ID   A0A2K5E7E1_AOTNA        Unreviewed;       468 AA.
AC   A0A2K5E7E1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   28-JAN-2026, entry version 27.
DE   RecName: Full=Reticulon {ECO:0000256|RuleBase:RU210713};
GN   Name=RTN2 {ECO:0000313|Ensembl:ENSANAP00000029069.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000029069.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000029069.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSANAP00000029069.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU210713}.
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   AlphaFoldDB; A0A2K5E7E1; -.
DR   Ensembl; ENSANAT00000047096.1; ENSANAP00000029069.1; ENSANAG00000032309.1.
DR   GeneTree; ENSGT00940000160599; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
DR   GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
DR   GO; GO:0007420; P:brain development; IEA:TreeGrafter.
DR   GO; GO:0071787; P:endoplasmic reticulum tubular network formation; IEA:TreeGrafter.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:UniProtKB-ARBA.
DR   GO; GO:0030182; P:neuron differentiation; IEA:TreeGrafter.
DR   FunFam; 1.20.5.2480:FF:000001; Reticulon; 1.
DR   Gene3D; 1.20.5.2480; -; 1.
DR   InterPro; IPR003388; Reticulon.
DR   InterPro; IPR046964; RTN1-4.
DR   PANTHER; PTHR45799:SF3; RETICULON-2; 1.
DR   PANTHER; PTHR45799; RETICULON-LIKE PROTEIN; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU210713};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU210713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU210713};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU210713}.
FT   TRANSMEM        287..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU210713"
FT   TRANSMEM        386..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU210713"
FT   DOMAIN          268..468
FT                   /note="Reticulon"
FT                   /evidence="ECO:0000259|PROSITE:PS50845"
FT   REGION          1..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..163
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  50797 MW;  5E57ADE909E2DE11 CRC64;
     MGQVLPVFAH CKKQGSPSPA AGGNDDSDFR ELHTAREFSE DDEEETTSQD WGTPRELTFS
     YIAFDGVVGS GSRRDSTARR PRPQGRSVSE PRDQHPQPSL GDSLESIPSL SQSPEPGRRG
     DPDTAPPSER PLEDLRLRLD QLDWVAARGV GSGEDSSTSS STPLEDEEPE EPDGLEAGEA
     GEELDLRLRL AQPSPPEVLT PQLSPGSGTP QAETPSPSRS RDSNSGPEEP LLEEEEKQRG
     PLEREPIKGQ CLDSTGQSEF TVEPRLLVAD LLYWKDTRTS GVVFTGLMVS LLCLLHFSIV
     SVAAYVALLL LCGTISLRVY RKVLQAVHRG DGANPFQAYL DVDLTLTREQ TERLSQQIAS
     RVVSAATQLR HFFLVEDLVD SLKLALLFYI LTFVGAIFNG LTLLILGVIG LFTVPLLYRQ
     HQAQIDQYVG LVTNQLSHVK AKIRAKIPGT GALASAAAAV SGSKAKAE
//