RTN1_XENTR
ID RTN1_XENTR Reviewed; 764 AA.
AC A7MC64; Q0VFF6; Q6IFY6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Reticulon-1;
GN Name=rtn1 {ECO:0000312|EMBL:AAI18847.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAI52061.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI52061.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI52061.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 413-599 (ISOFORM A).
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:DAA02071.1}
RP IDENTIFICATION (ISOFORM A).
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).
CC -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC blocking BACE1 activity. {ECO:0000250|UniProtKB:Q16799}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5MY90}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q5MY90}. Note=Mainly
CC localized to the endoplasmic reticulum with some expression in the
CC nucleus and polysome fractions. {ECO:0000250|UniProtKB:Q5MY90}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=A7MC64-1; Sequence=Displayed;
CC Name=C;
CC IsoId=A7MC64-2; Sequence=VSP_052644, VSP_052645;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI18847.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI52061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AL635298; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=DAA02071.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC118846; AAI18847.1; ALT_INIT; mRNA.
DR EMBL; BC152060; AAI52061.1; ALT_INIT; mRNA.
DR EMBL; AL635298; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK004008; DAA02071.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001078819.2; NM_001085350.2. [A7MC64-1]
DR AlphaFoldDB; A7MC64; -.
DR SMR; A7MC64; -.
DR STRING; 8364.ENSXETP00000058548; -.
DR PaxDb; A7MC64; -.
DR PRIDE; A7MC64; -.
DR DNASU; 677736; -.
DR GeneID; 677736; -.
DR KEGG; xtr:677736; -.
DR CTD; 6252; -.
DR Xenbase; XB-GENE-1011333; rtn1.
DR eggNOG; KOG1792; Eukaryota.
DR HOGENOM; CLU_048580_2_1_1; -.
DR InParanoid; A7MC64; -.
DR OrthoDB; 244299at2759; -.
DR PhylomeDB; A7MC64; -.
DR Reactome; R-XTR-8849932; Synaptic adhesion-like molecules.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000016983; Expressed in central nervous system and 11 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..764
FT /note="Reticulon-1"
FT /id="PRO_0000315934"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 578..764
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..557
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052644"
FT VAR_SEQ 558..577
FT /note="VLGKTSTLPLKPLPFLSKRK -> MQASADSTRMECLWSNWKCQ (in
FT isoform C)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052645"
SQ SEQUENCE 764 AA; 84448 MW; 09373C83A307BBBF CRC64;
MAANPEVFSG RLEGNVAAAR RPGSAQEEEG EAAGGALSCV DQGRTIKAEQ AGHPTVAMEI
TSTDFTSTLH LHDAESKELP GDENGLSYTY LSSDKHSHTD STYFTGISKK GTESPDIKEF
SGVGPRSPKE IPTFDSRGLL SSDSGIEMTP AECSEVNKSL ADPTEEEKQE AYKYIDISRS
PDMKPQQVLD KDFGENKAST IGQAAPTEQQ AYDSVTMSWQ KDHYNGNISE YLPYVPYMEE
PRKDFGLYNS PTSKEPKSAP VTISFTGMET TLQTEYPENQ QGKSDKGLKL SPDMVPTVTV
SEPEDNSPES ITPPSTDADG YTEPSGLEEQ RKYKISEDEL ISAIKAKEGT KGFSSETNEE
KQSYSFNVEK QDFTVLPTRD APAPLDMEGS STESGDSEIE LVSEDQVGAE EAMQSAYMTF
SHIGGPPPSP ASPSIQYSIL REEREAELDS ELIIESCDGS SASEESPKRD QDSPMMKPMI
MDIIEEENLS RAESFDASDF ESCSLKERKL NMENLAESAC YLKGTYHTEI RADMPSTKKE
ELLPQKKSPE GSAYQSKVLG KTSTLPLKPL PFLSKRKAIE LLYWRDIKQT GIVFGSVLLM
LFSLTQFSVV SVIAYLALAA LSATISFRIY KSVLQAVQKT DEGHPFKSYL DMEISLSQEQ
IQKYTDCLQA YTNSIVKELR RLFLVQDLVD SLKFAVLMWL LTYVGALFNG LTLLIMAVVS
MFSLPVVYDK YQAQIDQYLG LVRTNMNTIV TKIQAKIPGT KQKE
