Full text data of RTN1
RTN1
(NSP)
[Confidence: low (only semi-automatic identification from reviews)]
Reticulon-1 (Neuroendocrine-specific protein)
Reticulon-1 (Neuroendocrine-specific protein)
UniProt
Q16799
ID RTN1_HUMAN Reviewed; 776 AA.
AC Q16799; Q16800; Q16801; Q5BKZ4; Q9BQ59;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
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.,
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 (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
RT project: 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.,
RA Schoenmakers E.F.P.M., 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 NDRG1.
RX PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
RA Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C.,
RA Watts G.F., Kremensky I., Kalaydjieva L.;
RT "NDRG1 interacts with APO A-I and A-II and is a functional candidate
RT for the HDL-C QTL on 8q24.";
RL Biochem. Biophys. Res. Commun. 332:982-992(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASS
RP SPECTROMETRY.
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 [8]
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).
CC -!- FUNCTION: May be involved in neuroendocrine secretion or in
CC membrane trafficking in neuroendocrine cells.
CC -!- SUBUNIT: Interacts with NDRG1.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
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
CC and cell cultures derived therefrom. Expression of isoform RTN1-C
CC is strongly correlated with neuronal differentiation.
CC -!- PTM: Isoforms RTN1-A and RTN1-B are phosphorylated.
CC -!- SIMILARITY: Contains 1 reticulon domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; A46583; A46583.
DR PIR; I60904; I60904.
DR RefSeq; NP_066959.1; NM_021136.2.
DR RefSeq; NP_996734.1; NM_206852.2.
DR UniGene; Hs.368626; -.
DR ProteinModelPortal; Q16799; -.
DR SMR; Q16799; 639-704.
DR IntAct; Q16799; 4.
DR MINT; MINT-154554; -.
DR STRING; 9606.ENSP00000267484; -.
DR PhosphoSite; Q16799; -.
DR DMDM; 12643733; -.
DR PaxDb; Q16799; -.
DR PRIDE; Q16799; -.
DR Ensembl; ENST00000267484; ENSP00000267484; ENSG00000139970.
DR Ensembl; ENST00000342503; ENSP00000340716; ENSG00000139970.
DR GeneID; 6252; -.
DR KEGG; hsa:6252; -.
DR UCSC; uc001xen.1; human.
DR CTD; 6252; -.
DR GeneCards; GC14M060062; -.
DR HGNC; HGNC:10467; RTN1.
DR HPA; CAB002745; -.
DR MIM; 600865; gene.
DR neXtProt; NX_Q16799; -.
DR PharmGKB; PA34880; -.
DR eggNOG; NOG306139; -.
DR HOGENOM; HOG000134444; -.
DR HOVERGEN; HBG008971; -.
DR InParanoid; Q16799; -.
DR OMA; GEGSCYT; -.
DR OrthoDB; EOG7CZK7J; -.
DR PhylomeDB; Q16799; -.
DR ChiTaRS; RTN1; human.
DR GeneWiki; RTN1; -.
DR GenomeRNAi; 6252; -.
DR NextBio; 24277; -.
DR PRO; PR:Q16799; -.
DR ArrayExpress; Q16799; -.
DR Bgee; Q16799; -.
DR CleanEx; HS_RTN1; -.
DR Genevestigator; Q16799; -.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; TAS:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; NAS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
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 Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 776 Reticulon-1.
FT /FTId=PRO_0000168158.
FT TRANSMEM 603 623 Helical; (Potential).
FT TRANSMEM 705 725 Helical; (Potential).
FT DOMAIN 589 776 Reticulon.
FT COMPBIAS 609 612 Poly-Leu.
FT MOD_RES 487 487 Phosphoserine.
FT VAR_SEQ 1 568 Missing (in isoform RTN1-C).
FT /FTId=VSP_005645.
FT VAR_SEQ 1 420 Missing (in isoform RTN1-B).
FT /FTId=VSP_005644.
FT VAR_SEQ 569 588 GPGPLGPGAPPPLLFLNKQK -> MQATADSTKMDCVWSNW
FT KSQ (in isoform RTN1-C).
FT /FTId=VSP_005646.
FT VARIANT 247 247 G -> E (in dbSNP:rs35645652).
FT /FTId=VAR_053630.
