van de Velde H.J.K., Ramaekers F.C., Broers J.L.;
RT "Neuronal differentiation is accompanied by NSP-C expression.";
RL Cell Tissue Res. 292:229-237(1998).
RN [6]
RP INTERACTION WITH UGCG, AND SUBCELLULAR LOCATION.
RX PubMed=12873973;
RA Di Sano F., Fazi B., Citro G., Lovat P.E., Cesareni G., Piacentini M.;
RT "Glucosylceramide synthase and its functional interaction with RTN-1C
RT regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells.";
RL Cancer Res. 63:3860-3865(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH BACE1.
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 peptide
RT generation.";
RL Nat. Med. 10:959-965(2004).
RN [8]
RP INTERACTION WITH NDRG1.
RX PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
RA Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F.,
RA Kremensky I., Kalaydjieva L.;
RT "NDRG1 interacts with APO A-I and A-II and is a functional candidate for
RT the HDL-C QTL on 8q24.";
RL Biochem. Biophys. Res. Commun. 332:982-992(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP INTERACTION WITH TMEM33.
RX PubMed=25612671;
RA Urade T., Yamamoto Y., Zhang X., Ku Y., Sakisaka T.;
RT "Identification and characterization of TMEM33 as a reticulon-binding
RT protein.";
RL Kobe J. Med. Sci. 60:E57-E65(2014).
CC -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC blocking BACE1 activity. {ECO:0000269|PubMed:15286784}.
CC -!- SUBUNIT: Interacts with NDRG1 (PubMed:15922294). Interacts with BACE1
CC (PubMed:15286784). {ECO:0000269|PubMed:15286784,
CC ECO:0000269|PubMed:15922294}.
CC -!- SUBUNIT: [Isoform RTN1-A]: Interacts with TMEM33 (PubMed:25612671).
CC {ECO:0000269|PubMed:25612671}.
CC -!- SUBUNIT: [Isoform RTN1-C]: Interacts with UGCG; regulates the ceramide
CC glucosyltransferase activity of UGCG (PubMed:12873973).
CC {ECO:0000269|PubMed:12873973}.
CC -!- INTERACTION:
CC Q16799-3; P42858: HTT; NbExp=9; IntAct=EBI-10180131, EBI-466029;
CC Q16799-3; P55145: MANF; NbExp=4; IntAct=EBI-10180131, EBI-1044104;
CC Q16799-3; O00560: SDCBP; NbExp=3; IntAct=EBI-10180131, EBI-727004;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12873973}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:12873973};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=RTN1-A; Synonyms=NSP-A;
CC IsoId=Q16799-1; Sequence=Displayed;
CC Name=RTN1-B; Synonyms=NSP-B;
CC IsoId=Q16799-2; Sequence=VSP_005644;
CC Name=RTN1-C; Synonyms=NSP-C;
CC IsoId=Q16799-3; Sequence=VSP_005645, VSP_005646;
CC -!- TISSUE SPECIFICITY: Expressed in neural and neuroendocrine tissues and
CC cell cultures derived therefrom. Expression of isoform RTN1-C is
CC strongly correlated with neuronal differentiation.
CC {ECO:0000269|PubMed:9560466}.
CC -!- PTM: Isoforms RTN1-A and RTN1-B are phosphorylated.
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DR EMBL; L10333; AAA59950.1; -; mRNA.
DR EMBL; L10334; AAA59951.1; -; mRNA.
DR EMBL; L10335; AAA59952.1; -; mRNA.
DR EMBL; CH471061; EAW80762.1; -; Genomic_DNA.
DR EMBL; BC090862; AAH90862.1; -; mRNA.
DR EMBL; BC000314; AAH00314.2; -; mRNA.
DR EMBL; BC003003; AAH03003.2; -; mRNA.
DR CCDS; CCDS9740.1; -. [Q16799-1]
DR CCDS; CCDS9741.1; -. [Q16799-3]
DR PIR; A46583; A46583.
DR PIR; I60904; I60904.
DR RefSeq; NP_066959.1; NM_021136.2. [Q16799-1]
DR RefSeq; NP_996734.1; NM_206852.2. [Q16799-3]
DR AlphaFoldDB; Q16799; -.
DR SMR; Q16799; -.
DR BioGRID; 112165; 110.
DR IntAct; Q16799; 42.
DR MINT; Q16799; -.
DR STRING; 9606.ENSP00000267484; -.
DR TCDB; 8.A.102.1.9; the reticulon (reticulon) family.
DR GlyGen; Q16799; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16799; -.
DR PhosphoSitePlus; Q16799; -.
DR SwissPalm; Q16799; -.
DR BioMuta; RTN1; -.
DR DMDM; 12643733; -.
DR EPD; Q16799; -.
DR jPOST; Q16799; -.
DR MassIVE; Q16799; -.
DR MaxQB; Q16799; -.
DR PaxDb; Q16799; -.
DR PeptideAtlas; Q16799; -.
DR PRIDE; Q16799; -.
