RTN2_XENLA
ID RTN2_XENLA Reviewed; 321 AA.
AC Q4FZ76; Q4FZ77; Q5J6M9; Q5J6N0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Reticulon-2;
DE Short=xRTN2;
GN Name=rtn2 {ECO:0000312|EMBL:DAA05171.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS85779.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15765506; DOI=10.1002/dvdy.20327;
RA Park E.C., Shim S., Han J.-K.;
RT "Identification and expression of XRTN2 and XRTN3 during Xenopus
RT development.";
RL Dev. Dyn. 233:240-247(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI33258.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-228 (ISOFORM B).
RC TISSUE=Eye, and Tadpole {ECO:0000312|EMBL:AAI33258.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI33258.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-198 (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 190-321.
RC TISSUE=Tail bud {ECO:0000269|Ref.3};
RA Kohara Y., Shin-i T., Mochii M., Kitayama A., Terasaka C., Ueno N.;
RT "Expressed genes in X. laevis embryo.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA05171.1}
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:0000269|PubMed:15765506}; 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 {ECO:0000269|PubMed:15765506};
CC IsoId=Q4FZ76-1; Sequence=Displayed;
CC Name=C {ECO:0000269|PubMed:15765506, ECO:0000269|Ref.3};
CC IsoId=Q4FZ76-2; Sequence=VSP_052654, VSP_052655;
CC -!- TISSUE SPECIFICITY: Isoform B is expressed in the anterior structure at
CC the mid-neurula stage, localizing to the neural plate and eye anlagen
CC by the late neurula stage through till the early tail bud stage. In
CC stage 25 embryos, expressed in the head and neural tissues. Expression
CC is restricted to specific regions of the brain during the tadpole
CC stages. Isoform C is expressed in the paraxial mesoderm at the mid-
CC neurula stage, with expression shifting posteriorly as the neural fold
CC closes. At later stages, expressed in the myotome of the somite and in
CC specific regions of the brain. {ECO:0000269|PubMed:15765506}.
CC -!- DEVELOPMENTAL STAGE: Isoform B and isoform C are expressed zygotically
CC from the early neurula stage, with expression maintained until the
CC tadpole stage. {ECO:0000269|PubMed:15765506}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CD252970; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CD252970; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AY495962; AAS85778.1; -; mRNA.
DR EMBL; AY495963; AAS85779.1; -; mRNA.
DR EMBL; BC133257; AAI33258.1; -; mRNA.
DR EMBL; CD252970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BJ063888; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BJ082011; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK004977; DAA05171.1; -; mRNA.
DR EMBL; BK004978; DAA05172.1; -; mRNA.
DR RefSeq; NP_001089014.1; NM_001095545.2. [Q4FZ76-1]
DR AlphaFoldDB; Q4FZ76; -.
DR GeneID; 496400; -.
DR KEGG; xla:496400; -.
DR CTD; 496400; -.
DR Xenbase; XB-GENE-941650; rtn2.L.
DR OMA; ENTCELK; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 496400; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
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_0000316858"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 134..321
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..86
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|PubMed:15765506, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_052654"
FT VAR_SEQ 130..133
FT /note="VFRA -> MNKT (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15765506, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_052655"
FT CONFLICT 178
FT /note="S -> T (in Ref. 3; BJ063888)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="N -> D (in Ref. 2; CD252970)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> R (in Ref. 1; AAS85778/AAS85779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35715 MW; F6FE67D0C8CE5EC3 CRC64;
MGHVLSFTHC KDAPSTASST PDSCPLEGED DDTPVTEVDF WPLPSPHEPT FSYITIGSSA
PLSRPPVRAR RGLGQGRVHE APREETEEKE VKDVVNYVLL ENTCELKQIS PLQVQEEVVF
VAKPQPQVEV FRAVKDLLYW RDTLLSTGCL TGVTLSLLCL SQFSVISVFA YGCLIILSVT
LTLRLYTKLL HALKRGNGAN PFQYYLDTDL KLTTKQAEEI VARAFSLAST TLCTLRSLFL
VEELKDSLKF LVIVYLLTYV GAVFNGITVL LLCVIGAFTF PILYKQHQTQ VDHYVSLVSK
KVNAFRSKFQ GAAKKPPAKQ K