FT VARIANT 357 357 I -> V (in dbSNP:rs35707243).
FT /FTId=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
//
ID RTN1_HUMAN Reviewed; 776 AA.
AC Q16799; Q16800; Q16801; Q5BKZ4; Q9BQ59;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
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.,
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 (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
RT project: 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.,
RA Schoenmakers E.F.P.M., 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 NDRG1.
RX PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
RA Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C.,
RA Watts G.F., Kremensky I., Kalaydjieva L.;
RT "NDRG1 interacts with APO A-I and A-II and is a functional candidate
RT for the HDL-C QTL on 8q24.";
RL Biochem. Biophys. Res. Commun. 332:982-992(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASS
RP SPECTROMETRY.
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 [8]
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).
CC -!- FUNCTION: May be involved in neuroendocrine secretion or in
CC membrane trafficking in neuroendocrine cells.
CC -!- SUBUNIT: Interacts with NDRG1.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
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
CC and cell cultures derived therefrom. Expression of isoform RTN1-C
CC is strongly correlated with neuronal differentiation.
CC -!- PTM: Isoforms RTN1-A and RTN1-B are phosphorylated.
CC -!- SIMILARITY: Contains 1 reticulon domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; A46583; A46583.
DR PIR; I60904; I60904.
DR RefSeq; NP_066959.1; NM_021136.2.
DR RefSeq; NP_996734.1; NM_206852.2.
DR UniGene; Hs.368626; -.
DR ProteinModelPortal; Q16799; -.
DR SMR; Q16799; 639-704.
DR IntAct; Q16799; 4.
DR MINT; MINT-154554; -.
DR STRING; 9606.ENSP00000267484; -.
DR PhosphoSite; Q16799; -.
DR DMDM; 12643733; -.
DR PaxDb; Q16799; -.
DR PRIDE; Q16799; -.
DR Ensembl; ENST00000267484; ENSP00000267484; ENSG00000139970.
DR Ensembl; ENST00000342503; ENSP00000340716; ENSG00000139970.
DR GeneID; 6252; -.
DR KEGG; hsa:6252; -.
DR UCSC; uc001xen.1; human.
DR CTD; 6252; -.
DR GeneCards; GC14M060062; -.
DR HGNC; HGNC:10467; RTN1.
DR HPA; CAB002745; -.
DR MIM; 600865; gene.
DR neXtProt; NX_Q16799; -.
DR PharmGKB; PA34880; -.
DR eggNOG; NOG306139; -.
DR HOGENOM; HOG000134444; -.
DR HOVERGEN; HBG008971; -.
DR InParanoid; Q16799; -.
DR OMA; GEGSCYT; -.
DR OrthoDB; EOG7CZK7J; -.
DR PhylomeDB; Q16799; -.
DR ChiTaRS; RTN1; human.
DR GeneWiki; RTN1; -.
DR GenomeRNAi; 6252; -.
DR NextBio; 24277; -.
DR PRO; PR:Q16799; -.
DR ArrayExpress; Q16799; -.
DR Bgee; Q16799; -.
DR CleanEx; HS_RTN1; -.
DR Genevestigator; Q16799; -.
DR GO; GO:0030176; C:integral to endoplasmic reticulum membrane; TAS:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; NAS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
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 Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 776 Reticulon-1.
FT /FTId=PRO_0000168158.
FT TRANSMEM 603 623 Helical; (Potential).
FT TRANSMEM 705 725 Helical; (Potential).
FT DOMAIN 589 776 Reticulon.
FT COMPBIAS 609 612 Poly-Leu.
FT MOD_RES 487 487 Phosphoserine.
FT VAR_SEQ 1 568 Missing (in isoform RTN1-C).
FT /FTId=VSP_005645.
FT VAR_SEQ 1 420 Missing (in isoform RTN1-B).
FT /FTId=VSP_005644.
FT VAR_SEQ 569 588 GPGPLGPGAPPPLLFLNKQK -> MQATADSTKMDCVWSNW
FT KSQ (in isoform RTN1-C).
FT /FTId=VSP_005646.
FT VARIANT 247 247 G -> E (in dbSNP:rs35645652).
FT /FTId=VAR_053630.
FT VARIANT 357 357 I -> V (in dbSNP:rs35707243).
