RTN2_XENTR
ID RTN2_XENTR Reviewed; 321 AA.
AC Q4FZ58; Q4FZ59;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Reticulon-2;
GN Name=rtn2 {ECO:0000312|EMBL:DAA05191.1}; ORFNames=TTpA029b01, TTpA048i08;
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}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 162-321.
RC TISSUE=Tadpole;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-260 (ISOFORM B).
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:DAA05191.1}
RP IDENTIFICATION (ISOFORMS B AND C).
RX PubMed=15858203; DOI=10.1093/molbev/msi158;
RA Diekmann H., Klinger M., Oertle T., Heinz D., Pogoda H.-M., Schwab M.E.,
RA Stuermer C.A.O.;
RT "Analysis of the reticulon gene family demonstrates the absence of the
RT neurite growth inhibitor Nogo-A in fish.";
RL Mol. Biol. Evol. 22:1635-1648(2005).
CC -!- FUNCTION: Inhibits amyloid precursor protein processing, probably by
CC blocking BACE1 activity (By similarity). Enhances trafficking of the
CC glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to
CC the cell surface (By similarity). Plays a role in the translocation of
CC SLC2A4/GLUT4 from intracellular membranes to the cell membrane which
CC facilitates the uptake of glucose into the cell (By similarity).
CC {ECO:0000250|UniProtKB:O70622, ECO:0000250|UniProtKB:O75298,
CC ECO:0000250|UniProtKB:Q6WN19}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q4FZ76}; Multi-pass membrane protein
CC {ECO:0000255}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6WN19}; Multi-pass
CC membrane protein {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:O70622}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:O70622}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O70622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=A {ECO:0000269|PubMed:15858203};
CC IsoId=Q4FZ58-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q4FZ58-2; Sequence=VSP_052656, VSP_052657;
CC -!- SEQUENCE CAUTION:
CC Sequence=CF264052; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CF264052; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX724945; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX734625; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CF264052; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK005002; DAA05190.1; -; mRNA.
DR EMBL; BK005003; DAA05191.1; -; mRNA.
DR RefSeq; NP_001107739.1; NM_001114267.2.
DR AlphaFoldDB; Q4FZ58; -.
DR STRING; 8364.ENSXETP00000060227; -.
DR GeneID; 100135745; -.
DR KEGG; xtr:100135745; -.
DR CTD; 6253; -.
DR Xenbase; XB-GENE-941644; rtn2.
DR eggNOG; KOG1792; Eukaryota.
DR InParanoid; Q4FZ58; -.
DR OrthoDB; 1011511at2759; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0014802; C:terminal cisterna; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0046324; P:regulation of glucose import; 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; Cell membrane; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Membrane; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT CHAIN 1..321
FT /note="Reticulon-2"
FT /id="PRO_0000316859"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 134..321
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052656"
FT VAR_SEQ 130..132
FT /note="VFR -> MNK (in isoform C)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_052657"
FT CONFLICT 229
FT /note="S -> F (in Ref. 1; BX734625)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="H -> P (in Ref. 1; BX734625)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="G -> V (in Ref. 1; BX724945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35678 MW; 2A33B182ED7D4DDA CRC64;
MGHVLSFTHC KDAPSTASST PDSCPPEGEE DDSPVTEVNF WPLPSPHEPT FSYITIGSTA
PLSRPPVRAR RGLGQSRVHA APREETEEKE VKDVVTYVLL EKTCQLKKLS PPHVQEEVVF
VAKPQPQLEV FRAVKDLLYW RDILLSAGCL TGVTLSLLCL SQFSVISVFA YGCLIILSVT
LTLRLYTKLL HALKRGNGAN PFQYYLDADL KLTTKQAEEI TARVLSLLST TICTLRSLFL
VEELKDSLKF LVIIYLLTYV GAVFNGITVL LLCVIGAFTF PILYKQHQTQ VDHYVSLVSK
KGNAFRSKIQ GTVKKPPAKQ K
