RTN1_RAT
ID RTN1_RAT Reviewed; 777 AA.
AC Q64548; Q64547;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Reticulon-1;
DE AltName: Full=Neuroendocrine-specific protein;
DE AltName: Full=S-rex;
GN Name=Rtn1; Synonyms=Nsp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RTN1-B AND RTN1-S).
RC STRAIN=Wistar; TISSUE=Brain cortex;
RX PubMed=8793864; DOI=10.1006/mcne.1996.0022;
RA Baka I.D., Ninkina N.N., Pinon L.G.P., Adu J., Davies A.M., Georgiev G.P.,
RA Buchman V.L.;
RT "Intracellular compartmentalization of two differentially spliced s-rex/NSP
RT mRNAs in neurons.";
RL Mol. Cell. Neurosci. 7:289-303(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-68; SER-210; SER-241;
RP SER-325; SER-348; SER-350 AND SER-485, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC blocking BACE1 activity. {ECO:0000250|UniProtKB:Q16799}.
CC -!- SUBUNIT: Interacts with NDRG1. Interacts with BACE1. Interacts with
CC TMEM33. {ECO:0000250|UniProtKB:Q16799}.
CC -!- SUBUNIT: [Isoform RTN1-S]: Interacts with UGCG; regulates the ceramide
CC glucosyltransferase activity of UGCG. {ECO:0000250|UniProtKB:Q16799}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q16799}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q16799};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RTN1-B; Synonyms=S-RexB;
CC IsoId=Q64548-1; Sequence=Displayed;
CC Name=RTN1-S; Synonyms=S-RexS;
CC IsoId=Q64548-2; Sequence=VSP_005647, VSP_005648;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in central and peripheral
CC nervous system of newborn and adult rats. Low levels have been also
CC detected in heart, adrenal gland and spleen. Expression of isoform
CC RTN1-B is restricted to particular neuronal types.
CC -!- DEVELOPMENTAL STAGE: Detected on embryonic day E10 in the hindbrain and
CC in E11 in the forebrain. During the next 3 embryonic days the levels of
CC RTN1-S increases and remains stable at E13 in the hindbrain and at E14
CC in the forebrain. The levels of RTN1-B does not change as significantly
CC during development of the hindbrain.
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DR EMBL; U17604; AAC53046.1; -; mRNA.
DR EMBL; U17603; AAC53045.1; -; mRNA.
DR RefSeq; NP_446317.1; NM_053865.1. [Q64548-1]
DR RefSeq; XP_008762912.1; XM_008764690.2. [Q64548-2]
DR AlphaFoldDB; Q64548; -.
DR SMR; Q64548; -.
DR BioGRID; 250529; 5.
DR CORUM; Q64548; -.
DR IntAct; Q64548; 1.
DR MINT; Q64548; -.
DR STRING; 10116.ENSRNOP00000064845; -.
DR iPTMnet; Q64548; -.
DR PhosphoSitePlus; Q64548; -.
DR SwissPalm; Q64548; -.
DR jPOST; Q64548; -.
DR PRIDE; Q64548; -.
DR Ensembl; ENSRNOT00000006373; ENSRNOP00000006373; ENSRNOG00000004794. [Q64548-2]
DR GeneID; 116644; -.
DR KEGG; rno:116644; -.
DR UCSC; RGD:620986; rat. [Q64548-1]
DR CTD; 6252; -.
DR RGD; 620986; Rtn1.
DR VEuPathDB; HostDB:ENSRNOG00000004794; -.
DR GeneTree; ENSGT00940000155077; -.
DR HOGENOM; CLU_048580_2_1_1; -.
DR InParanoid; Q64548; -.
DR OrthoDB; 244299at2759; -.
DR PhylomeDB; Q64548; -.
DR TreeFam; TF105431; -.
DR PRO; PR:Q64548; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004794; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; Q64548; baseline and differential.
DR Genevisible; Q64548; RN.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS: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..777
FT /note="Reticulon-1"
FT /id="PRO_0000168161"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 590..777
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..569
FT /note="Missing (in isoform RTN1-S)"
FT /evidence="ECO:0000303|PubMed:8793864"
FT /id="VSP_005647"
FT VAR_SEQ 570..589
FT /note="IPGPLGSDLVPPLPFFNKQK -> MQATADSTKMDCVWSNWKSQ (in
FT isoform RTN1-S)"
FT /evidence="ECO:0000303|PubMed:8793864"
FT /id="VSP_005648"
SQ SEQUENCE 777 AA; 83002 MW; AF7479C50F28D0AC CRC64;
MAAPPDLQDE PLSPANPGSQ LFGGRGEGEE ATPKGARPAQ QDGEPAWGSG AGAGVVSSRG
LCSGPARSPP VAMETASTGV AAVPDALDHS SSPTLKDGEG ACYTSLISDI CYPPREDSAY
FTGILQKENG HITTSESPEE LGTPGPSLPE VPGTEPHGLL SSDSGIEMTP AESTEVNKIL
ADPLDQMKAE ACKYIDITRP QEAKGQEEQS PGLEDKDLDF KDKDSEVSTK PEGVHAPNQP
SPVEGKLIKD NLFEESTFAP YIDELSDEQH RMSLVTAPVK ITLTEIGPPV MTATHETIPE
KQDLCLKPSP DTVPTVTVSE PEDDSPGSVT PPSSGTEPSA AESQGKGSVS EDELIAAIKE
AKGLSYETTE SPRPVGQAAD RPKVKARSGL PTIPSSLDQE ASSAESGDSE IELVSEDPMA
SEDALPSGYV SFGHVSGPPP SPASPSIQYS ILREEREAEL DSELIIESCD ASSASEESPK
REQDSPPMKP GVLDAIREET SSRATEERAP SHQGPVEPDP ILSFTPVTLQ SRPEPSSGDG
APVPEPPKSQ QQKPEEEAVS SSQSPAATEI PGPLGSDLVP PLPFFNKQKA IDLLYWRDIK
QTGIVFGSFL LLLFSLTQFS VVSVVAYLAL AALSATISFR IYKSVLQAVQ KTDEGHPFKA
YLELEITLSQ EQIQKYTDCL QLYVNSTLKE LRRLFLVQDL VDSLKFAVLM WLLTYVGALF
NGLTLLLMAV VSMFTLPVVY VKHQAQVDQY LGLVRTHINT VVAKIQAKIP GAKRHAE