FT /FTId=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
//
MIM
600865
*RECORD*
*FIELD* NO
600865
*FIELD* TI
*600865 RETICULON 1; RTN1
;;NEUROENDOCRINE-SPECIFIC PROTEIN; NSP
*FIELD* TX
CLONING
read more
Roebroek et al. (1993) described the cloning of a gene, which they
designated NSP, that encodes several neuroendocrine-specific proteins.
The original cDNA was identified by screening an expression library of
the small-cell lung cancer (SCLC) NCI-H82 cell line with antibodies to
the previously identified proteins. The gene can produce 3 different
transcripts (3.4, 2.3, and 1.8 kb), which are identical at their 3-prime
ends but have unique amino termini. The common carboxyl-terminal region
contains 2 large hydrophobic domains. The largest cDNA (NSP-A) produces
a 135-kD (776-amino acid) protein which is rich in proline and serine
residues and contains multiple potential phosphorylation sites. NSP-B
and NSP-C have predicted reading frames of 356 and 208 amino acids,
respectively. The B transcript was found only in the NCI-H82 cell line.
NSP-specific antibodies showed that the proteins are localized to
membranes of the endoplasmic reticulum (Senden et al., 1994), leading to
their proposed designation as 'reticulons.' Immunohistochemical studies
in the rat (van de Velde et al., 1994) showed the presence of NSP-A
protein in many regions of the brain. NSP-A or -C transcripts were found
in 18 different SCLC lines but not in any of 11 nonendocrine non-SCLCs
(van de Velde et al., 1994).
GENE STRUCTURE
Roebroek et al. (1996) found that the NSP exons are dispersed over a
genomic region of about 275 kb. The genomic organization explained the
generation of NSP mRNA variants encoding NSP protein isoforms. Multiple
promoters rather than alternative splicing of internal exons seemed to
be involved in this diversity. Comparison of NSP genomic and cDNA
sequences with databank nucleotide sequences resulted in the discovery
of other human members of this novel family of reticulon encoding genes.
Mannan et al. (2006) noted that RTN1 has 9 exons spanning approximately
295 kb.
MAPPING
Kools et al. (1994) mapped the human NSP gene to chromosome 14q21-q22 by
fluorescence in situ hybridization. Mannan et al. (2006) stated that the
RTN1 gene maps to chromosome 14q23.1.
GENE FUNCTION
By yeast 2-hybrid analysis and coimmunoprecipitation studies in mouse
fibroblast cells (NIH3T3) and HeLa cells, Mannan et al. (2006)
demonstrated that reticulon-1 interacts with spastin (SPAST; 604277),
which is mutated in hereditary spastic paraplegia-4 (SPG4; 182601). The
interaction is mediated through the spastin N-terminal region, which
contains a microtubule-interacting and trafficking domain. Intracellular
distribution studies showed colocalization of the 2 proteins in discrete
cytoplasmic vesicles. The findings strengthened the hypothesis that
disruption of intracellular vesicular transport processes may underlie
spastic paraplegia. Mannan et al. (2006) failed to identify mutations in
the coding or flanking intronic sequences of the RTN1 gene in 2 index
patients from families with SPG15 (270700), which had been mapped to
chromosome 14q.
*FIELD* RF
1. Kools, P. F. J.; Roebroek, A. J. M.; van de Velde, H. J. K.; Marynen,
P.; Bullerdiek, J.; Van de Ven, W. J. M.: Regional mapping of the
human NSP gene to chromosome region 14q21-q22 by fluorescence in situ
hybridization analysis. Cytogenet. Cell Genet. 66: 48-50, 1994.
2. Mannan, A. U.; Boehm, J.; Sauter, S. M.; Rauber, A.; Byrne, P.
C.; Neesen, J.; Engel, W.: Spastin, the most commonly mutated protein
in hereditary spastic paraplegia interacts with reticulon 1 an endoplasmic
reticulum protein. Neurogenetics 7: 93-103, 2006.
3. Roebroek, A. J. M.; Ayoubi, T. A. Y.; van de Velde, H. J. K.; Schoenmakers,
E. F. P. M.; Pauli, I. G. L.; Van de Ven, W. J. M.: Genomic organization
of the human NSP gene, prototype of a novel gene family encoding reticulons. Genomics 32:
191-199, 1996.