DR ProteomicsDB; 61074; -. [Q16799-1]
DR ProteomicsDB; 61075; -. [Q16799-2]
DR ProteomicsDB; 61076; -. [Q16799-3]
DR Antibodypedia; 3447; 509 antibodies from 26 providers.
DR DNASU; 6252; -.
DR Ensembl; ENST00000267484.10; ENSP00000267484.5; ENSG00000139970.18. [Q16799-1]
DR Ensembl; ENST00000342503.8; ENSP00000340716.4; ENSG00000139970.18. [Q16799-3]
DR GeneID; 6252; -.
DR KEGG; hsa:6252; -.
DR MANE-Select; ENST00000267484.10; ENSP00000267484.5; NM_021136.3; NP_066959.1.
DR UCSC; uc001xek.3; human. [Q16799-1]
DR CTD; 6252; -.
DR DisGeNET; 6252; -.
DR GeneCards; RTN1; -.
DR HGNC; HGNC:10467; RTN1.
DR HPA; ENSG00000139970; Tissue enhanced (brain, pituitary gland).
DR MIM; 600865; gene.
DR neXtProt; NX_Q16799; -.
DR OpenTargets; ENSG00000139970; -.
DR PharmGKB; PA34880; -.
DR VEuPathDB; HostDB:ENSG00000139970; -.
DR eggNOG; KOG1792; Eukaryota.
DR GeneTree; ENSGT00940000155077; -.
DR InParanoid; Q16799; -.
DR OMA; AFRIHNT; -.
DR OrthoDB; 244299at2759; -.
DR PhylomeDB; Q16799; -.
DR TreeFam; TF105431; -.
DR PathwayCommons; Q16799; -.
DR SignaLink; Q16799; -.
DR BioGRID-ORCS; 6252; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; RTN1; human.
DR GeneWiki; RTN1; -.
DR GenomeRNAi; 6252; -.
DR Pharos; Q16799; Tbio.
DR PRO; PR:Q16799; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q16799; protein.
DR Bgee; ENSG00000139970; Expressed in Brodmann (1909) area 23 and 179 other tissues.
DR ExpressionAtlas; Q16799; baseline and differential.
DR Genevisible; Q16799; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..776
FT /note="Reticulon-1"
FT /id="PRO_0000168158"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 589..776
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64548"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0T0"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0T0"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..568
FT /note="Missing (in isoform RTN1-C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7685762"
FT /id="VSP_005645"
FT VAR_SEQ 1..420
FT /note="Missing (in isoform RTN1-B)"
FT /evidence="ECO:0000303|PubMed:7685762"
FT /id="VSP_005644"
FT VAR_SEQ 569..588
FT /note="GPGPLGPGAPPPLLFLNKQK -> MQATADSTKMDCVWSNWKSQ (in
FT isoform RTN1-C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7685762"
FT /id="VSP_005646"
FT VARIANT 247
FT /note="G -> E (in dbSNP:rs35645652)"
FT /id="VAR_053630"
FT VARIANT 357
FT /note="I -> V (in dbSNP:rs35707243)"
FT /id="VAR_053631"
SQ SEQUENCE 776 AA; 83618 MW; CA5B6232353096FE CRC64;
MAAPGDPQDE LLPLAGPGSQ WLRHRGEGEN EAVTPKGATP APQAGEPSPG LGARAREAAS
REAGSGPARQ SPVAMETAST GVAGVSSAMD HTFSTTSKDG EGSCYTSLIS DICYPPQEDS
TYFTGILQKE NGHVTISESP EELGTPGPSL PDVPGIESRG LFSSDSGIEM TPAESTEVNK
ILADPLDQMK AEAYKYIDIT RPEEVKHQEQ HHPELEDKDL DFKNKDTDIS IKPEGVREPD
KPAPVEGKII KDHLLEESTF APYIDDLSEE QRRAPQITTP VKITLTEIEP SVETTTQEKT
PEKQDICLKP SPDTVPTVTV SEPEDDSPGS ITPPSSGTEP SAAESQGKGS ISEDELITAI
KEAKGLSYET AENPRPVGQL ADRPEVKARS GPPTIPSPLD HEASSAESGD SEIELVSEDP
MAAEDALPSG YVSFGHVGGP PPSPASPSIQ YSILREEREA ELDSELIIES CDASSASEES
PKREQDSPPM KPSALDAIRE ETGVRAEERA PSRRGLAEPG SFLDYPSTEP QPGPELPPGD
GALEPETPML PRKPEEDSSS NQSPAATKGP GPLGPGAPPP LLFLNKQKAI DLLYWRDIKQ
TGIVFGSFLL LLFSLTQFSV VSVVAYLALA ALSATISFRI YKSVLQAVQK TDEGHPFKAY
LELEITLSQE QIQKYTDCLQ FYVNSTLKEL RRLFLVQDLV DSLKFAVLMW LLTYVGALFN
GLTLLLMAVV SMFTLPVVYV KHQAQIDQYL GLVRTHINAV VAKIQAKIPG AKRHAE