4. Roebroek, A. J. M.; van de Velde, H. J. K.; Van Bokhoven, A.; Broers,
J. L. V.; Ramaekers, F. C. S.; Van de Ven, W. J. M.: Cloning and
expression of alternative transcripts of a novel neuroendocrine-specific
gene and identification of its 135-kDa translational product. J.
Biol. Chem. 268: 13439-13447, 1993.
5. Senden, N. H. M.; van de Velde, H. J. K.; Broers, J. L. V.; Timmer,
E. D. J.; Roebroek, A. J. M.; van de Ven, W. J. M.; Ramaekers, F.
C. S.: Cluster-10 lung-cancer antibodies recognize NSPs, novel neuro-endocrine
proteins associated with membranes of the endoplasmic reticulum. Int.
J. Cancer (Suppl.): 8:-84-88, 1994.
6. van de Velde, H. J. K.; Roebroek, A. J. M.; van Leeuwen, F. W.;
Van de Ven, W. J. M.: Molecular analysis of expression in rat brain
of NSP-A, a novel neuroendocrine-specific protein of the endoplasmic
reticulum. Molec. Brain Res. 23: 81-92, 1994.
7. van de Velde, H. J. K.; Senden, N. H. M.; Roskams, T. A. D.; Broers,
J. L. V.; Ramaekers, F. C. S.; Roebroek, A. J. M.; Van de Ven, W.
J. M.: NSP-encoded reticulons are neuroendocrine markers of a novel
category in human lung cancer diagnosis. Cancer Res. 54: 4769-4776,
1994.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/5/2006
*FIELD* CD
Alan F. Scott: 10/15/1995
*FIELD* ED
carol: 03/02/2012
terry: 3/10/2011
wwang: 3/2/2011
wwang: 9/7/2006
ckniffin: 9/5/2006
carol: 10/20/1999
alopez: 9/8/1998
terry: 4/17/1996
mark: 3/25/1996
terry: 3/14/1996
mark: 12/13/1995
terry: 10/30/1995
mark: 10/15/1995
*RECORD*
*FIELD* NO
600865
*FIELD* TI
*600865 RETICULON 1; RTN1
;;NEUROENDOCRINE-SPECIFIC PROTEIN; NSP
*FIELD* TX
CLONING
read more
Roebroek et al. (1993) described the cloning of a gene, which they
designated NSP, that encodes several neuroendocrine-specific proteins.
The original cDNA was identified by screening an expression library of
the small-cell lung cancer (SCLC) NCI-H82 cell line with antibodies to
the previously identified proteins. The gene can produce 3 different
transcripts (3.4, 2.3, and 1.8 kb), which are identical at their 3-prime
ends but have unique amino termini. The common carboxyl-terminal region
contains 2 large hydrophobic domains. The largest cDNA (NSP-A) produces
a 135-kD (776-amino acid) protein which is rich in proline and serine
residues and contains multiple potential phosphorylation sites. NSP-B
and NSP-C have predicted reading frames of 356 and 208 amino acids,
respectively. The B transcript was found only in the NCI-H82 cell line.
NSP-specific antibodies showed that the proteins are localized to
membranes of the endoplasmic reticulum (Senden et al., 1994), leading to
their proposed designation as 'reticulons.' Immunohistochemical studies
in the rat (van de Velde et al., 1994) showed the presence of NSP-A
protein in many regions of the brain. NSP-A or -C transcripts were found
in 18 different SCLC lines but not in any of 11 nonendocrine non-SCLCs
(van de Velde et al., 1994).
GENE STRUCTURE
Roebroek et al. (1996) found that the NSP exons are dispersed over a
genomic region of about 275 kb. The genomic organization explained the
generation of NSP mRNA variants encoding NSP protein isoforms. Multiple
promoters rather than alternative splicing of internal exons seemed to
be involved in this diversity. Comparison of NSP genomic and cDNA
sequences with databank nucleotide sequences resulted in the discovery
of other human members of this novel family of reticulon encoding genes.
Mannan et al. (2006) noted that RTN1 has 9 exons spanning approximately
295 kb.
MAPPING
Kools et al. (1994) mapped the human NSP gene to chromosome 14q21-q22 by
fluorescence in situ hybridization. Mannan et al. (2006) stated that the
RTN1 gene maps to chromosome 14q23.1.
GENE FUNCTION
By yeast 2-hybrid analysis and coimmunoprecipitation studies in mouse
fibroblast cells (NIH3T3) and HeLa cells, Mannan et al. (2006)
demonstrated that reticulon-1 interacts with spastin (SPAST; 604277),
which is mutated in hereditary spastic paraplegia-4 (SPG4; 182601). The
interaction is mediated through the spastin N-terminal region, which
contains a microtubule-interacting and trafficking domain. Intracellular
distribution studies showed colocalization of the 2 proteins in discrete
cytoplasmic vesicles. The findings strengthened the hypothesis that
disruption of intracellular vesicular transport processes may underlie
spastic paraplegia. Mannan et al. (2006) failed to identify mutations in
the coding or flanking intronic sequences of the RTN1 gene in 2 index
patients from families with SPG15 (270700), which had been mapped to
chromosome 14q.
*FIELD* RF
1. Kools, P. F. J.; Roebroek, A. J. M.; van de Velde, H. J. K.; Marynen,
P.; Bullerdiek, J.; Van de Ven, W. J. M.: Regional mapping of the
human NSP gene to chromosome region 14q21-q22 by fluorescence in situ
hybridization analysis. Cytogenet. Cell Genet. 66: 48-50, 1994.
2. Mannan, A. U.; Boehm, J.; Sauter, S. M.; Rauber, A.; Byrne, P.
C.; Neesen, J.; Engel, W.: Spastin, the most commonly mutated protein
in hereditary spastic paraplegia interacts with reticulon 1 an endoplasmic
reticulum protein. Neurogenetics 7: 93-103, 2006.
3. Roebroek, A. J. M.; Ayoubi, T. A. Y.; van de Velde, H. J. K.; Schoenmakers,
E. F. P. M.; Pauli, I. G. L.; Van de Ven, W. J. M.: Genomic organization
of the human NSP gene, prototype of a novel gene family encoding reticulons. Genomics 32:
191-199, 1996.
4. Roebroek, A. J. M.; van de Velde, H. J. K.; Van Bokhoven, A.; Broers,
J. L. V.; Ramaekers, F. C. S.; Van de Ven, W. J. M.: Cloning and
expression of alternative transcripts of a novel neuroendocrine-specific
gene and identification of its 135-kDa translational product. J.
Biol. Chem. 268: 13439-13447, 1993.
5. Senden, N. H. M.; van de Velde, H. J. K.; Broers, J. L. V.; Timmer,
E. D. J.; Roebroek, A. J. M.; van de Ven, W. J. M.; Ramaekers, F.
C. S.: Cluster-10 lung-cancer antibodies recognize NSPs, novel neuro-endocrine
proteins associated with membranes of the endoplasmic reticulum. Int.
J. Cancer (Suppl.): 8:-84-88, 1994.
6. van de Velde, H. J. K.; Roebroek, A. J. M.; van Leeuwen, F. W.;
Van de Ven, W. J. M.: Molecular analysis of expression in rat brain
of NSP-A, a novel neuroendocrine-specific protein of the endoplasmic
reticulum. Molec. Brain Res. 23: 81-92, 1994.
7. van de Velde, H. J. K.; Senden, N. H. M.; Roskams, T. A. D.; Broers,
J. L. V.; Ramaekers, F. C. S.; Roebroek, A. J. M.; Van de Ven, W.
J. M.: NSP-encoded reticulons are neuroendocrine markers of a novel
category in human lung cancer diagnosis. Cancer Res. 54: 4769-4776,
1994.
*FIELD* CN
Cassandra L. Kniffin - updated: 9/5/2006
*FIELD* CD
Alan F. Scott: 10/15/1995
*FIELD* ED
carol: 03/02/2012
terry: 3/10/2011
wwang: 3/2/2011
wwang: 9/7/2006
ckniffin: 9/5/2006
carol: 10/20/1999
alopez: 9/8/1998
terry: 4/17/1996
mark: 3/25/1996
terry: 3/14/1996
mark: 12/13/1995
terry: 10/30/1995
mark: 10/15/1995